ࡱ>  NEFGHIJKLM  \p Administrator Ba==?'8X@"1Arial1Arial1Arial1Arial1Arial1<Arial @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @  @ @ , @ @ * @ @  @ @ + @ @ )@ @ X@ @  `*antiviral_protein"   DRAVPR_IDSequenceSequence_LengthNameSource Uniprot_IDGenePDB_IDTarget_OrganismActivityPredicted_structure_IDComment Modification Pubmed_IDAuthorTitle Connectives DRAVPR0001>MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW1Phospholipid scramblase 1(PL scramblase 1,PLSCR1)Homo sapiens (Human)O15162PLSCR11Y2A$HBV,HIV-1,HTLV1,IAV,EBV,HCMV,HCV,VSV[Ref.35650588]Hepatitis B virus(HBV):PLSCR1 plays an antiviral role by promoting the ubiquitination and proteasomal degradation of the HBV X protein (HBx), resulting in reduced HBx levels.##Human immunodeficiency virus type-1(HIV-1):PLSCR1 exhibits antiviral activity by inhibiting Tat functions by reducing its nuclear localization and perturbing the virus entry process by modulating CD4-SLPI interaction.##Human T-lymphotropic virus type 1 (HTLV-1):PLSCR1-Tax interaction reduced the cytoplasmic redistribution of Tax and its homodimerization, thus inhibiting Tax-mediated transactivation of HTLV-1 long terminal repeat.##Influenza A virus (IAV):PLSCR1 inhibits the nuclear import of NP/vRNP thus limiting viral replication.##Epstein-Barr virus (EBV): PLSCR1 represses BZLF1-dependent lytic gene expression.##Human cytomegalovirus (HCMV):PLSCR1 inhibits CREB functions and CREB-IE2, CBP-IE2 complexes, resulting in the repression of HCMV replication.##[Ref.15308695]Vesicular stomatitis virus (VSV):PLSCR1 inhibits accumulation of primary VSV transcripts, similar to the effects of IFN against VSV.##[Ref.21806988]Hepatitis C virus (HCV):PLSCR1 contributes to HCV entry and infection through HCVpp and HCVcc assays. AF-O15162-F1PLSCR1 may play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes.y`$Phosphorylation of Tyr at position 69,74,161a$The Cys at position 184,185,186,188 and 189 indicates S-palmitoyl cysteine.15308695##21806988##35650588$Dong B, Zhou Q, Zhao J, Zhou A, Harty RN, Bose S, Banerjee A, Slee R, Guenther J, Williams BR, Wiedmer T, Sims PJ, Silverman RH.##Gong Q, Cheng M, Chen H, Liu X, Si Y, Yang Y, Yuan Y, Jin C, Yang W, He F, Wang J.##Dal Col J, Lamberti MJ, Nigro A, Casolaro V, Fratta E, Steffan A, Montico B. Phospholipid scramblase 1 potentiates the antiviral activity of interferon.##Phospholipid scramblase 1 mediates hepatitis C virus entry into host cells.##Phospholipid scramblase 1: a protein with multiple functions via multiple molecular interactors.LAnti-HBV,Anti-HIV-1,Anti-HTLV1,Anti-IAV,Anti-EBV,Anti-HCMV,Anti-HCV,Anti-VSV DRAVPR0002MSCHNCSDPQVLCSSGQLFLQPLWDHLRSWEALLQSPFFPVIFSITTYVGFCLPFVVLDILCSWVPALRRYKIHPDFSPSAQQLLPCLGQTLYQHVMFVFPVTLLHWARSPALLPHEAPELLLLLHHILFCLLLFDMEFFVWHLLHHKVPWLYRTFHKVHHQNSSSFALATQYMSVWELFSLGFFDMMNVTLLGCHPLTTLTFHVVNIWLSVEDHSGYNFPWSTHRLVPFGWYGGVVHHDLHHSHFNCNFAPYFTHWDKILGTLRTASVPAR!Cholesterol 25-hydroxylase(h25OH)O95992CH25H NoneSARS-CoV-2,VSVg[Ref.33239446]SARS-CoV-2:The product of Cholesterol 25-hydroxylase, 25-hydroxycholesterol, activates the ER-localized enzyme ACAT to induce internalization of accessible cholesterol on the plasma membrane and restricts SARS-CoV-2 S protein-mediated fusion which inhibits virus replication.(inhibition of VSV-SARS-CoV-2 infection in MA104 cells(EC50=1.49 M)). AF-O95992-F125HC has been shown to have broad antiviral activity by inhibiting the host cell entry of human immunodeficiency virus (HIV), vesicular stomatitis virus (VSV), Zika virus (ZIKV), Ebola virus (EBOV), Nipah virus (NiV), Russian spring-summer encephalitis virus (RSSEV), porcine viruses (PEDV, PEGV, porcine intestine coronavirus), reovirus, and norovirus. For ZIKV, treatment with 25HC protected mice and rhesus monkeys from ZIKV infection.+Glycosylation of Asn at position 5,163,189.33239446##32944968hZang R, Case JB, Yutuc E, Ma X, Sh< en S, Gomez Castro MF, Liu Z, Zeng Q, Zhao H, Son J, Rothlauf PW, Kreutzberger AJB, Hou G, Zhang H, Bose S, Wang X, Vahey MD, Mani K, Griffiths WJ, Kirchhausen T, Fremont DH, Guo H, Diwan A, Wang Y, Diamond MS, Whelan SPJ, Ding S. ##Wang S, Li W, Hui H, Tiwari SK, Zhang Q, Croker BA, Rawlings S, Smith D, Carlin AF, Rana TM. Cholesterol 25-hydroxylase suppresses SARS-CoV-2 replication by blocking membrane fusion.##Cholesterol 25-Hydroxylase inhibits SARS-CoV-2 and other coronaviruses by depleting membrane cholesterol.Anti-SARS-CoV-2,Anti-VSV DRAVPR0003MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLAESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPSTLQAASTPQAEEDWTCTIL%2'-5'-oligoadenylate synthase 1(OAS1)P00973OAS14IG8 SARS-CoV-2[Ref.34581622]SARS-CoV-2:OAS1 recognizes short stretches of double-stranded RNA (dsRNA) and activates RNase L, which leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. AF-P00973-F1+When prenylated at C-terminal, acts as a double-stranded RNA (dsRNA) sensor specifically targeted to membranous replicative organelles in SARS coronavirus-2/SARS-CoV-2 infected cells where it binds to dsRNA structures in the SARS-CoV-2 5'-UTR and initiates a potent block to SARS-CoV-2 replication.<The Cys at position 397 indicates S-geranylgeranyl cysteine.34581622MWickenhagen A, Sugrue E, Lytras S, Kuchi S, Noerenberg M, Turnbull ML, Loney C, Herder V, Allan J, Jarmson I, Cameron-Ruiz N, Varjak M, Pinto RM, Lee JY, Iselin L, Palmalux N, Stewart DG, Swingler S, Greenwood EJD, Crozier TWM, Gu Q, Davies EL, Clohisey S, Wang B, Trindade Maranho Costa F, Freire Santana M, de Lima Ferreira LC, Murphy L, Fawkes A, Meynert A, Grimes G; ISARIC4C Investigators, Da Silva Filho JL, Marti M, Hughes J, Stanton RJ, Wang ECY, Ho A, Davis I, Jarrett RF, Castello A, Robertson DL, Semple MG, Openshaw PJM, Palmarini M, Lehner PJ, Baillie JK, Rihn SJ, Wilson SJ.<A prenylated dsRNA sensor protects against severe COVID-19.Anti-SARS-CoV-2 DRAVPR0004oMEHGLRSIPAWTLDKFIEDYLLPDTTFGADVKSAVNVVCDFLKERCFQGAAHPVRVSKVVKGGSSGKGTTLKGKSDADLVVFLNNLTSFEDQLNRRGEFIKEIKKQLYEVQHERRFRVKFEVQSSWWPNARSLSFKLSAPHLHQEVEFDVLPAFDVLGHVNTSSKPDPRIYAILIEECTSLGKDGEFSTCFTELQRNFLKQRPTKLKSLIRLVKHWYQLCKEKLGKPLPPQYALELLTVFAWEQGNGCYEFNTAQGFRTVLELVINYQHLRIYWTKYYDFQHQEVSKYLHRQLRKARPVILDPADPTGNVAGGNPEGWRRLAEEADVWLWYPCFIKKDGSRVSSWDVPTVVPVPFEQVEENWTCILL 2'-5'-oligoadenylate synthase 1AMus musculus (Mouse)P11928Oas1a AF-P11928-F1+Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L.<The Cys at position 364 indicates S-geranylgeranyl cysteine. DRAVPR0005(MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM9HLA class II histocompatibility antigen gamma chain(CD74)P04233CD74 X1A6A##1ICF##1IIE##1L3H##1MUJ##3PDO##3PGC##3PGD##3QXA##3QXD##4AEN##4AH2##4X5W##5KSU##5KSVEBOV,SARS-CoV-2[Ref.32855215]Ebola virus (EBOV):The p41 isoform of CD74 disrupts cathepsin-mediated Ebola glycoprotein processing, which prevents viral fusion and entry.##SARS-CoV-2: CD74 p41 can stymie the endosomal entry of coronaviruses including SARS-CoV-2. AF-P04233-F1nHas antiviral activity by stymieing the endosomal entry of Ebola virus and coronaviruses, including SARS-CoV-2`$Glycosylation of Asn at position 130,136,256.a$There are three disulfide bonds be< tween Cys213 and Cys232, Cys243 and Cys250, Cys252 and Cys271.b$Glycosylation of Thr at position 203.c$Glycosylation of Ser at position 281.32855215Bruchez A, Sha K, Johnson J, Chen L, Stefani C, McConnell H, Gaucherand L, Prins R, Matreyek KA, Hume AJ, Mhlberger E, Schmidt EV, Olinger GG, Stuart LM, Lacy-Hulbert A.eMHC class II transactivator CIITA induces cell resistance to Ebola virus and SARS-like coronaviruses.Anti-EBOV,Anti-SARS-CoV-2 DRAVPR0006jMRCLAPRPAGSYLSEPQGSSQCATMELGPLEGGYLELLNSDADPLCLYHFYDQMDLAGEEEIELYSEPDTDTINCDQFSRLLCDMEGDEETREAYANIAELDQYVFQDSQLEGLSKDIFKHIGPDEVIGESMEMPAEVGQKSQKRPFPEELPADLKHWKPAEPPTVVTGSLLVRPVSDCSTLPCLPLPALFNQEPASGQMRLEKTDQIPMPFSSSSLSCLNLPEGPIQFVPTISTLPHGLWQISEAGTGVSSIFIYHGEVPQASQVPPPSGFTVHGLPTSPDRPGSTSPFAPSATDLPSMPEPALTSRANMTEHKTSPTQCPAAGEVSNKLPKWPEPVEQFYRSLQDTYGAEPAGPDGILVEVDLVQARLERSSSKSLERELATPDWAERQLAQGGLAEVLLAAKEHRRPRETRVIAVLGKAGQGKSYWAGAVSRAWACGRLPQYDFVFSVPCHCLNRPGDAYGLQDLLFSLGPQPLVAADEVFSHILKRPDRVLLILDGFEELEAQDGFLHSTCGPAPAEPCSLRGLLAGLFQKKLLRGCTLLLTARPRGRLVQSLSKADALFELSGFSMEQAQAYVMRYFESSGMTEHQDRALTLLRDRPLLLSHSHSPTLCRAVCQLSEALLELGEDAKLPSTLTGLYVGLLGRAALDSPPGALAELAKLAWELGRRHQSTLQEDQFPSADVRTWAMAKGLVQHPPRAAESELAFPSFLLQCFLGALWLALSGEIKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLIFQPPARCLGALLGPSAAASVDRKQKVLARYLKRLQPGTLRARQLLELLHCAHEAEEAGIWQHVVQELPGRLSFLGTRLTPPDAHVLGKALEAAGQDFSLDLRSTGICPSGLGSLVGLSCVTRFRAALSDTVALWESLQQHGETKLLQAAEEKFTIEPFKAKSLKDVEDLGKLVQTQRTRSSSEDTAGELPAVRDLKKLEFALGPVSGPQAFPKLVRILTAFSSLQHLDLDALSENKIGDEGVSQLSATFPQLKSLETLNLSQNNITDLGAYKLAEALPSLAASLLRLSLYNNCICDVGAESLARVLPDMVSLRVMDVQYNKFTAAGAQQLAASLRRCPHVETLAMWTPTIPFSVQEHLQQQDSRISLRMHC class II transactivatorP33076CIITA AF-P33076-F1Has antiviral activity against Ebola virus and coronaviruses, including SARS-CoV-2. Induces resistance by up-regulation of the p41 isoform of CD74, which blocks cathepsin-mediated cleavage of viral glycoproteins, thereby preventing viral fusion!No modifications on the sequence. DRAVPR0007MPPRSLSNLSFPTEANESELVPEVWEKDFLPDSDGTTAELVIRCVIPSLYLIIISVGLLGNIMLVKIFLTNSAMRNVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWVFGKLGCKLIPAIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGVLLWTSLKAVGIWVVSVLLAVPEAVFSEVARIGSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLVIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFVFCWFPNHVLYLYRSFNYKEIDPSLGHMIVTLVARVLSFSNSCVNPFALYLLSESFRKHFNSQLCCGRKSYPERSTSYLLSSSAVRMTSLKSNTKNVVTNSVLLNGHSTKQEIALNeuromedin-B receptor(NMB-R)O54799NmbrIAV[Ref.31601264]Influenza virus strain A/Puerto Rico/8/1934 (H1N1):Neuromedin-B receptor plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6. AF-O54799-F1The NMB/NMBR system appeared to increase IFN- expression and decrease IL-6 expression after PR8 infection, which may serve to establish an antiviral state in the host.`$Glycosylation of Asn at position 8, 16, 192.a$The Cys at position 341 indicates S-palmitoyl cysteine.b$Phosphorylation of Ser at position 352.c$There is a disulfide bond between cys116 and Cys198.316012647Yang G, Huang H, Tang M, Cai Z, Huang C, Qi B, Chen JL.~Role of neuromedin B and its receptor in the innate immune responses against influenza A virus infection in vitro and in vivo.Anti-IAV DRAVPR0008yMARRAGGARMFGSLLLFALLAAGVAPLSWDLPEPRSRASKIRVHSRGNLWATGHFMGKKSLEPSSPSPLGTAPHTSLRDQRLQLSHDLLGILLLKKALGVSLSRPAPQIQYRRLLVQILQK Neuromedin-BP08949NMB 1C98##1C9A[Ref.31601264]Influenza virus strain A/Puerto Rico/8/1934 (H1N1): NMR up-regulated in response to infection with influenza A virus. AF-P08949-F1It is likely that NMB plays an anti-inflammatory role via the regulation of the host type I IFN signalling pathway. The NMB/NMBR system appeared to increase IFN- expression and decrease IL-6 expression after PR8 infection, which may serve to establish an antiviral state in the host.$The Met at position 56 is amidation. DRAVPR0009yMTRQAGSSWLLRGLLLFALFASGVAPFNWDLPEPRSRASKIRVHPRGNLWATGHFMGKKSLEPPSLSLVGTAPPNTPRDQRLQLSHDLLRILLRKKALGMNFSGPAPPIQYRRLLEPLLQKQ9CR53Nmb AF-Q9CR53-F1 DRAVPR0010MPSKSLSNLSVTTGANESGSVPEGWERDFLPASDGTTTELVIRCVIPSLYLLIITVGLLGNIMLVKIFITNSAMRSVPNIFISNLAAGDLLLLLTCVPVDASRYF< FDEWMFGKVGCKLIPVIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGALLRTCVKAMGIWVVSVLLAVPEAVFSEVARISSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLAIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFIFCWFPNHILYMYRSFNYNEIDPSLGHMIVTLVARVLSFGNSCVNPFALYLLSESFRRHFNSQLCCGRKSYQERGTSYLLSSSAVRMTSLKSNAKNMVTNSVLLNGHSMKQEMALNeuromedin-B receptorP28336NMBR:No predicted structure information available for the entry DRAVPR0011MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS#Ubiquitin-like protein ISG15(ISG15)P05161ISG15Y1Z2M## 2HJ8##3PHX##3PSE##3R66##3RT3##3SDL##5TL6##5W8T##5W8U##6BI8##6FFA##6XA9##7RBS##7S6PHIV-1,EBOV,IAV[Ref.16434471]Human immunodeficiency virus type-1(HIV-1):inhibits the ubiquitination of HIV-1-encoded Gag polypeptide and Tsg101 and the interaction of Tsg101, a central component of ESCRT-1 with the p6 domain of the Gag polyprotein, thereby preventing assembly and release of virions from infected cells.##[Ref.18305167]Ebola virus(EBOV):inhibits Ebola virus budding mediated by the VP40 protein by disrupting ubiquitin ligase activity of NEDD4 and its ability to ubiquitinate VP40.##[Ref.20133869]Influenza A virus(IAV):ISG15 modification of K41 of the NS1A protein inhibits influenza A virus replication and thus contributes to the antiviral action of IFN-. AF-P05161-F1YISG15 may affect replication not only of HIV-1, but also of a broad group of RNA viruses.2The Cys at position78 indicates S-nitrosocysteine.16434471##18305167##20133869mOkumura A, Lu G, Pitha-Rowe I, Pitha PM.##Okumura A, Pitha PM, Harty RN.##Zhao C, Hsiang TY, Kuo RL, Krug RM.(Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15.##ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity.##ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells.Anti-HIV-1,Anti-EBOV,Anti-IAV DRAVPR0012MAGSREVVAMDCEMVGLGPHRESGLARCSLVNVHGAVLYDKFIRPEGEITDYRTRVSGVTPQHMVGATPFAVARLEILQLLKGKLVVGHDLKHDFQALKEDMSGYTIYDTSTDRLLWREAKLDHCRRVSLRVLSERLLHKSIQNSLLGHSSVEDARATMELYQISQRIRARRGLPRLAVSD0Interferon-stimulated gene 20 kDa protein(ISG20)Q96AZ6ISG201WLJ HCV,HAV,YFV[Ref.21036379]Hepatitis C virus (HCV):ISG20 inhibits HCV RNA replication and progeny virus release in Huh7.5 cells that lack both RIG-I and TLR3 viral RNA sensing pathways which recognize HCV replication and trigger IFN antiviral responses.##ISG20 against HCV, HAV(hepatitis A virus), BVDV(bovine viral diarrhea virus) and YFV(yellow fever virus) all require the exonuclease activity of ISG20. AF-Q96AZ6-F1vISG20 is an interferon-inducible 32  52 exonuclease that inhibits replication of several human and animal RNA viruses. 21036379##12594219Zhou Z, Wang N, Woodson SE, Dong Q, Wang J, Liang Y, Rijnbrand R, Wei L, Nichols JE, Guo JT, Holbrook MR, Lemon SM, Li K.##Espert L, Degols G, Gongora C, Blondel D, Williams BR, Silverman RH, Mechti N.Antiviral activities of ISG20 in positive-strand RNA virus infections.##ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses.Anti-HCV,Anti-HAV,Anti-YFV DRAVPR0013MRQKAVSLFLCYLLLFTCSGVEAGKKKCSESSDSGSGFWKALTFMAVGGGLAVAGLPALGFTGAGIAANSVAASLMSWSAILNGGGVPAGGLVATLQSLGAGGSSVVIGNIGALMGYATHKYLDSEEDEE*Interferon alpha-inducible protein 6(IFI6)P09912IFI6 HCV[Ref.25757571]Hepatitis C virus (HCV):IFI6 inhibits HCV entry by disrupting EGFR activation and HRas/Raf-1 signaling and downstream CD81-CLDN1 interactions in response to HCV infection or CD81 crosslinking. AF-P09912-F1IFI6 was one of a number of ISGs shown to inhibit yellow fever virus (YFV) infection in STAT1-deficient human.IFI6 suggests a block at a subsequent step in DENV replication.257575715Meyer K, Kwon YC, Liu S, Hagedorn CH, Ray RB, Ray R. jInterferon- inducible protein 6 impairs EGFR activation by CD81 and inhibits hepatitis C virus infection.Anti-HCV DRAVPR0014zMEASALTSSAVTSVAKVVRVASGSAVVLPLARIATVVIGGVVAMAAVPM< VLSAMGFTAAGIASSSIAAKMMSAAAIANGGGVASGSLVATLQSLGATGLSGLTKFILGSIGSAIAAVIARFY-Interferon alpha-inducible protein 27(ISG12a)P40305IFI27[Ref.27194766]Hepatitis C virus (HCV):ISG12a mediates NS5A degradation via a ubiquitination-dependent proteasomal pathway, which is a multifunctional protein is indispensable for HCV replication and virus production. AF-P40305-F1ISG12a relies on the E3 ligase domain of SKP2 to restrict viral infection.The antiviral effects of ISG12a/IFI27 on HCV, NDV, WNV, and mouse hepatitis virus (MHV) infection in vitro or in vivo have been determined.27194766##27777077Xue B, Yang D, Wang J, Xu Y, Wang X, Qin Y, Tian R, Chen S, Xie Q, Liu N, Zhu H.##Chen Y, Jiao B, Yao M, Shi X, Zheng Z, Li S, Chen L.ISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-Dependent Degradation Pathway.##ISG12a inhibits HCV replication and potentiates the anti-HCV activity of IFN- through activation of the Jak/STAT signaling pathway independent of autophagy and apoptosis. DRAVPR0015]MELRHTPARDLDKFIEDHLLPNTCFRTQVKEAIDIVCRFLKERCFQGTADPVRVSKVVKGGSSGKGTTLRGRSDADLVVFLTKLTSFEDQLRRRGEFIQEIRRQLEACQREQKFKVTFEVQSPRRENPRALSFVLSSPQLQQEVEFDVLPAFDALGQWTPGYKPNPEIYVQLIKECKSRGKEGEFSTCFTELQRDFLRNRPTKLKSLIRLVKHWYQTCKKTHGNKLPPQYALELLTVYAWEQGSRKTDFSTAQGFQTVLELVLKHQKLCIFWEAYYDFTNPVVGRCMLQQLKKPRPVILDPADPTGNVGGGDTHSWQRLAQEARVWLGYPCCKNLDGSLVGAWTMLQKI(2'-5'-oligoadenylate synthase 1(p42 OAS)Sus scrofa (Pig)Q295991PX5##4RWN##4RWO##4RWP##4RWQVSV,HSV-2,EMCV[Ref.20844035]encephalomyocarditis virus (EMCV):inhibition of the cytopathic effect in HepG2 cells(EC50=24.5 g/ml);inhibition of the cytopathic effect in Vero cells(EC50=18.5 g/ml). AF-Q29599-F1wThe OAS family of proteins mediates antiviral activity via the synthesis of 2-5A and subsequent activation of RNase L. 20844035Kristiansen H, Scherer CA, McVean M, Iadonato SP, Vends S, Thavachelvam K, Steffensen TB, Horan KA, Kuri T, Weber F, Paludan SR, Hartmann R. Extracellular 2'-5' oligoadenylate synthetase stimulates RNase L-independent antiviral activity: a novel mechanism of virus-induced innate immunity.Anti-VSV,Anti-HSV-2,EMCV DRAVPR0016MAWRYSQLLLVPVQLVFLASVCCPGVWGSTVSEELHRMVGQSLSVQCQYKPKEESYVLKTWCRQTAPSKCTRVVTTSEPRKAARELQHTIWDDPEAGFFNITMTQLTEDDSAFYWCGPYYPSLREVTVLRNISLVVSPAPSTLPSQTIAPLPESTATIFMPFPVLTTSPEETTDSSINGTGHRNQSSSSPGWTSPGLLVSVQYGLLLLKALMLSVFCVLLCWRSGQGREYMAETMELSKLPHISKSLDTVSHISGYEKKANWY%Trem-like transcript 4 protein(TLT-4)Q3LRV9Treml4[Ref.25848864]TREML4 plays an important role in the regulation of TLR7 signaling and that its expression in vivo is required for antiviral host defense to influenza and for promotion of TLR7-mediated autoimmune disease. AF-Q3LRV9-F1No comments found in the entryZ`$Glycosylation of Asn at position 100.a$There is a disulfide bond between Cys47 and Cys116.25848864Ramirez-Ortiz ZG, Prasad A, Griffith JW, Pendergraft WF 3rd, Cowley GS, Root DE, Tai M, Luster AD, El Khoury J, Hacohen N, Means TK. bThe receptor TREML4 amplifies TLR7-mediated signaling during antiviral responses and autoimmunity. DRAVPR00176MKMKVLEVVGLAISIWLMLTPPASSNIVFDVENATPETYSNFLTSLREAVKDKKLTCHGMIMATTLTEQPKYVLVDLKFGSGTFTLAIRRGNLYLEGYSDIYNGKCRYRIFKDSESDAQETVCPGDKSKPGTQNNIPYEKSYKGMESKGGARTKLGLGKITLKSRMGKIYGKDATDQKQYQKNEAEFLLIAVQMVTEASRFKYIENKVKAKFDDANGYQPDPKAISLEKNWDSVSKVIAKVGTSGDSTVTLPGDLKDENNKPWTTATMNDLKNDIMALLTHVTCKVKSSMFPEIMSYYYRTSISNLGEFEAntiviral protein II/III>Phytolacca americana (American pokeweed) (Phytolacca decandra)Q40772PAP21LLN HIV-1,TMV$[Ref.10403789]Human immunodeficiency virus (HIV)-1:inhibition the replication of HIV-1 in human peripheral blood mononuclear cells(PAP-II:IC50=25 nM;PAP-III:IC50=16 nM);##tobacco mosaic virus(TMV):PAP-II and PAP-III cause concentration-dependent depurination of genomic RNA purified from TMV. AF-Q40772-F1The potent antiviral activity of PAP may in part be due to its unique ability to extensively depurinate viral RNA. The protein has 2 forms, PAP-II and PAP-III, which differ in their seasonal expression.JThere are two disulfide bonds between Cys57 and Cys284, Cys106 and Cys123.104037892Rajamohan F, < Venkatachalam TK, Irvin JD, Uckun FM.wPokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1. Anti-HIV-1,Anti-TMV DRAVPR00189MKSMLVVTISIWLILAPTSTWAVNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVGGSCQTTYNQNAMFPQLIMSTYYNYMVNLGDLFEGFAntiviral protein IP10297PAP1#1D6A## 1PAF##1PAG##1QCG##1QCI##1QCJ(No specific virus mentioned in the entry[Ref.10403789]Human immunodeficiency virus (HIV)-1:inhibition the replication of HIV-1 in human peripheral blood mononuclear cells(IC50=17 nM);##tobacco mosaic virus(TMV):PAP-I cause concentration-dependent depurination of genomic RNA purified from TMV. AF-P10297-F1rThe potent antiviral activity of PAP may in part be due to its unique ability to extensively depurinate viral RNA.JThere are two disulfide bonds between Cys56 and Cys281, Cys107 and Cys128. DRAVPR0019KMTSPHFSSYDEGPLDVSMAATNLENQLHSAQKNLLFLQREHASTLKGLHSEIRRLQQHCTDLTYELTVKSSEQTGDGTSKSSELKKRCEELEAQLKVKENENAELLKELEQKNAMITVLENTIKEREKKYLEELKAKSHKLTLLSSELEQRASTIAYLTSQLHAAKKKLMSSSGTSDASPSGSPVLASYKPAPPKDKLPETPRRRMKKSLSAPLHPEFEEVYRFGAESRKLLLREPVDAMPDPTPFLLARESAEVHLIKERPLVIPPIASDRSGEQHSPAREKPHKAHVGVAHRIHHATPPQAQPEVKTLAVDQVNGGKVVRKHSGTDRTV(Coiled-coil domain-containing protein 92Q53HC0CCDC92EBOV[Ref.32528005]Ebola virus(EBOV):CCDC92 can inhibit viral transcription and the formation of complete virions via an interaction with the viral protein NP. AF-Q53HC0-F1CCDC92 clearly inhibits viral transcription, which is mediated through the C-terminal coiled-coil domain of CCDC92 (aa 81 151) that is necessary for the interaction with NP.'Phosphorylation of Ser at position 209.32528005hKuroda M, Halfmann PJ, Hill-Batorski L, Ozawa M, Lopes TJS, Neumann G, Schoggins JW, Rice CM, Kawaoka Y.SIdentification of interferon-stimulated genes that attenuate Ebola virus infection. Anti-EBOV DRAVPR0020xMEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG)Inactive 2'-5'-oligoadenylate synthase 1BQ60856Oas1bWNV[Ref.16371364]West Nile virus(WNV):Oas1b inhibits the replication of WNV by preventing viral RNA accumulation inside infected cells. AF-Q60856-F1Oas1b-dependent antiviral activity is restricted to the early stages of WNV replication,the Oas1b-mediated inhibition of viral protein synthesis and the subsequent suppression of viral growth are due to a lack of accumulation of viral RNA inside cells.16371364LKajaste-Rudnitski A, Mashimo T, Frenkiel MP, Gunet JL, Lucas M, Desprs P. sThe 2',5'-oligoadenylate synthetase 1b is a potent inhibitor of West Nile virus replication inside infected cells. Anti-WNV DRAVPR0021MARLCAFLMILIVMSYWSTCSLGCDLPHTYNLRNKRALKVLAQMRRLTPLSCLKDRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNATLLDSFCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLREKKHSPCAWEVVRAEVWRALSSSANVLGRLREEKAInterferon alpha-11(Limitin)Q61716Ifna11[Ref.22912583]IFN-11-mediated activation of NK cells enabled cytolytic killing of FV-infected target cells via the exocytosis pathway. AF-Q61716-F1RIFN-11 significantly reduced viral loads during Friend retrovirus infection (FV).p`$Glycosylation of Asn at position 101.a$There are two disulfide bonds between Cys24 and Cys122, Cys52 and Cys162.22912583aGibbert K, Joedicke JJ, Meryk A, Trilling M, Francois S, Duppach J, Kraft A, Lang KS, Dittmer U. [Interferon-alpha subtype 11 activates NK cells and enables control of retroviral infection. DRAVPR0022MSLFPSLPLLLLSMVAASYSETVTCEDAQKTCPAVIACSSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVA< TPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI Mannose-binding protein C(MBP-C)P11226MBL2 1HUPd[Ref.35102342]SARS-CoV-2:MBL bound trimeric spike protein and then activated the lectin pathway of complement activation, which leads to the inhibition SARS-CoV-2 infection and a reduction of the induced inflammatory response.(Spike-mediated viral entry was inhibited by 90% at the concentration of 10 g/ml(34 nM) in 293T cells, EC50= 0.5 g/ml (1.7 nM)). AF-P11226-F1MBL was found to interact with spike protein and have antiviral activity with an EC50 of approximately 0.08 g ml 1 (0.27 nM) and an affinity of 34 nM.}`$Hydroxylation of Pro at position 47,73,79,82,88.a$There are two disulfide bonds between Cys155 and Cys244, Cys222 and Cys236.35102342SStravalaci M, Pagani I, Paraboschi EM, Pedotti M, Doni A, Scavello F, Mapelli SN, Sironi M, Perucchini C, Varani L, Matkovic M, Cavalli A, Cesana D, Gallina P, Pedemonte N, Capurro V, Clementi N, Mancini N, Invernizzi P, Bayarri-Olmos R, Garred P, Rappuoli R, Duga S, Bottazzi B, Uguccioni M, Asselta R, Vicenzi E, Mantovani A, Garlanda C.cRecognition and inhibition of SARS-CoV-2 by humoral innate immunity pattern recognition molecules. DRAVPR0023}MHKEEHEVAVLGPPPSTILPRSTVINIHSETSVPDHVVWSLFNTLFLNWCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTIGFILLLVFGSVTVYHIMLQIIQEKRGY2Interferon-induced transmembrane protein 1(IFITM1)P13164IFITM1HCV,SARS-CoV-2C[Ref.26354436]Hepatitis C Virus(HCV):IFITM1 to be able to limit HCV infection at the level of HCV entry through an interaction with the essential entry co-receptor CD81.##[Ref.33270927]SARS-CoV-2:IFITM1 likely restrict SARS CoV 2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes. AF-P13164-F1WIFITM1, IFITM2, and IFITM3 primarily act on the early stages of HCV infection.Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV).d`$Phosphorylation of Ser at position 16.a$The Cys at position 50,51,84 indicates S-palmitoyl cysteine.26354436##33270927##33051876~Narayana SK, Helbig KJ, McCartney EM, Eyre NS, Bull RA, Eltahla A, Lloyd AR, Beard MR.##Shi G, Kenney AD, Kudryashova E, Zani A, Zhang L, Lai KK, Hall-Stoodley L, Robinson RT, Kudryashov DS, Compton AA, Yount JS.##Buchrieser J, Dufloo J, Hubert M, Monel B, Planas D, Rajah MM, Planchais C, Porrot F, Guivel-Benhassine F, Van der Werf S, Casartelli N, Mouquet H, Bruel T, Schwartz O.The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3 Inhibit Hepatitis C Virus Entry.##Opposing activities of IFITM proteins in SARS-CoV-2 infection. ##Syncytia formation by SARS-CoV-2-infected cells. Anti-HCV,Anti-SARS-CoV-2 DRAVPR0024MNHIVQTFSPVNSGQPPNYEMLKEEQEVAMLGVPHNPAPPMSTVIHIRSETSVPDHVVWSLFNTLFMNTCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGIFMTILLIIIPVLVVQAQR2Interferon-induced transmembrane protein 2(IFITM2)Q01629IFITM2j[Ref.26354436]Hepatitis C Virus(HCV):inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome.##[Ref.33270927]SARS-CoV-2:IFITM2 likely restrict SARS CoV 2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes. AF-Q01629-F1xIFITM1, IFITM2, and IFITM3 primarily act on the early stages of HCV infection.Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV)e`$Phosphorylation of Ser at position 19.a$The Cys at position 70,71,104 indicates S-palmitoyl cysteine.26354436##33270927Narayana SK, Helbig KJ, McCartney EM, Eyre NS, Bull RA, Eltahla A, Lloyd AR, Beard MR.##Shi G, Kenney AD, Kudryashov< a E, Zani A, Zhang L, Lai KK, Hall-Stoodley L, Robinson RT, Kudryashov DS, Compton AA, Yount JS.The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3 Inhibit Hepatitis C Virus Entry.##Opposing activities of IFITM proteins in SARS-CoV-2 infection. DRAVPR0025MNHTVQTFFSPVNSGQPPNYEMLKEEHEVAVLGAPHNPAPPTSTVIHIRSETSVPDHVVWSLFNTLFMNPCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTILLIVIPVLIFQAYG2Interferon-induced transmembrane protein 3(IFITM3)Q01628IFITM3 j[Ref.26354436]Hepatitis C Virus(HCV):inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome.##[Ref.33270927]SARS-CoV-2:IFITM3 likely restrict SARS CoV 2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes. AF-Q01628-F1IFITM1, IFITM2, and IFITM3 primarily act on the early stages of HCV infection.IFITM3 exhibits both anti and pro viral effects against SARS-CoV-2, inhibiting endocytic entry of the virus while also enhancing virus fusion at the plasma membrane.Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) e`$Phosphorylation of Ser at position 20.a$The Cys at position 71,72,105 indicates S-palmitoyl cysteine. DRAVPR0026"MAISKKSSLFLPIFTFITMFLMVVNKVSSSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDANVIRNSTTIDFNAAYNADTIVAVELDTYPNTDIGDPNYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNEIPDIATVVConcanavalin-A4Canavalia gladiata (Sword bean) (Dolichos gladiatus)P14894N/A1WUV##2D7F##2EF6##2OVU##2P2KHIV-1j[Ref.15935326]Human immunodeficiency virus type-1(HIV-1):Inhibits HIV-1 reverse transcriptase.(IC50=35 M) AF-P14894-F1HThe mechanism of anti-HIV-1 activity may be protein protein interaction.%Glycosylation of Asn at position 152.15935326Wong JH, Ng TB. tIsolation and characterization of a glucose/mannose/rhamnose-specific lectin from the knife bean Canavalia gladiata. Anti-HIV-1 DRAVPR0027MEASPASGPRHLMDPHIFTSNFNNGIGRHKTYLCYEVERLDNGTSVKMDQHRGFLHNQAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFKHCWDTFVDHQGCPFQPWDGLDEHSQALSGRLRAILQNQGN#DNA dC->dU-editing enzyme APOBEC-3AP31941APOBEC3A(2M65##4XXO##5KEG##5SWW##7D3V##7D3W##7D3X HTLV-1,AAV[Ref.22457529]Human T-lymphotropic virus type 1(HTLV-1):APOBEC3A hapII potently decrease HTLV-1 infectivity.##[Ref.16527742]adeno-associated virus(AAV):APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. AF-P31941-F1Exhibits antiviral activity against adeno-associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. 22457529##16527742|Ooms M, Krikoni A, Kress AK, Simon V, Mnk C. ##Chen H, Lilley CE, Yu Q, Lee DV, Chou J, Narvaiza I, Landau NR, Weitzman MD.APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1.##APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons.Anti-HTLV-1,Anti-AAV DRAVPR0028~MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQVYFKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAFLHRTLKEILRYLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLMDQHMGFLCNEAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWDGLEEHSQALSGRLRAILQNQGN#DNA dC->dU-editing enzyme APOBEC-3BQ9UH17APOBEC3BF2NBQ##5CQD##5CQH##5CQI##5CQK##5SXG##5SXH##5TD5##5TKM##6NFK##6NFL##6NFM HTLV-1,SIV9[Ref.22457529]Human T-lymphotropic virus type 1(HTLV-1):APOBEC3B hapII potently decrease HTLV-1 infectivity.##[Ref.15466872]simian immunodeficiency virus(SIV):APOBEC3B induced abunda< nt G ! A mutations in both wild-type and SIV reverse transcripts, exert efficient antiretroviral effects in infected target cells. AF-Q9UH17-F1Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T-cell leukemia virus type 1 (HTLV-1).22457529##15466872hOoms M, Krikoni A, Kress AK, Simon V, Mnk C. ##Yu Q, Chen D, Knig R, Mariani R, Unutmaz D, Landau NR. APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1.##APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication.Anti-HTLV-1,Anti-SIV DRAVPR0029MNPQIRNPMKAMYPGTFYFQFKNLWEANDRNETWLCFTVEGIKRRSVVSWKTGVFRNQVDSETHCHAERCFLSWFCDDILSPNTKYQVTWYTSWSPCPDCAGEVAEFLARHSNVNLTIFTARLYYFQYPCYQEGLRSLSQEGVAVEIMDYEDFKYCWENFVYNDNEPFKPWKGLKTNFRLLKRRLRESLQ#DNA dC->dU-editing enzyme APOBEC-3CQ9NRW3APOBEC3C 3VM8##3VOW SIV,HSV-1,EBV%[Ref.15466872]simian immunodeficiency virus(SIV):APOBEC3C have potent antiviral activity against simian immuno-deficiency virus (SIV).##[Ref.21632763]Herpes simplex virus 1(HSV-1):APOBEC3C restricts the replication of HSV-1;##Epstein-Barr virus (EBV):APOBEC3C restricts the replication of EBV. AF-Q9NRW3-F1Exhibits antiviral activity against simian immunodeficiency virus (SIV), herpes simplex virus 1 (HSV-1) and Epstein-Barr virus (EBV).15466872##21632763Yu Q, Chen D, Knig R, Mariani R, Unutmaz D, Landau NR. ##Suspne R, Aynaud MM, Koch S, Pasdeloup D, Labetoulle M, Gaertner B, Vartanian JP, Meyerhans A, Wain-Hobson S. APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication.##Genetic editing of herpes simplex virus 1 and Epstein-Barr herpesvirus genomes by human APOBEC3 cytidine deaminases in culture and in vivo.Anti-SIV,Anti-HSV-1,Anti-EBV DRAVPR0030MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGPVLPKRQSNHRQEVYFRFENHAEMCFLSWFCGNRLPANRRFQITWFVSWNPCLPCVVKVTKFLAEHPNVTLTISAARLYYYRDRDWRWVLLRLHKAGARVKIMDYEDFAYCWENFVCNEGQPFMPWYKFDDNYASLHRTLKEILRNPMEAMYPHIFYFHFKNLLKACGRNESWLCFTMEVTKHHSAVFRKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLCYFWDTDYQEGLCSLSQEGASVKIMGYKDFVSCWKNFVYSDDEPFKPWKGLQTNFRLLKRRLREILQ#DNA dC->dU-editing enzyme APOBEC-3DQ96AK3 APOBEC3D _[Ref.16920826]Human immunodeficiency virus type 1 (HIV-1):after the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA AF-Q96AK3-F1KAPOBEC3D blocked the replication of both HIV-1 and SIV but not that of MLV.16920826&Dang Y, Wang X, Esselman WJ, Zheng YH.[Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. DRAVPR0031uMKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPRLDAKIFRGQVYSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLAEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDDEEFAYCWENFVYSEGQPFMPWYKFDDNYAFLHRTLKEILRNPMEAMYPHIFYFHFKNLRKAYGRNESWLCFTMEVVKHHSPVSWKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLYYFWDTDYQEGLRSLSQEGASVEIMGYKDFKYCWENFVYNDDEPFKPWKGLKYNFLFLDSKLQEILE#DNA dC->dU-editing enzyme APOBEC-3FQ8IUX4APOBEC3F43WUS##4IOU##4J4J##5HX4##5HX5##5W2M##5ZVA##5ZVB##6NIL HIV-1,XMRV[Ref.15141007]Human immunodeficiency virus type 1(HIV-1):APOBEC3F induced G to A hypermutations in HIV genomic DNA at the step of reverse transcription in target cells and thus inhibited the replication of HIV-1.##[Ref.20335265]Xenotropic murine leukemia virus-related virus (XMRV):the expression of APOBEC3F in virus-producing cells resulted in their virion incorporation, inhibition of XMRV replication, and G-to-A hypermutation of the viral DNA. AF-Q8IUX4-F1Exhibits antiviral activity also against hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV).4There is a disulfide bond between Cys280 and Cys283.15141007##20335265Zheng YH, Irwin D, Kurosu T, Tokunaga K, Sata T, Peterlin BM.##Pa< protka T, Venkatachari NJ, Chaipan C, Burdick R, Delviks-Frankenberry KA, Hu WS, Pathak VK. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication.##Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs. Anti-HIV-1,Anti-XMRV DRAVPR0032MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN#DNA dC->dU-editing enzyme APOBEC-3GQ9HC16APOBEC3G`2JYW## 2KBO## 2KEM##3E1U##3IQS##3IR2##3V4J##3V4K##4ROV##4ROW##5ZVA##5ZVB##6BUX##6BWY##6K3J##6K3K HIV-1,HBV[Ref.15031497]Hepatitis B virus(HBV):The block of HBV DNA accumulation by APOBEC3G thus seems to result primarily from an inhibition of viral pregenomic RNA packaging. AF-Q9HC16-F1Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV).)Phosphorylation of Thr at position 32,21812808466##15031497nMangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D.##Turelli P, Mangeat B, Jost S, Vianin S, Trono D.Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.##Inhibition of hepatitis B virus replication by APOBEC3G.Anti-HIV-1,Anti-HBV DRAVPR0033MKPHFRNPVERMYQDTFSDNFYNRPILSHRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSKLKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLHQDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLAKAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLEEHSQALSGRLRAILQNQGNPan troglodytes (Chimpanzee)Q7YR24 HIV-1,SFV"[Ref.12859895]Human immunodeficiency virus type 1(HIV-1):APOBEC3G can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells.##[Ref.16378963]simian foamy virus (SFV):inhibition of the replication of SFV. AF-Q7YR24-F1Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also against simian foamy virus (SFV). *Phosphorylation of Thr at position 32,218.12859895##16378963Mariani R, Chen D, Schrfelbauer B, Navarro F, Knig R, Bollman B, Mnk C, Nymark-McMahon H, Landau NR. ##Delebecque F, Suspne R, Calattini S, Casartelli N, Sab A, Froment A, Wain-Hobson S, Gessain A, Vartanian JP, Schwartz O.~Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.##Restriction of foamy viruses by APOBEC cytidine deaminases.Anti-HIV-1,Anti-SFV DRAVPR0034yMNPQIRNMVEQMEPDIFVYYFNNRPILSGRNTVWLCYEVKTKDPSGPPLDANIFQGKLYPEAKDHPEMKFLHWFRKWRQLHRDQEYEVTWYVSWSPCTRCANSVATFLAEDPKVTLTIFVARLYYFWKPDYQQALRILCQERGGPHATMKIMNYNEFQHCWNEFVDGQGKPFKPRKNLPKHYTLLHATLGELLRHVMDPGTFTSNFNNKPWVSGQRETYLCYKVERSHNDTWVLLNQHRGFLRNQAPDRHGFPKGRHAELCFLDLIPFWKLDDQQYRVTCFTSWSPCFSCAQKMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLHRDGAKIAVMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSGRLRAI<Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)Q7YR25 DRAVPR0035MALLTAETFRLQFNNKRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFINEIKSMGLDETQCYQVTCYLTWSPCSSCAWELVDFIKAHDHLNLGIFASRLYYHWCKPQQKGLRLLCGSQVPVEVMGFPEFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKIPGVRAQGRYMDILCDAEV#DNA dC->dU-editing enzyme APOBEC-3HQ6NTF7APOBEC3H5W45##6B0B## 6BBO HTLV-1,HIV-1[Ref.22457529]Human T-lymphotropic virus type 1(HTLV-1):APOBEC3H hapII potently decrease HTLV-1 infectivity.##[Ref.18299330]Human immunod< eficiency virus type 1 (HIV-1):APOBEC3H inhibits HIV-1 replication potently by a cytidine deamination-independent mechanism. AF-Q6NTF7-F1yAPOBEC3H blocked replication of both HIV-1 and SIV. Moreover, its antiretroviral activity was not countered by HIV-1 Vif.22457529##18299330bOoms M, Krikoni A, Kress AK, Simon V, Mnk C.##Dang Y, Siew LM, Wang X, Han Y, Lampen R, Zheng YH.APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1.##Human cytidine deaminase APOBEC3H restricts HIV-1 replication.Anti-HTLV-1,Anti-HIV-1 DRAVPR0036rMVEPMDPRTFVSNFNNRPILSGLNTVWLCCEVKTKDPSGPPLDAKIFQGKVYSKAKYHPEMRFLRWFHKWRQLHHDQEYKVTWYVSWSPCTRCANSVATFLAKDPKVTLTIFVARLYYFWKPDYQQALRILCQKRGGPHATMKIMNYNEFQDCWNKFVDGRGKPFKPRNNLPKHYTLLQATLGELLRHLMDPGTFTSNFNNKPWVSGQHETYLCYKVERLHNDTWVPLNQHRGFLRNQAPNIHGFPKGRHAELCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKFISNNEHVSLCIFAARIYDDQGRYQEGLRALHRDGAKIAMMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSGRLRAIMacaca mulatta (Rhesus macaque)Q7YR23[Ref.21835787]Human immunodeficiency virus type 1 (HIV-1):the protein expressed in CD4 T lymphocytes, are packaged into and restrict Vif-deficient HIV-1 when stably expressed in T cells, mutate proviral DNA, and are counteracted by HIV-1 Vif. dExhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs).)Phosphorylation of Thr at position 25,21112859895##21835787Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D.##Hultquist JF, Lengyel JA, Refsland EW, LaRue RS, Lackey L, Brown WL, Harris RS.Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.##Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1. DRAVPR0037MALLTAKTFSLQFNNKRRVNKPYYPRKALLCYQLTPQNGSTPTRGHLKNKKKDHAEIRFINKIKSMGLDETQCYQVTCYLTWSPCPSCAGELVDFIKAHRHLNLRIFASRLYYHWRPNYQEGLLLLCGSQVPVEVMGLPEFTDCWENFVDHKEPPSFNPSEKLEELDKNSQAIKRRLERIKSRSVDVLENGLRSLQLGPVTPSSSIRNSRQ19Q52[Ref.21835787]Human immunodeficiency virus type 1 (HIV-1):the protein expressed in CD4 T lymphocytes, are packaged into and restrict Vif-deficient HIV-1 when stably expressed in T cells, mutate proviral DNA. AF-Q19Q52-F1cExhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIV).21835787OHultquist JF, Lengyel JA, Refsland EW, LaRue RS, Lackey L, Brown WL, Harris RS.}Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1. DRAVPR0038MQPQRLGPRAGMGPFCLGCSHRKCYSPIRNLISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLKVLSPREEFKITWYMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWKRLLTNFRYQDSKLQEILRPCYISVPSSSSSTLSNICLTKGLPETRFWVEGRRMDPLSEEEFYSQFYNQRVKHLCYYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMELSQVTITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRPFWPWKGLEIISRRTQRRLRRIKESWGLQDLVNDFGNLQLGPPMS"DNA dC->dU-editing enzyme APOBEC-3Q99J72Apobec3 MMTV,FrMLV[Ref.17259974]mouse mammary tumour virus(MMTV):APOBEC3 inhibits mouse mammary tumour virus replication.##[Ref.18786991]friend leukemia virus(FrMLV):Mouse APOBEC3 restricts friend leukemia virus infection in vivo. AF-Q99J72-F1TRIM52 is a RING-type E3 ligase, the RING domain of TRIM52 is required for TRIM52 to control JEV replication.TRIM22 is endowed with a potent capacity to repress various viral infections, including HIV, HBV, EMCV, and IAV.17259974##18786991Okeoma CM, Lovsin N, Peterlin BM, Ross SR.##Takeda E, Tsuji-Kawahara S, Sakamoto M, Langlois MA, Neuberger MS, Rada C, Miyazawa M. APOBEC3 inhibits mouse mammary tumour virus replication in vivo.##Mouse APOBEC3 restricts friend leukemia virus infection and pathogenesis in vivo.Anti-MMTV,Anti-FrMLV DRAVPR0039)MAGYATTPSPMQTLQEEAVCAICLDYFKDPVSISCGHNFCRGCVTQLWSKEDEEDQNEEEDEWEEEEDEEAVGAMDGWDGSIREVLYRGNADEELFQDQDDDELWLGDSGITNWDNVDYMWDEEEEEEEEDQDYYLGGLRPDLRIDVYREEEILEAYDEDEDEELYPDIHPPPSLPLPGQFTCPQCRKSFTRRSFRPNLQLANMVQIIRQMCPTPYRGNRSNDQGMCFKHQEALKLFCEVDKEAICVVCRESRSHKQHSVLPLEEVVQEYQEIKLETTLV< GILQIEQESIHSKAYNQ"E3 ubiquitin-protein ligase TRIM52Q96A61TRIM52JEV[Ref.27667714]Japanese encephalitis virus (JEV):TRIM52 interacted with NS2A and induced NS2A ubiquitination, resulting in NS2A degradation. AF-Q96A61-F1Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV).276677142Fan W, Wu M, Qian S, Zhou Y, Chen H, Li X, Qian P.TTRIM52 inhibits Japanese Encephalitis Virus replication by degrading the viral NS2A.Anti-JEV DRAVPR0040jMPKEQQEVVVLGSPHISTSATATTINMPEISTPDHVVWSLFNTLFMNFCCLGFVAYAYSVKSRDRKMVGDTTGAQAFASTAKCLNISSLFFTILTAIVVIVVCAIR+Interferon-induced transmembrane protein 1 Q9D103Ifitm1 MERS-CoVw[Ref.25256397]MERS-CoV:Expression of IFITM proteins in target cells inhibited entry driven by the S protein of MERS-CoV AF-Q9D103-F1Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV).<The Cys at position 49,50,83 indicates S-palmitoyl cysteine.25256397!Wrensch F, Winkler M, Phlmann S.| IFITM proteins inhibit entry driven by the MERS-coronavirus spike protein: evidence for cholesterol-independent mechanisms. Anti-MERS-CoV DRAVPR0041MSHNSQAFLSTNAGLPPSYETIKEEYGVTELGEPSNSAVVRTTVINMPREVSVPDHVVWSLFNTLFFNACCLGFVAYAYSVKSRDRKMVGDVVGAQAYASTAKCLNISSLIFSILMVIICIIIFSTTSVVVFQSFAQRTPHSGF*Interferon-induced transmembrane protein 2Q99J93Ifitm2SARS-CoV,IAV,EBOV[Ref.21253575]influenza A virus(IAV):Ifitm2 inhibits infection mediated by the influenza A virus (IAV) hemagglutinin (HA) protein.##SARS-CoV:IFITM proteins can restrict the replication of infectious SARS coronavirus (SARS-CoV) and entry mediated by the SARS-CoV spike (S) protein. ##Ebola virus(EBOV):IFITM proteins restricted infection mediated by the entry glycoproteins (GP1,2) of Ebola filoviruses. AF-Q99J93-F1+Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) 21253575Huang IC, Bailey CC, Weyer JL, Radoshitzky SR, Becker MM, Chiang JJ, Brass AL, Ahmed AA, Chi X, Dong L, Longobardi LE, Boltz D, Kuhn JH, Elledge SJ, Bavari S, Denison MR, Choe H, Farzan M. hDistinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus. Anti-SARS-CoV,Anti-IAV,Anti-EBOV DRAVPR0042MNHTSQAFITAASGGQPPNYERIKEEYEVAEMGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAYSVKSRDRKMVGDVTGAQAYASTAKCLNISTLVLSILMVVITIVSVIIIVLNAQNLHT+Interferon-induced transmembrane protein 3 Q9CQW9Ifitm3SARS-CoV,IAV,EBOV,SARS-CoV-2,[Ref.21253575]influenza A virus(IAV):Ifitm3 inhibits infection mediated by the influenza A virus (IAV) hemagglutinin (HA) protein.##SARS-CoV:IFITM proteins can restrict the replication of infectious SARS coronavirus (SARS-CoV) and entry mediated by the SARS-CoV spike (S) protein. ##Ebola virus(EBOV):IFITM proteins restricted infection mediated by the entry glycoproteins (GP1,2) of Ebola filoviruses.##[Ref.33270927]SARS-CoV-2:IFITM3 likely restrict SARS CoV 2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes. AF-Q9CQW9-F1OVAMP8 plays an antiviral role in response to Japanese encephalitis virus (JEV).h`$Phosphorylation of Ser at position 20,27.a$The Cys at position 71,72,105 indicates S-palmitoyl cysteine.21253575##33270927;Huang IC, Bailey CC, Weyer JL, Radoshitzky SR, Becker MM, Chiang JJ, Brass AL, Ahmed AA, Chi X, Dong L, Longobardi LE, Boltz D, Kuhn JH, Elledge SJ, Bavari S, Denison MR, Choe H, Farzan M. ##Shi G, Kenney AD, Kudryashova E, Zani A, Zhang L, Lai KK, Hall-Stoodley L, Robinson RT, Kudryashov DS, Compton AA, Yount JS.Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus.##Opposing activities of IFITM proteins in SARS-CoV-2 infection.0Anti< -SARS-CoV,Anti-IAV,Anti-EBOV,Anti-SARS-CoV-2 DRAVPR0043dMEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS%Vesicle-associated membrane protein 8Q9BV40VAMP8 4WY4##7BV6[Ref.31694946]West Nile virus(WNV):VAMP8 contributes to the TRIM6-mediated type I interferon antiviral response during west nile virus infection. AF-Q9BV40-F1Cyclophilin A regulates the life cycle of several viruses including human immunodeficiency virus type 1, vesicular stomatitis virus, vaccinia virus (VV), hepatitis C virusx`$Phosphorylation of Ser at position 5,18,55.a$The N-terminal is acetylation.b$Phosphorylation of Thr at position 28,48,54.31694946Lvan Tol S, Atkins C, Bharaj P, Johnson KN, Hage A, Freiberg AN, Rajsbaum R. nVAMP8 Contributes to the TRIM6-Mediated Type I Interferon Antiviral Response during West Nile Virus Infection. DRAVPR0044MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE4Peptidyl-prolyl cis-trans isomerase A(Cyclophilin A)P62937PPIA41AWQ##1BCK##1CWF##1M9X##1W8M##2CPL##3K0M##4N1M##4YUO IAV,HIV-1N[Ref.19207730]influenza A virus(IAV):cyclophilin A interacts with M1 protein and impairs the early stage of the vial replication.##Human immunodeficiency virus type 1(HIV-1):Cyclophilin A interacts with the Gag protein of HIV-1 by the CA domain and then is incorporated into HIV-1 virion, influencing the infectivity of HIV-1 virions. AF-P62937-F1`$Phosphorylation of Ser at position 77.a$The N-terminal is acetylation.b$Phosphorylation of Thr at position 93.c$The Lys at position 28,44,76,82,125,131,133 indicates N6-acetyllysine.19207730JLiu X, Sun L, Yu M, Wang Z, Xu C, Xue Q, Zhang K, Ye X, Kitamura Y, Liu W.oCyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication.Anti-IAV,Anti-HIV-1 DRAVPR0045MSKLRNLLPTIFGGKEAQNPTPVEGRLEKDAAPVDDNEPDNNNSGALALPSTAGTPTASSDLTESVLRELSDPNYNSMDVVHSANIPGTLSNVQTNNTMNVHSAQQQVVMNFSNANNLHFGSVYNFNQNLSACSSRKGSTSTAEESVASPDGKPRASATRKTVSIVAMMQSQEEPDVRLLDVVSTHLGEGWKQVMRDLGMSEGQIDQAIIDHQMHGNIREVIYQLLLQWIRSSADGVATVGRLTTLLWESQHRDCVQRMKLVWKALEKRKTNSProtein immune deficiency #Drosophila melanogaster (Fruit fly)Q7K4Z4imdSVh[Ref.19763182]Sindbis virus(SV):Imd pathway mediates an antiviral response to Sindbis virus replication. AF-Q7K4Z4-F1197631828Avadhanula V, Weasner BP, Hardy GG, Kumar JP, Hardy RW. }A novel system for the launch of alphavirus RNA synthesis reveals a role for the Imd pathway in arthropod antiviral response.Anti-SV DRAVPR0046MVHRQLPETVLLLLVSSTIFSLEPKRIPFQLWMNRESLQLLKPLPSSSVQQCLAHRKNFLLPQQPVSPHQYQEGQVLAVVHEILQQIFTLLQTHGTMGIWEENHIEKVLAALHRQLEYVESLGGLNAAQKSGGSSAQNLRLQIKAYFRRIHDYLENQRYSSCAWIIVQTEIHRCMFFVFRFTTWLSRQDPDPInterferon epsilonQ80ZF2IfneHSV-2a[Ref.23449591]Herpes simplex virus 2(HSV-2):Interferon- directly protects from viral infection. AF-Q80ZF2-F1IL-17A was implicated in priming T cell responses during lymphocytic choriomeningitis virus (LCMV) hepatitis and mediating the immunopathogenicity of viral infections, such as influenza virus, respiratory syncytial virus, murine encephalomyelitis virus, and hepatitis B virus infections.3There is a disulfide bond between Cys52 and Cys162.23449591Fung KY, Mangan NE, Cumming H, Horvat JC, Mayall JR, Stifter SA, De Weerd N, Roisman LC, Rossjohn J, Robertson SA, Schjenken JE, Parker B, Gargett CE, Nguyen HP, Carr DJ, Hansbro PM, Hertzog PJ. WInterferon- protects the female reproductive tract from viral and bacterial infection. Anti-HSV-2 DRAVPR0047MSPGRASSVSLMLLLLLSLAATVKAAAIIPQSSACPNTEAKDFLQNVKVNLKVFNSLGAKVSSRRPSDYLNRSTSPWTLHRNEDPDRYPSVIWEAQCRHQRCVNAEGKLDHHMNSVLIQQEILVLKREPESCPFTFRVEKMLVGVGCTCVASIVRQAAInterleukin-17A(IL-17)Q62386Il17aH5N1,WNV[Ref.21946434]H5N1:IL17A may play a beneficial role in influenza A virus (H5N1) infection by enhancing B cell recruitment and immune response in the lung.##[Ref.27795421]West Nile virus(WNV):IL17A promotes CD8+ T cell cytotoxicity to facilitate west nile virus clearance< . AF-Q62386-F1Viperin contains an N-terminal amphipathic -helix that localizes to the cytosolic face of the ER and inhibits bulk protein secretion (22), which could impact virus production directly or indirectly. Viperin also inhibits farnesyl diphosphate synthetase, a cholesterol and isoprenoid biosynthesis enzyme, resulting in the inhibition of lipid raft formation and influenza virus buddingp`$Glycosylation of Asn at position 71.a$There are two disulfide bonds between Cys97 and Cys147, Cys102 and Cys149.21946434##27795421Wang X, Chan CC, Yang M, Deng J, Poon VK, Leung VH, Ko KH, Zhou J, Yuen KY, Zheng BJ, Lu L.##Acharya D, Wang P, Paul AM, Dai J, Gate D, Lowery JE, Stokic DS, Leis AA, Flavell RA, Town T, Fikrig E, Bai F. A critical role of IL-17 in modulating the B-cell response during H5N1 influenza virus infection.##Interleukin-17A Promotes CD8+ T Cell Cytotoxicity To Facilitate West Nile Virus Clearance. Anti-H5N1,Anti-WNV DRAVPR0048jMGMLVPTALAARLLSLFQQQLGSLWSGLAILFCWLRIALGWLDPGKEQPQVRGEPEDTQETQEDGNSTQPTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGEYLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADLKLDWBRadical S-adenosyl methionine domain-containing protein 2(Viperin)Q8CBB9Rsad25VSL##5VSM##6Q2P##6Q2QWNV,SBVZ[Ref.21880757]West Nile virus(WNV):viperin contributes to the antiviral responses against WNV in vivo, as the targeted deletion of viperin was associated with increased lethality and selectively enhanced replication in specific tissues.##[Ref.17686841]Sindbis virus (SBV):viperin exhibited modest replication inhibition of sindbis virus in vitro. AF-Q8CBB9-F1 Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, implicated in inhibiting the replication of a remarkable range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus2 and HIV.Viperin suppresses the replication of influenza A and HIV-1 by blocking the release of viral particles, interacts with the RC of HCV and DENV to inhibit viral replication by binding with the nonstructural HCV protein NS5A and the DENV NS3 protein2The Lys at position 198 idnicates N6-acetyllysine.17686841##21880757rZhang Y, Burke CW, Ryman KD, Klimstra WB.##Szretter KJ, Brien JD, Thackray LB, Virgin HW, Cresswell P, Diamond MS.Identification and characterization of interferon-induced proteins that inhibit alphavirus replication.##The interferon-inducible gene viperin restricts West Nile virus pathogenesis.Anti-WNV,Anti-SBV DRAVPR0049iMWVLTPAAFAGKLLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRRKQQLVLRGPDETKEEEEDPPLPTTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPSVSIVSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRWCRDYRVAFKINSVINRFNVEEDMTEQIKALNPVRWKVFQCLLIEGENCGEDALREAERFVIGDEEFERFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCRKGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYIWSKADLKLDWQ8WXG1RSAD2ZIKV,WNV,DENV,HCV,EVA71,HSV-1m[Ref.29925952]Zika virus(ZIKV)/west nile virus(WNV)/dengue virus (DENV)/hepatitis C virus(HCV):viperin catalyzes the conversion of cytidine triphosphate (CTP) to 32 -deoxy-32 ,42 -didehydro-CTP (ddhCTP),and inhibits in vivo replication of ZIKA virus.##[Ref.30587778]Enterovirus A71 (EVA71):amino acids 50 60 in the N-terminal domain of viperin were the key residues responsible for viperin interaction with 2C, the N-terminal domain of viperin was found responsible for inhibiting EVA71 replication.##[Ref.31921110]Herpes Simplex Virus 1(HSV-1):gD(Glycoprotein D) of HSV-1 and viperin interaction inhibits HSV-1 replication.XThe SAM and N-terminal viperin domains were most important for CSFV and PEDV inhibition.2The Lys at position 197 idnicates N6-acetyllysine.29925952##30587778##31921110KGizzi AS, Grove TL, Arnold JJ, Jose J, Jangra RK, Garforth SJ, Du Q, Cahill SM, Dulyaninova NG, Love JD, Chandran K, Bresnick AR, Cameron CE, Almo SC.##Wei C, Zheng C, Sun J, Luo D, Tang Y< , Zhang Y, Ke X, Liu Y, Zheng Z, Wang H. ##Li M, Liao Z, Xu Z, Zou X, Wang Y, Peng H, Li Y, Ou X, Deng Y, Guo Y, Gan W, Peng T, Chen D, Cai M. A naturally occurring antiviral ribonucleotide encoded by the human genome.##Viperin Inhibits Enterovirus A71 Replication by Interacting with Viral 2C Protein.##The Interaction Mechanism Between Herpes Simplex Virus 1 Glycoprotein D and Host Antiviral Protein Viperin. ;Anti-ZIKV,Anti-WNV,Anti-DENV,Anti-HCV,Anti-EVA71,Anti-HSV-1 DRAVPR0050jMWTLVPVTFALRLLSTFVQPLGSLGSSLGPLFLWLWAAFWRAGGDRSRQQLQGKTEAGEPPRAQEDSHLPTTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLWLLKEAGMEKINFSGGEPFIHDRGEYLGKLVRFCKEELQLPSVSIVSNGSLIWERWFKSYGEYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRTWCRDYKVAFKINSVINRFNVEEDMTEHIKALNPVRWKVFQCLLIEGENVGEDALREAEQFVISDEEFEEFLDRHKDVSCLVPESNRQMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEKAIKFSGFDEKMFLKRGGKYVWSKADLKLDW9Radical S-adenosyl methionine domain-containing protein 2Q9MZU4RSAD2 PEDV,CSFVj[Ref.32719955]Porcine epidemic diarrhea virus(PEDV):The interaction of the viperin S-adenosylmethionine domain with the N protein of PEDV might interfere with viral replication or assembly to reduce virus proliferation.##[Ref.31517388]Classical swine fever virus (CSFV):Viperin inhibits the replication of CSFV by interacting with viral nonstructural 5A protein. AF-Q9MZU4-F132719955##31517388Wu J, Chi H, Fu Y, Cao A, Shi J, Zhu M, Zhang L, Hua D, Huang J.##Xu C, Feng L, Chen P, Li A, Guo S, Jiao X, Zhang C, Zhao Y, Jin X, Zhong K, Guo Y, Zhu H, Han L, Yang G, Li H, Wang Y.The antiviral protein viperin interacts with the viral N protein to inhibit proliferation of porcine epidemic diarrhea virus.##Viperin inhibits classical swine fever virus replication by interacting with viral nonstructural 5A protein.Anti-PEDV,Anti-CSFV DRAVPR0051eLGKFSQTCYNSAIQGSVLTSTCERTNGGYNTSSIDLNSVIENVDGSLKWQPSNFIETCRNTQLAGSSELAAECKTRAQQFVSTKINLDDHIANIDGTLKYE Cyanovirin-NNostoc ellipsosporumP811801LOM##2RDK##3CZZ##4J4C##6X7HHIVy[Ref.20162270]Human immunodeficiency virus(HIV):CVN is effective against most HIV strains with an EC50 of less than 1 nM. AF-P81180-F1Elevated cellular levels of human BST-2 inhibited the release of virus-like particles (VLPs) consisting of the matrix proteins of multiple highly virulent NIAID Priority Pathogens, including arenaviruses (LASV and Machupo virus [MACV]), filoviruses (ZEBOV and MARV), and paramyxoviruses (Nipah virus). However, filoviruses, RVFV, and CPXV are immune to the inhibitory effect of BST-2.FThere are two disulfide bonds between Cys8 and Cys22, Cys58 and Cys73.20162270Xiong S, Fan J, Kitazato K.YThe antiviral protein cyanovirin-N: the current state of its production and applications.Anti-HIV DRAVPR0052MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ'Bone marrow stromal antigen 2(Tetherin)Q10589BST2(2LK9##2X7A##2XG7##3MQ7##3MQ9##4P6Z##6CM95SARS-CoV,HCoV 229E,HIV-1,LASV, MACV, ZEBOV, MARV, NiV[Ref.31199522]SARS-CoV/HCoV 229E:BST2 is capable of inhibiting SARS CoV and HCoV 229E VLP release.##[Ref.18342597]Human immunodeficiency virus 1(HIV-1):BST-2 inhibits the release of virions from cells.##[Ref.20686043]Zaire ebolavirus (ZEBOV)/Lake Victoria marburgvirus (MARV)/Lassa virus (LASV)/Machupo virus(MACV)/paramyxoviral (NiV):BST-2 inhibits the release of a variety of VLPs, generated by the expression of arenaviral (LASV and MACV), filoviral (ZEBOV and MARV), or paramyxoviral (NiV) matrix proteins. AF-Q10589-F1'Glycosylation of Asn at position 65,92.31199522##18342597##20686043Wang SM, Huang KJ, Wang CT.##Van Damme N, Goff D, Katsura C, Jorgenson RL, Mitchell R, Johnson MC, Stephens EB, Guatelli J.##Radoshitzky SR, Dong L, Chi X, Clester JC, Retterer C, Spurgers K, Kuhn JH, Sandwick S, Ruthel G, Kota K, Boltz D, Warren T, Kranzusch PJ, Whelan SP, Bavari S.TSevere acute respiratory syndrome coronavirus spike protein counteracts BST2-mediated restriction of virus-like particle release.##The interferon-induced protein BST-2 restricts HIV-1 release<  and is downregulated from the cell surface by the viral Vpu protein.##Infectious Lassa virus, but not filoviruses, is restricted by BST-2/tetherin.NAnti-SARS-CoV,HCoV 229E,Anti-HIV-1,LASV, Anti-MACV, ZAnti-EBOV, MARV, Anti-NiV DRAVPR0053MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE%Interleukin enhancer-binding factor 2Q12905 ILF2 (NF45)[Ref.31212927]Japanese Encephalitis Virus(JEV):ILF2 interacts with JEV NS3, and involved in the JEV life cycle and inhibits JEV replication in 293T cells. AF-Q12905-F1C19orf66 was suggested to be a novel ISG, the products of which can suppress DENV, WNV, hepatitis C virus (HCV) and Kunjin virus, Chikungunya virus, herpes simplex virus type 1, and human adenovirus replication in vitro.`$Phosphorylation of Ser at position 52,68.a$The Arg at position 16,24 indicates Omega-N-methylarginine.b$Phosphorylation of Thr at position 388.31212927<Cui X, Qian P, Rao T, Wei Y, Zhao F, Zhang H, Chen H, Li X. pCellular Interleukin Enhancer-Binding Factor 2, ILF2, Inhibits Japanese Encephalitis Virus Replication In Vitro. DRAVPR0054#MSQEGVELEKSVRRLREKFHGKVSSKKAGALMRKFGSDHTGVGRSIVYGVKQKDGQELSNDLDAQDPPEDMKQDRDIQAVATSLLPLTEANLRMFQRAQDDLIPAVDRQFACSSCDHVWWRRVPQRKEVSRCRKCRKRYEPVPADKMWGLAEFHCPKCRHNFRGWAQMGSPSPCYGCGFPVYPTRILPPRWDRDPDRRSTHTHSCSAADCYNRREPHVPGTSCAHPKSRKQNHLPKVLHPSNPHISSGSTVATCLSQGGLLEDLDNLILEDLKEEEEEEEEVEDEEGGPREGShiftless antiviral inhibitor of ribosomal frameshifting protein(RyDEN)Q9NUL5SHFL(C19orf66) ZIKV,DENV,HCVA[Ref.32150556]Zika virus(ZIKV):C19orf66 interacts and co-localizes with ZIKV nonstructural protein 3 (NS3), thus inducing NS3 degradation via a lysosome-dependent pathway and interrupts the replication of ZIKV.##[Ref.26735137]Dengue Virus(DENV):RyDEN is likely to interfere with the translation of DENV via interaction with viral RNA and cellular mRNA-binding proteins, resulting in the inhibition of virus replication in infected cells.##[Ref.32294532]Hepatitis C Virus(HCV):C19orf66 inhibits the replication of HCV by restricting formation of the viral replication organelle. AF-Q9NUL5-F1The expression of MARCH2 to be upregulated upon HIV-1 infection. MARCH2 inhibits the production and infection of HIV-1 through ligase activity-dependent envelope protein degradation and/or intracellular retention.0Acetylation of Ser at position 2(N-acetylserine)32150556##26735137##322945322Wu Y, Yang X, Yao Z, Dong X, Zhang D, Hu Y, Zhang S, Lin J, Chen J, An S, Ye H, Zhang S, Qiu Z, He Z, Huang M, Wei G, Zhu X.##Suzuki Y, Chin WX, Han Q, Ichiyama K, Lee CH, Eyo ZW, Ebina H, Takahashi H, Takahashi C, Tan BH, Hishiki T, Ohba K, Matsuyama T, Koyanagi Y, Tan YJ, Sawasaki T, Chu JJ, Vasudevan SG, Sano K, Yamamoto N.##Kinast V, Plociennikowska A, Anggakusuma, Bracht T, Todt D, Brown RJP, Boldanova T, Zhang Y, Brggemann Y, Friesland M, Engelmann M, Vieyres G, Broering R, Vondran FWR, Heim MH, Sitek B, Bartenschlager R, Pietschmann T, Steinmann E.OC19orf66 interrupts Zika virus replication by inducing lysosomal degradation of viral NS3.##Characterization of RyDEN (C19orf66) as an Interferon-Stimulated Cellular Inhibitor against Dengue Virus Replication.##C19orf66 is an interferon-induced inhibitor of HCV replication that restricts formation of the viral replication organelle. Anti-ZIKV,Anti-DENV,Anti-HCV DRAVPR0055MTTGDCCHLPGSLCDCSGSPAFSKVVEATGLGPPQYVAQVTSRDGRLLSTVIRALDTPSDGPFCRICHEGANGECLLSPCGCTGTLGAVHKSCLEKWLSSSNTSYCELCHTEFAVEKRPRPLTEWLKDPGPRTEKRTLCCDMVCFLFITPLAAISGWLCLRGAQDHLRLHSQLEAVGLIALTIALFTIYVLWTLVSFRYHCQLYSEWRKTNQKVRLKIREADSPEGPQHSPLAAGLLKKVAEETPV#E3 ubiquitin-protein ligase MARCHF2Q9P0N8MARCHF2%[Ref.29573664]Human immunodeficiency virus type 1(HIV-1):MARCH2 decreased or increased the HIV-1 production in both the VSV-G- and Env-pseudo-typed HIV-1 produc< tion system. And it exerted its function by degrading VSV-G via the lysosome or by reducing the amount of Env on the plasma membrane.GMARCH8 might display broad-spectrum activity against enveloped viruses.29573664Zhang Y, Lu J, Liu X. }MARCH2 is upregulated in HIV-1 infection and inhibits HIV-1 production through envelope protein translocation or degradation. DRAVPR0056#MSMPLHQISAIPSQDAISARVYRSKTKEKEREEQNEKTLGHFMSHSSNISKAGSPPSASAPAPVSSFSRTSITPSSQDICRICHCEGDDESPLITPCHCTGSLHFVHQACLQQWIKSSDTRCCELCKYEFIMETKLKPLRKWEKLQMTSSERRKIMCSVTFHVIAITCVVWSLYVLIDRTAEEIKQGQATGILEWPFWTKLVVVAIGFTGGLLFMYVQCKVYVQLWKRLKAYNRVIYVQNCPETSKKNIFEKSPLTEPNFENKHGYGICHSDTNSSCCTEPEDTGAEIIHV#E3 ubiquitin-protein ligase MARCHF8Q5T0T0MARCHF82D8S$[Ref.26523972]Human immunodeficiency virus type 1(HIV-1):MARCH8 blocks the incorporation of HIV-1 envelope glycoprotein into virus particles by downregulating it from the cell surface, probably through their interaction, resulting in a substantial reduction in the efficiency of viral entry. AF-Q5T0T0-F1SAMHD1 interferes with HIV infection of macrophages by preventing efficient viral cDNA synthesis.HIV-2 and related simian viruses have evolved the Vpx function to counteract SAMHD1.'Phosphorylation of Ser at position 253.26523972[Tada T, Zhang Y, Koyama T, Tobiume M, Tsunetsugu-Yokota Y, Yamaoka S, Fujita H, Tokunaga K.[MARCH8 inhibits HIV-1 infection by reducing virion incorporation of envelope glycoproteins. DRAVPR0057rMQRADSEQPSKRPRCDDSPRTPSNTPSAEADWSPGLELHPDYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQIHVDTMKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPELQISERDVLCVQIAGLCHDLGHGPFSHMFDGRFIPLARPEVKWTHEQGSVMMFEHLINSNGIKPVMEQYGLIPEEDICFIKEQIVGPLESPVEDSLWPYKGRPENKSFLYEIVSNKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARVCEVDNELRICARDKEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKADDYIEITGAGGKKYRISTAIDDMEAYTKLTDNIFLEILYSTDPKLKDAREILKQIEYRNLFKYVGETQPTGQIKIKREDYESLPKEVASAKPKVLLDVKLKAEDFIVDVINMDYGMQEKNPIDHVSFYCKTAPNRAIRITKNQVSQLLPEKFAEQLIRVYCKKVDRKSLYAARQYFVQWCADRNFTKPQDGDVIAPLITPQKKEWNDSTSVQNPTRLREASKSRVQLFKDDPM8Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 Q9Y3Z3SAMHD1 A2E8O## 4BZB##4MZ7##4QFY##4RXQ##4TNP##4TO4##6CM2##6DWD##6TXC##7LTT[Ref.21613998]Human immunodeficiency virus type 1(HIV-1):dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells. AF-Q9Y3Z3-F1MX2 suppresses infection by all HIV-1 strains tested, has equivalent or reduced effects on divergent simian immunodeficiency viruses, and does not inhibit other retroviruses such as murine leukaemia virus.z`$Phosphorylation of Ser at position 18,33,93.a$The N-terminal is acetylation.b$Phosphorylation of Thr at position 21,25,592.21720370##21613998Hrecka K, Hao C, Gierszewska M, Swanson SK, Kesik-Brodacka M, Srivastava S, Florens L, Washburn MP, Skowronski J.##Laguette N, Sobhian B, Casartelli N, Ringeard M, Chable-Bessia C, Sgral E, Yatim A, Emiliani S, Schwartz O, Benkirane M.Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein.##SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx. DRAVPR0058MSKAHKPWPYRRRSQFSSRKYLKKEMNSFQQQPPPFGTVPPQMMFPPNWQGAEKDAAFLAKDFNFLTLNNQPPPGNRSQPRAMGPENNLYSQYEQKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKQPCEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLLEEGSATVPRLAERLTTELIMHIQKSLPLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWVGILATNTQKVKNIIHEEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLQKAMEIIQQAFINVAKKHFGEFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQMVFCQDQIYSVVLKKVREEIFNPLGTPSQNMKLNSHFPSNESSVSSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLTQARHALCQFSSKEIH*Interferon-induced GTP-binding protein Mx2P20592MX24WHJ##4X0R##5UOT[Ref.24121441]Human immunodeficiency viru< s type 1(HIV-1): MX2 acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. AF-P20592-F1Human MxA protein has a broad antiviral activity against a wide range of RNA and even some DNA viruses, including influenza A/B/C virus, ASFV(African swine fever virus); CCHFV(Crimean-Congo hemorrhagic fever virus); CVB(Coxsackie virus B); HBV(hepatitis B virus); HNTV(Hantaan virus); HPIV-3(human parainfluenza virus type 3); IBDV( infectious bursal disease virus); LACV(LaCrosse virus); MV(measles virus); RVFV(Rift Valley fever virus); SFV(Semliki Forest virus); THOV(Thogoto virus); VSV(vesicular stomatitis virus).24048477##24121441Goujon C, Moncorg O, Bauby H, Doyle T, Ward CC, Schaller T, Hu S, Barclay WS, Schulz R, Malim MH. ##Kane M, Yadav SS, Bitzegeio J, Kutluay SB, Zang T, Wilson SJ, Schoggins JW, Rice CM, Yamashita M, Hatziioannou T, Bieniasz PD.Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection.##MX2 is an interferon-induced inhibitor of HIV-1 infection. DRAVPR0059MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLLEEGKATVPCLAEKLTSELITHICKSLPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTIIENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQARRRLAQFPG/Interferon-induced GTP-binding protein Mx1(MxA)P20591MX1(3LJB##3SZR##3SZR##4P4S##4P4T##4P4U##5GTM IAV,DUGV,VSV[Ref.14687945]Dugbe nairovirus(DUGV):MX1 protein inhibits the replication of DUGV.##[Ref.2161946]Influenza virus/vesicular stomatitis virus(VSV):transfected cell lines expressing MxA acquired a high degree of resistance to influenza A virus and vesicular stomatitis virus. AF-P20591-F1The N-terminal is acetylation.21166595##14687945##2161946oHaller O, Kochs G.##Bridgen A, Dalrymple DA, Weber F, Elliott RM.##Pavlovic J, Zrcher T, Haller O, Staeheli P. Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.##Inhibition of Dugbe nairovirus replication by human MxA protein. ##Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein.Anti-IAV,Anti-DUGV,Anti-VSV DRAVPR0060MKERTSACRHGTPQKHPDTSEESQAMESVDNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKQLKQGEKWSGKVIYKDTEIEISHPSLVEREINKAQNLIAGEGLKISSDLISLEVSSPHVPDLTLIDLPGITRVAVGDQPADIEHKIKRLITEYIQKQETINLVVVPSNVDIATTEALKMAQEVDPQGDRTIGILTKPDLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRVLLEDGKATVPCLAKRLTMELTSHICKSLPILENQINVNHQIASEELQKYGADIPEDDSKRLSFLMNKINVFNKDILSLVQAQENISWEESRLFTKLRNEFLAWNDYIEEHFKKTLGSSEKHSQMEKFESHYRGRELPGFVDYKAFENIIKKEVKALEEPALNMLHRVTTMVKNAFTKVSSNNFGDFLNLHSTAKSKIEDIRFNQEKEAEKLIRLHFQMEHIVYCQDQAYKKALQEIREKEAEKEKSTFGAFQHNSPRKELTTTEMTQHLNAYYQECGRNIGRQIPLIIQYSILQTFGQEMEKAMLQLLQDTSKCNWFLTEQSDSREKKKFLKRRLLRLDEAQRKLAKFSN*Interferon-induced GTP-binding protein Mx1Rattus norvegicus (Rat)P18588Mx1IAV,THOV[Ref.21166595]influenza A virus(IAV)/Thogoto virus(THOV):exhibits antiviral activity against IAV and THOV.##[Ref.8249287]Influenza A virus(IAV):murine Mx1 protein blocks primary transcription of orthomyxoviruses via molecular interaction with the PB2 subunit of the viral polymerase. AF-P18588-F121166595##82492879Haller O, Kochs G.##Stranden AM, Staeheli P, Pavlovic J. Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.##Function of the mouse Mx1 protein is inhibited by overexpression of the PB2 protein of influenza virus. Anti-IAV, DRAVPR0061wMDSVNNLCRHYEEKVRPCIDLIDTLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKLKEGEEWRGKVSY< DDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGVLTKPDLVDRGAEGKVLDVMRNLVYPLKKGYMIVKCRGQQDIQEQLSLTEAFQKEQVFFKDHSYFSILLEDGKATVPCLAERLTEELTSHICKSLPLLEDQINSSHQSASEELQKYGADIPEDDRTRMSFLVNKISAFNRNIMNLIQAQETVSEGDSRLFTKLRNEFLAWDDHIEEYFKKDSPEVQSKMKEFENQYRGRELPGFVDYKAFESIIKKRVKALEESAVNMLRRVTKMVQTAFVKILSNDFGDFLNLCCTAKSKIKEIRLNQEKEAENLIRLHFQMEQIVYCQDQVYKETLKTIREKEAEKEKTKALINPATFQNNSQFPQKGLTTTEMTQHLKAYYQECRRNIGRQIPLIIQYFILKTFGEEIEKMMLQLLQDTSKCSWFLEEQSDTREKKKFLKRRLLRLDEARQKLAKFSDP09922 IAV,IBV,THOV[Ref.21166595]influenza A virus(IAV)/Thogoto virus(THOV)/influenza B virus (IBV)/:exhibits antiviral activity against IAV,IBV and THOV. AF-P09922-F1poMx1 decreases or delays NP synthesis, and inhibits production of progeny viral particles and hampers viral infection at an early stage.21166595Haller O, Kochs G.\Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.Anti-IAV,Anti-IBV,Anti-THOV DRAVPR0062MVYSSCESKEPDSVSASNHLLLNGNDELVEKSHKTGPENNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEEDEWKGKVSYRDSEIELSDASQVEKEVSAAQIAIAGEGVGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPYDIEYQIKSLIKKYICKQETINLVVVPCNVDIATTEALRMAQEVDPEGDRTIGILTKPDLVDKGTEDKIVDVARNLVFHLKKGYMIVKCRGQQDIQEQLSLAKALQKEQAFFENHAHFRDLLEEGRATIPCLAERLTSELIMHICKTLPLLENQIKESHQKITEELQKYGSDIPEDESGKMFFLIDKIDAFNSDITALIQGEELVVEYECRLFTKMRNEFCRWSAVVEKNFKNGYDAICKQIQLFENQYRGRELPGFVNYKTFETIIKKQVSVLEEPAVDMLHTVTDLVRLAFTDVSETNFNEFFNLHRTAKSKIEDIKLEQEKEAETSIRLHFQMEQIVYCQDQVYRGALQKVREKEAEEEKNRKSNQYFLSSPAPSSDPSIAEIFQHLIAYHQEVGKRISSHIPLIIQFFILRTFGQQLQKSMLQLLQNKDQYDWLLRERSDTSDKRKFLKERLMRLTQARRRLAKFPGP27594[Ref.20167191]Influenza A virus(IAV):Inhibits IAV replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. AF-P27594-F1BoMx1 inhibits the replication of members of the Rhabdoviridae and Orthomyxoviridae families. Contrary to human MxA, however, Sendai, bovine and human parainfluenza-3, and measles viruses are resistant to boMx1. 20167191,Palm M, Garigliany MM, Cornet F, Desmecht D.cInterferon-induced Sus scrofa Mx1 blocks endocytic traffic of incoming influenza A virus particles. DRAVPR0063MVHSDLGIEELDSPESSLNGSEDMESKSNLYSQYEEKVRPCIDLIDSLRSLGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLGNEDEWKGKVSFLDKEIEIPDASQVEKEISEAQIAIAGEGTGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPPDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQEVDPQGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQDIKHRMSLDKALQRERIFFEDHAHFRDLLEEGKATIPCLAERLTSELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFCLIEKIDTFNKEIISTIEGEEFVEQYDSRLFTKVRAEFSKWSAVVEKNFEKGYEAIRKEIKQFENRYRGRELPGFVNYKTFETIIKKQVRVLEEPAVDMLHTVTDIIRNTFTDVSGKHFNEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKNKKSNHYFQSQVSEPSTDEIFQHLTAYQQEVSTRISGHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLERLTRARQRLAKFPGBos taurus (Bovine)P79135RABVZ[Ref.16202617]rabies virus(RABV):bovine Mx1 can interfere the replication of rabies virus. AF-P79135-F116202617##22385204=Leroy M, Pire G, Baise E, Desmecht D.##Dermine M, Desmecht D.Expression of the interferon-alpha/beta-inducible bovine Mx1 dynamin interferes with replication of rabies virus.##In Vivo modulation of the innate response to pneumovirus by type-I and -III interferon-induced Bos taurus Mx1. Anti-RABV DRAVPR0064MVLSTEENTGVDSVNLPSGETGLGEKDQESVNNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKLNEGEEWRGKVSYDDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDRGTEDKVVDVVRNLVYHLKKGYMIVKCRGQQDIQEQLSLTEALQNEQIFFKEHPHFRVLLEDGKATVPCLAERLTAELISHICKSLPLLENQIKESHQSASEELQKYGMDIPEDDSEKTFFLIEKINAFNQDITALVQGEENVAEGECRLFTRLRKEFLSWSKEIEKNFAKGYAVLYNEVWAFEKQYRGRELPGFVNYKTFENIIRRQIKTLEEPAIEMLHTVTEIVRAAFTSVSEKNFSEFYNLHRTTKSKLEDIRLEQEKEAEMSIRLHFKMEQIIYCQDQIYRGALQKVREEEAEEEKKTKHGTSSSSQSQDLQTSSMAEIFQHLNAYRQEAHNRISSHVPLIIQYFILKMFAERLQKGMLQLLQDKDSCSWLLKEQSDTSEKRKFLKERLARLAQARRRLAKFPGQ9WVP9Mx2VSV,HNTV[Ref.21166595]vesicular stomatitis virus(VSV)/Hantaan virus(HNTV):exhi< bits antiviral activity against VSV and HNTV.##[Ref.11266216]Hantavirus(HNTV):When the Mx2 gene was constitutively expressed in transfected Vero cells, it prvented the accumulation of viral transcripts and proteins of hantaviruses.##[Ref.10233954]vesicular stomatitis virus(VSV):Mx2 inhibits the replication of VAV. AF-Q9WVP9-F121166595##11266216##10233954Haller O, Kochs G.##Jin HK, Yoshimatsu K, Takada A, Ogino M, Asano A, Arikawa J, Watanabe T. ##Jin HK, Takada A, Kon Y, Haller O, Watanabe T.NHuman MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.##Mouse Mx2 protein inhibits hantavirus but not influenza virus replication.##Identification of the murine Mx2 gene: interferon-induced expression of the Mx2 protein from the feral mouse gene confers resistance to vesicular stomatitis virus. Anti-VSV,HNTV DRAVPR0065MVLSTEENRSVDLVNLPSVPLPDGEAGVGENNKDSLNNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEVELSDPSEVEEAINTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLITNYIQKQETINLVVVPSNVDIATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRALLEDGKATVPCLAERLTMELISHICKSLPLLENQIKESHQSTSEELQKYGADIPEDENEKTLFLIEKINAFNQDITAIVEGEEIVREKECRLFTKLRKEFFLWSEEIERNFQKGSDALYKEVYTFEMQYRGRELPGFVNYKTFENIIRRQIKTLEEPAMEMLHKVTEIVRAAFTTVSEKNFSEFFNLHRTTKSKLEDIRLEQETEAEKSIRLHFQMEQIIYCQDQIYRKALQKVREEEAEEEERKHGKSRSSQSKNLQTSSMDEIFQHLNAYRQEAHNRISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEHSDTSEKRRFLKERLARLAQAQRRLAKFPGP18589VSVQ[Ref.2173790]vesicular stomatitis virus(VSV):Mx2 inhibits the replication of VSV. AF-P18589-F1Obovine Mx1 protein participates in antiviral activity against the rabies virus.2173790'Meier E, Kunz G, Haller O, Arnheiter H.2Activity of rat Mx proteins against a rhabdovirus.Anti-VSV DRAVPR0066MSMSFRPLKYKRHTQTSTQHHPKQDIYFHQQPPGPPLGQTMSPPQWQVEESNPDFLPNNFNQLNLDPQQPEAKGGQQMSKGPENNLYRKYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIITRCPLVLKLTKRECEWTGKITYRNITQQLQNPSEVEWEIRRAQNIIAGNGLGISHELINLEITSPEVPDLTLIDLPGITRVAVENQPQDIGLQIKALIKKYIQRQETINLVVVPCNVDIATTEALSMAQEVDPDGDRTIGILTKPDLVDKGTEKGVLKVMQNLTYHLKKGYMIVKCRGQQDITNKLSLAEATRKETMFFETHPYFRILLDEGKATVPLLAERLTTELIWHINKSLPLLENQIKEKHQRATEELQQYGDDIPSDEGDKMFFLIEKIKVFNEDIGKLIEGEEIVMETESRLCNKIREEFTSWILILTTNIEKVKSILNEEVSKYEKKYRGKELLGFVNYKTFETVVKHYLGQLIDPALKMLQKAMEIVWQTFKDTAKKHFAEFCNLHQTVQNKIEDIKTKQMAEAANLIQLQFRMEKLVFCQDQIYGVVLNKVREDIFNSMGKASETPQSKQPFLNDQSSISSIVEIGVHLNAYFMETSKRLANQIPFIIQYFMLQENGDKVQKAMMQLLQDTQHYSWLLQEQSDTATKRKFLKEKIFRLTQAQQALYEFPHFKGQ9BDI7[Ref.17119954]vesicular stomatitis virus(VSV):bovine Mx1 protein confers antiviral activity against vesicular stomatitis virus (VSV). AF-Q9BDI7-F117119954PBabiker HA, Nakatsu Y, Yamada K, Yoneda A, Takada A, Ueda J, Hata H, Watanabe T.IBovine and water buffalo Mx2 genes: polymorphism and antiviral activity. DRAVPR0067MPKPRMSWPYQRHRQASSPPHPHKEMNFFPQQPLPLGAGPGQMTFPLNWQMGGKDLTKGLNMLTLSPQQPGGKSGQQTSKGPENNLYSPFEEKVRPCIDLIDSLRALGVEQDLALPTIAVIGDQSSGKSSVLEALSGVPLPRGSGIITRCPLALRLKKKECPWQGRISYRKVELQLQDPSQVEREIRKAQDAIAGSGVGISHELISLEVTSPEVPDLTLIDLPGITRVAVGNQPQDIGLQIKALIRKYIQEQQTINLVVVPCNVDIATTEALRMAQEVDPEGDRTIGILTKPDLVDTGAEKVVLNVMQNLTYHLKKGYMIVKCRGQQEILNKLSLAEATKREIAFFHSHPHFRILLEEGKATVPRLAERLTVELIGHISKSLPLLFSQIKEIHQSATEELRLCGASVPSNDADKMFFLIEKIKVFNQDIENLAEGEEIVKEKEARLYNKIREEFKSWIVTLDCNSKKVKNIIHEEVSKYDRQYRGKELMGFVSYKTFESIVRQYLEELVDPALGMLQTVVEIVRQTFSDTAQKNFGEFSNLNQTTQNKVDSIAARAAERAEGLIRLQFRMEQLVFCQDDIYRVDLKAVREELFNPVAEHPQSLQLRLPFVNGPSPVSSITEIGVHVNAYFMGTSQRLANQIPFIIQYCVLQESRDHLQKAMMQMLQGREQYSWLLQEESHTSAKRHFLKEKIHRLAEARHTLSKFAQSLQGA7VK00t[Ref.18977535]Influenza A virus:porcine Mx2 inhibition of multiplication of influenza virus A/WSN/33 and A/Udorn/72. AF-A7VK00-F118977535Morozumi T, Naito T, Lan PD, Nakajima E, Mitsuhashi T, Mikawa S, Hayashi T, Awata T, Uenishi H, Nagata K, Watanabe T, Hamasima N.;Molecular cloning and characterization of porcine Mx2 gene. DRAVPR0068MSKAHGSRPYRRHNVVIPRQQPEKEMNFVQQQPPPSDAAARQMMYPPNCQVGVQDPVYLAKEFNLLTLNPQQLEGSRHQQMAKGPEKSLYSQYEQKVRPCIDLVDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKRDPHKAWRG< RISYRKTELQFQDPSQVEKEIRQAQNIIAGQGLGISHELISLEITSPEVPDLTLIDLPGITRVAVGNQPQDIGVQIKALIKNYIQKQETINLVVVPCNVDIATTEALSMAQEVDPNGDRTIGVLTKPDLVDRGTEKTVVNVAQNLTYHLQKGYMIVRCRGQEEITNQLSLAEATEKERMFFQTHPYFRALLEEGKATVPCLAERLTKELILHINKSLPLLEKQIRESHQRATDELHQCGDSIPSNEADKMFFLIEKIKLFNQDIDKLIEGEEIVKKNETRLYNKIREEFEHWALVLTANTQKVKNIVSEEVSVYEKQYRGKELLGFVNYKTFETIVHQYIEQLVEPALTMLRKTIEIVWQAFTDTAKKHFSVFSNLSQTIQNKIEDIKTRQAETAENLIRLQFRMEQLVYCQDQIYSVVLRKVRKEVFNPAGKAAQDLQLKFPFPKDLPSMSSNDEIGVHLNAYFLETSKRLANQIPFIIQYFVLQENGSCLQKAMMQILQEREQYSWLLQEHADTSAKRRFLKEKIYRLAQARRALYMFFS/Canis lupus familiaris (Dog) (Canis familiaris)Q9N0Y2[Ref.15767791]vesicular stomatitis virus (VSV):Mx2 had an antiviral activity against recombinant vesicular stomatitis virus (VSV). AF-Q9N0Y2-F1The protein target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). 15767791?Nakamura T, Asano A, Okano S, Ko JH, Kon Y, Watanabe T, Agui T.HIntracellular localization and antiviral property of canine Mx proteins. DRAVPR0069MTDPEVFCFITKILCAHGGRMTLEELLGEISLPEAQLYELLKAAGPDRFVLLETGDQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQVLKNHELSGLNQEELAVLLVQSDPFFMPEICKSYKGEGRKQICGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLAIMREHGLSSDVVQNIQDICNNKHTRRNPPSMRAPHPHRRGGAHRDRSKSRDRFHHNSLEVLSTVSPLGSGPPSPDVTGCKDPLEDVSADVTQKFKYLGTQDRAQLSSVSSKAAGVRGPSQMRASQEFLEDGDPDGLFSRNRSDSSTSRTSAAGFPLVAAQRNEAGAMKMGMPSGHHVEVKGKNEDIDRVPFLNSYIDGVTMEEATVSGILGKRATDNGLEEMILSSNHQKSVAKTQDPQTAGRITDSGQDTAFLHSKYEENPAWPGTSTHNGPNGFSQIMDETPNVSKSSPTGFGIKSAVTGGKEAVYSGVQSLRSHVLAMPGETTTPVQGSNRLPPSPLSSSTSHRVAASGSPGKSSTHASVSPASEPSRMMMMMSDPAEYSLCYIVNPVSPRMDDHGLKEICLDHLYRGCQQVNCNKNHFHLPYRWQLFILPTWMDFQDMEYIERAYCDPQIEIIVIEKHRINFKKMTCDSYPIRRLSTPSFVEKTLNSVFTTKWLWYWRNELNEYTQYGHESPSHTSSEINSAYLESFFHSCPRGVLQFHAGSQNYELSFQGMIQTNIASKTQRHVVRRPVFVSSKDVEQKRRGPDHQPVMPQADALTLFSSPQRNASTVSSNEYEFIELNNQDEEYAKISEQFKASMKQFKIVTIKRIWNQKLWDTFERKKQKMKNKTEMFLFHAVGRIHMDYICKNNFEWILHGNREIRYGKGLCWRRENCDSSHAHGFLEMPLASLGRTASLDSSGLQRK2Zinc finger CCCH-type antiviral protein 1(PARP-13)Q3UPF5Zc3hav16L1W,[Ref.21102435]PARP-13 inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. AF-Q3UPF5-F1Rat ZAP exhibits antiviral activity against diverse viruses including, in addition to alphaviruses, Moloney murine leukemia virus (MLV) and Ebola virus.`$Phosphorylation of Ser at position 257,262,265,269,273,324,350,425,553,583,680.a$Phosphorylation of Thr at position 277.b$Phosphorylation of Tyr at position 508.21102435Hayakawa S, Shiratori S, Yamato H, Kameyama T, Kitatsuji C, Kashigi F, Goto S, Kameoka S, Fujikura D, Yamada T, Mizutani T, Kazumata M, Sato M, Tanaka J, Asaka M, Ohba Y, Miyazaki T, Imamura M, Takaoka A.hZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses. DRAVPR0070MADPGVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQILKNHELSGLNQEELACLLVQSDPFFLPEICKSYKGEGRKQTCGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLTIMREHGLSPDVVQNIQDICNNKHARRNPPGTRAAHPHRRGGAHRDRSKSRDRFLHNSLEFLSPVVSPLGSGPPSPDVTSCKDSLEDVSVDVTQKFKYLGTHDRAQLSPVSSKAAGVQGPSQMRASQEFSEDGNLDDIFSRNRSDSSSSRASAAKVAQRNEAVAMKMGMEVKGKKEAPDIDRVPFLNSYIDGVTMEKASVSGIPGKKFTANDLENLLLLNDTWKNVAKPQDLQTTGRITDSGQDKAFLQNKYGGNPVWASASTHNAPNGSSQIMDETPNVSKSSTSGFAIKPAIAGGKEAVYSGVQSPRSQVLAVPGEATTPVQSNRLPQSPLSSSSHRAAASGSPGKNSTHTSVSPAIESSRMTSDPDEYLLRYILNPLFRMDNHGPKEICQDHLYKGCQQSHCDRSHFHLPYRWQMFVYTTWRDFQDMESIEQAYCDPHVELILIENHQINFQKMTCDSYPIRRLSTPSYEEKPLSAVFAT< KWIWYWKNEFNEYIQYGNESPGHTSSDINSAYLESFFQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHVVRRPVFVSSNDVEQKRRGPE.Zinc finger CCCH-type antiviral protein 1(ZAP)Rattus norvegicus (Rat) Q8K3Y63U9GSINV,EBOV,MARV[Ref.17928353]sindbis virus (SINV):ZAP inhibited translation of the incoming viral RNA.##[Ref.17182693]Ebola virus (EBOV)/Marburg virus (MARV):ZAP has an antiviral effect against EBOV and MARV in cell culture. AF-Q8K3Y6-F1The zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, including Moloney murine leukemia virus (MoMLV), HIV-1, and certain alphaviruses and filoviruses.`$Phosphorylation of Ser at position 257,262,266,270,274,283,325,351,398,544,667.a$Phosphorylation of Thr at position 278.b$Phosphorylation of Tyr at position 501.17928353##17182693tMacDonald MR, Machlin ES, Albin OR, Levy DE.##Mller S, Mller P, Bick MJ, Wurr S, Becker S, Gnther S, Kmmerer BM.The zinc finger antiviral protein acts synergistically with an interferon-induced factor for maximal activity against alphaviruses.##Inhibition of filovirus replication by the zinc finger antiviral protein.Anti-SINV,Anti-EBOV,Anti-MARV DRAVPR0071MADPEVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVATTRARVCRRKYCQRPCDNLHLCKLNLLGRCNYSQSERNLCKYSHEVLSEENFKVLKNHELSGLNKEELAVLLLQSDPFFMPEICKSYKGEGRQQICNQQPPCSRLHICDHFTRGNCRFPNCLRSHNLMDRKVLAIMREHGLNPDVVQNIQDICNSKHMQKNPPGPRAPSSHRRNMAYRARSKSRDRFFQGSQEFLASASASAERSCTPSPDQISHRASLEDAPVDDLTRKFTYLGSQDRARPPSGSSKATDLGGTSQAGTSQRFLENGSQEDLLHGNPGSTYLASNSTSAPNWKSLTSWTNDQGARRKTVFSPTLPAARSSLGSLQTPEAVTTRKGTGLLSSDYRIINGKSGTQDIQPGPLFNNNADGVATDITSTRSLNYKSTSSGHREISSPRIQDAGPASRDVQATGRIADDADPRVALVNDSLSDVTSTTSSRVDDHDSEEICLDHLCKGCPLNGSCSKVHFHLPYRWQMLIGKTWTDFEHMETIEKGYCNPGIHLCSVGSYTINFRVMSCDSFPIRRLSTPSSVTKPANSVFTTKWIWYWKNESGTWIQYGEEKDKRKNSNVDSSYLESLYQSCPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDVIRRPTFVPQWYVQQMKRGPDHQPAKTSSVSLTATFRPQEDFCFLSSKKYKLSEIHHLHPEYVRVSEHFKASMKNFKIEKIKKIENSELLDKFTWKKSQMKEEGKLLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNCPYDAKNVVMFVAQVLVGKFTEGNITYTSPPPQFDSCVDTRSNPSVFVIFQKDQVYPQYVIEYTEDKACVIS)Zinc finger CCCH-type antiviral protein 1Q7Z2W4ZC3HAV1"2X5Y##4X52##6UEI##6UEJ##7KZH##7TGQ XMRV,HIV-1r[Ref.22720057]Xenotropic murine leukemia virus-related virus (XMRV):ZAP inhibits XMRV replication by preventing the accumulation of viral mRNA in the cytoplasm.##[Ref.21876179]Human immunodeficiency virus type 1(HIV-1):ZAP inhibits HIV-1 by recruiting both the 52 and 32 mRNA degradation machinery to specifically promote the degradation of multiply spliced HIV-1 mRNAs. AF-Q7Z2W4-F1human OAS3 exhibits antiviral activity against alphaviruses, such as the Chikungunya virus, the Sindbis virus, and the Semliki Forest virus,`$Phosphorylation of Ser at position 257,263,267,271,275,284,302,327,335,355,378,387,407,469,492,494,572,590.a$Phosphorylation of Thr at position 554,393.b$The N-terminal is Acetylation.22720057##21876179dWang X, Tu F, Zhu Y, Gao G.##Zhu Y, Chen G, Lv F, Wang X, Ji X, Xu Y, Sun J, Wu L, Zheng YT, Gao G. Zinc-finger antiviral protein inhibits XMRV infection.##Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation.Anti-XMRV,Anti-HIV-1 DRAVPR0072?MDLYSTPAAALDRFVARRLQPRKEFVEKARRALGALAAALRERGGRLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYVDQRARRAEILSEMRASLESWWQNPVPGLRLTFPEQSVPGALQFRLTSVDLEDWMDVSLVPAFNVLGQAGSGVKPKPQVYSTLLNSGCQGGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQVCLQGLWKETLPPVYALELLTIFAWEQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLAQEAASCYDHPCFLRGMGDPVQSWKGPGLPRAGCSGLGHPIQLDPNQKTPENSKSLNAVYPRAGSKPPSCPAPGPTGAASIVPSVPGMALDLSQIPTKELDRFIQDHLKPSPQFQEQVKKAIDIILRCLHENCVHKASRVSKGGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPRRAEILDEMRAQLESWWQDQVPSLSLQFPEQNVPEALQFQLVSTALKSWTDVSLLPAFDAVGQLSSGTKPNPQVYSRLLTSGCQEGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGKGPAPASLPPAYALELLTIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHGSWELLAQEAAALGMQACFLSRDGTSVQPWDVMPALLYQTPAGDLDKFISEFLQPNRQFLAQVNKAVDTICSFLKENCFRNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGNKRAEIISEIRAQLEACQQERQFEVKFEVSKW< ENPRVLSFSLTSQTMLDQSVDFDVLPAFDALGQLVSGSRPSSQVYVDLIHSYSNAGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKISKGRGSLPPQHGLELLTVYAWEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNARWDLLAKEAAACTSALCCMGRNGIPIQPWPVKAAV2'-5'-oligoadenylate synthase 3Q9Y6K5OAS34S3N DENV,CHIKV[Ref.19923450]dengue virus(DENV):The antiviral effects of human OAS3 p100 correlate with their abilities to trigger RNase L activation in DEN-2-infected cells.##[Ref.19056102]Chikungunya virus(CHIKV):OAS3 exhibits antiviral effect by blocking the early stage of virus replication. AF-Q9Y6K5-F1OASL possesses two domains with HCV inhibitory activity. The OAS-homology domain without OAS activity is inhibitory for cell growth as well as HCV replication, whereas C-terminal Ub is inhibitory only for HCV replication.'Phosphorylation of Thr at position 365.19923450##19056102~Lin RJ, Yu HP, Chang BL, Tang WC, Liao CL, Lin YL.##Brhin AC, Casadmont I, Frenkiel MP, Julier C, Sakuntabhai A, Desprs P.Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection.##The large form of human 2',5'-Oligoadenylate Synthetase (OAS3) exerts antiviral effect against Chikungunya virus. Anti-DENV,CHIKV DRAVPR0073MALMQELYSTPASRLDSFVAQWLQPHREWKEEVLDAVRTVEEFLRQEHFQGKRGLDQDVRVLKVVKVGSFGNGTVLRSTREVELVAFLSCFHSFQEAAKHHKDVLRLIWKTMWQSQDLLDLGLEDLRMEQRVPDALVFTIQTRGTAEPITVTIVPAYRALGPSLPNSQPPPEVYVSLIKACGGPGNFCPSFSELQRNFVKHRPTKLKSLLRLVKHWYQQYVKARSPRANLPPLYALELLTIYAWEMGTEEDENFMLDEGFTTVMDLLLEYEVICIYWTKYYTLHNAIIEDCVRKQLKKERPIILDPADPTLNVAEGYRWDIVAQRASQCLKQDCCYDNRENPISSWNVKRARDIHLTVEQRGYPDFNLIVNPYEPIRKVKEKIRRTRGYSGLQRLSFQVPGSERQLLSSRCSLAKYGIFSHTHIYLLETIPSEIQVFVKNPDGGSYAYAINPNSFILGLKQQIEDQQGLPKKQQQLEFQGQVLQDWLGLGIYGIQDSDTLILSKKKGEALFPAS*2'-5'-oligoadenylate synthase-like proteinQ15646OASL 1WH3##4XQ7b[Ref.20074559]Hepatitis C virus(HCV):OASL is inhibitory to HCV repllication in HCV replicon cells. AF-Q15646-F12Acetylation of Ala at position 2(N-acetylalanine).20074559Ishibashi M, Wakita T, Esumi M.2',5'-Oligoadenylate synthetase-like gene highly induced by hepatitis C virus infection in human liver is inhibitory to viral replication in vitro. DRAVPR0074MNATHCILALQLFLMAVSGCYCHGTVIESLESLNNYFNSSGIDVEEKSLFLDIWRNWQKDGDMKILQSQIISFYLRLFEVLKDNQAISNNISVIESHLITTFFSNSKAKKDAFMSIAKFEVNNPQVQRQAFNELIRVVHQLLPESSLRKRKRSRCInterferon gamma(IFN-gamma)P01580Ifng[Ref.8456301]Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antiviral responses by activating effector immune cells and enhancing antigen presentation. AF-P01580-F1$TRIM56 exhibits a broad antiviral activity against bovine viral diarrhea virus (BVDV), yellow fever virus (YFV), dengue virus serotype 2 (DENV2), human coronavirus virus (HCoV), and influenza A and B viruses.TRIM56 had no effect on the replication of vesicular stomatitis virus (VSV) and HCV.'Glycosylation of Asn at position 38,90.8456301cHuang S, Hendriks W, Althage A, Hemmi S, Bluethmann H, Kamijo R, Vilcek J, Zinkernagel RM, Aguet M.AImmune response in mice that lack the interferon-gamma receptor. DRAVPR0075MVSQGSSPSLLEALSSDFLACKICLEQLRVPKTLPCLHTYCQDCLAQLAEGSRLRCPECRESVPVPPAGVAAFKTNFFVNGLLDLVKARAGGDLRAGKPACALCPLMGGASAGGPATARCLDCADDLCQACADGHRCTRQTHSHRVVDLVGYRAGWYDEEARERQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPLAEAVRARRPGLEELLAGVDNNLAELEATRLAEKEALARLREQAAKVVTQVEEASERVLRALLAQKQEVLGQLRAHVEAAEEGARERLGELEGQEQVAREAAAFARRVLSLGREAEILSLEGAIAQRLRQLQGCPWVPGPAPCQLPQLELYPGLLDKNCHLLRLSFEEQLPQKDSGKDGARSQGGDATQPQSRDGVQTPNQEDGAKTPKESRAQTPQEDGGTQARVGSRSNKKRKFKGRLKSVSREPSPAPGPNLEGSGLLPRPIFFCSFPTRMPGDKRAPRITGLCPFGSREILVADEQNRALKRFSLNGDYRGAVPVPEGCSPCSVAALQDTVAFSAAARLYLINHNGEVQWRRALSLCQASHAVAAMPSGDRVAVSVSGHVEVYNMEGSLATRFIPGGKANRGLRALVFLTTSPQGHFVGSDWQQNSLVVCDGLGQVVGEYRGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGRYLVVSLSNGTIHVFRVRPLDS"E3 ubiquitin-protein ligase TRIM56E1BD59TRIM56BVDV[Ref.21289118]bovine viral diarrhea virus (BVDV):TRIM56 inhibits BVDV propagation by acting on intracellular viral RNA replication. AF-E1BD59-F1X`$Phosphorylation of Ser at position<  452.a$Phosphorylation of Thr at position 402 and 419.21289118##27667714_Wang J, Liu B, Wang N, Lee YM, Liu C, Li K.##Fan W, Wu M, Qian S, Zhou Y, Chen H, Li X, Qian P.TRIM56 is a virus- and interferon-inducible E3 ubiquitin ligase that restricts pestivirus infection.##TRIM52 inhibits Japanese Encephalitis Virus replication by degrading the viral NS2A. Anti-BVDV DRAVPR0076MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK2'-5'-oligoadenylate synthase 2E9Q9A9Oas2p[Ref.12396720]2',5'-Oligoadenylate synthetase (2-5OAS) is one of the interferon (IFN)-induced proteins and mediates the antiviral action of IFN.##[Ref.21142819]The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. AF-E9Q9A9-F1Y`$The Gly at position 2 indicates N-myristoyl glycine.a$Acetylation of Lys at position 417.12396720##21142819bKakuta S, Shibata S, Iwakura Y.##Kristiansen H, Gad HH, Eskildsen-Larsen S, Despres P, Hartmann R.Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene family.##The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. DRAVPR0077MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIYRELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLTSPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSFDVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPKGSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNFP29728OAS2[Ref.21142819]The 2'-5' oligoadenylate synthetases (OAS) can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL.Y`$The Gly at position 2 indicates N-myristoyl glycine.a$Acetylation of Lys at position 378.21142819AKristiansen H, Gad HH, Eskildsen-Larsen S, Despres P, Hartmann R.dThe oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. DRAVPR0078qMGCNVMMELDYGGRAAWLAFHITNFDRSDLETILRGARVCNTWQDQRLSVYLVGRDCNLLRPFVQAAKFIHNTRRGQTLTHWFTKNIVFSSTGQETEPPIDPTCELLVELISGNon-structural protein 1(Murine pneumonia virus (strain 15) (MPV)P288881C(NS1)\[Ref.19052095]NS1 may serve some inhibitory role in viral transcription and RNA replication.19052095EBuchholz UJ, Ward JM, Lamirande EW, Heinze B, Krempl CD, Collins PL. Deletion of nonstructural proteins NS1 and NS2 from pneumonia virus of mice attenuates viral replication and reduces pulmonary cytokine expression and disease. DRAVPR0079MDTLVEDDICILNHEKAHRREAVTPLSAYPGDESVASHFALVTAYEDIKKRLKDSEKENSFLKKRIRALEERLVGARADEETSSVGREQVNKAYHAYREVCIDRDNLKNQLEKINKDNSESLKMLNEQLQSKEVELLQLRTEVETQQVMRNLNPPSSSWEVEKLSCDLKIHGLEQELGLLRKECSDLRTELQKARQTGPPQEDILQGRDVIRPSLSREEHVPHQGLHHSDNMQHAYWELKREMSNLHLVTQVQAELLRKLKTSAAVKKACTPVGCVEDLGRDSTKLHLTNFTATYKRHPSLSPNGKAPCYAPSSPLPGDRKVFSDKAVLQSWTDNERLVPNDGADFPEHSSYGRNSLEDNSWVFPSPPKSSETAFGENKSKILPLSNLPPLHYLDQQNQNCLYKS< %5-azacytidine-induced protein 2(Nap1)Q9QYP6Azi2T[Ref.17568778]Nap1 binds TBK1 and IKBKE playing a role in antiviral innate immunity. AF-Q9QYP6-F1+Phosphorylation of Ser at position 331,366.17568778Ryzhakov G, Randow F.iSINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK. DRAVPR0080MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE$NF-kappa-B essential modulator(NEMO)Q9Y6K9IKBKG2JVX##3BRV##4BWN##6MI3[Ref.20724660]TRIM23-mediated ubiquitin conjugation to NEMO is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. AF-Q9Y6K9-F1rAntiviral activity depends on K27-linked polyubiquitin conjugation to multiple sites of NEMO by TRIM23 expression.7Phosphorylation of Ser at position 31,43,68,85,376,387.20724660`Arimoto K, Funami K, Saeki Y, Tanaka K, Okawa K, Takeuchi O, Akira S, Murakami Y, Shimotohno K.jPolyubiquitin conjugation to NEMO by triparite motif protein 23 (TRIM23) is critical in antiviral defense. DRAVPR0081SMAPEIHMTGPMCLIENTNGELVANPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKNKGFSLGSTVKSHTKGIWMWCVPHPKKPEHTLVLLDTEGLGDVKKGDNQNDSWIFTLAVLLSSTLVYNSMGTINQQAMDQLYYVTELTHRIRSKSSPDENENEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLEYSLKLTQGTSQKDKNFNLPRLCIRKFFPKKKCFVFDLPIHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIKVNGPRLESLVLTYINAISRGDLPCMENAVLALAQIENSAAVQKAIAHYDQQMGQKVQLPAETLQELLDLHRVSEREATEVYMKNSFKDVDHLFQKKLAAQLDKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYCLFIQKLQDLEKKYYEEPRKGIQAEEILQTYLKSKESVTDAILQTDQILTEKEKEIEVECVKAESAQASAKMVEEMQIKYQQMMEEKEKSYQEHVKQLTEKMERERAQLLEEQEKTLTSKLQEQARVLKERCQGESTQLQNEIQKLQKTLKKKTKRYMSHKLKI"Guanylate-binding protein 3(GBP-3)Q9H0R5GBP3influenza virus[Ref.22106366]influenza virus:GBP-3 mediates anti-influenza activity through inhibition of viral transcription and replication. AF-Q9H0R5-F1221063667Nordmann A, Wixler L, Boergeling Y, Wixler V, Ludwig S.A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication.Anti-influenza virus DRAVPR0082PMASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTISGuanylate-binding protein 1P32455GBP11DG3##1F5N##2B8W##6K1Z[Ref.22106366]influenza virus:GBP-1 mediates anti-influenza activity through inhibition of viral transcription and replication. AF-P32455-F16The Cys at position 589 indicates S-farnesyl cysteine. DRAVPR0083WMSGPCGEKPVLEASPTMSLWEFEDSHSRQGTPRPGQELAAEEASALELQMKVDFFRKLGYSSTEIHSVLQKLGVQADTNTVLGELVKHGTATERERQTSPDPCPQLPLVPRGGGTPKAPNLEPPLPEEEKEGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTLEHRKQPCPYGRKCTYGIKCRFFHPERPSCPQRSVADELRANALLSPPRAPSKDKNGRRPSPSSQSSSLLTESEQCSLDGKKLGAQASPGSRQEGLTQTYAPSGRSLAPSGGSGSSFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFSVPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRSPWGRAGSLAKEQASVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHPSE Endoribonuclease ZC3H12A(MCPIP1)Q5D1E8ZC3H12A3V32##3V33##3V34 HIV,JEV,DENV0[Ref.24191027]Human immunodeficiency virus type 1(HIV-1):MCPIP1 exhibits antiviral activity agains< t HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA species.##[Ref.23355615]Japanese encephalitis virus (JEV)/dengue virus (DENV):MCPIP1 inhibits virus replication by binding to viral RNA. AF-Q5D1E8-F1MCPIP1 inhibited DENV2, encephalomyocarditis virus (EMCV), Yellow fever virus-vaccine strain 17D (YFV-17D), and the human coronavirus OC43 (HCoV-OC43), but it had a marginal effect or no effect on VSV, HSV-1, and new castle diseases virus (NDV)2Phosphorylation of Ser at position 99,344,438,442.24191027##23355615Liu S, Qiu C, Miao R, Zhou J, Lee A, Liu B, Lester SN, Fu W, Zhu L, Zhang L, Xu J, Fan D, Li K, Fu M, Wang T.##Lin RJ, Chien HL, Lin SY, Chang BL, Yu HP, Tang WC, Lin YL. MCPIP1 restricts HIV infection and is rapidly degraded in activated CD4+ T cells.##MCPIP1 ribonuclease exhibits broad-spectrum antiviral effects through viral RNA binding and degradation.Anti-HIV,Anti-JEV,Anti-DENV DRAVPR0084]MMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN8Nuclear factor erythroid 2-related factor 2(HEBP1,Nrf-2)Q16236 NFE2L2(NRF2)(2FLU##2LZ1##4IFL##5WFV##7K2A##7K2E##7O7B[Ref.33009401]SARS-CoV2:when NRF2 was activated, it limits the release of pro-inflammatory cytokines in response to SARS-CoV-2 infection inhibits SARS-CoV-2 replication. AF-Q16236-F1The inhibitory effect extends to the replication of several other pathogenic viruses including Herpes Simplex Virus-1 and-2, Vaccinia virus, and Zika virus through a type I interferon (IFN)-independent mechanism.`$Phosphorylation of Ser at position 40,215.a$Glycosylation of Lys at position 462,472,487,574.b$Glycosylation of Arg at position 499,569.c$The Lys at position 596 and 599 indicates N6-acetyllysine.33009401Olagnier D, Farahani E, Thyrsted J, Blay-Cadanet J, Herengt A, Idorn M, Hait A, Hernaez B, Knudsen A, Iversen MB, Schilling M, Jrgensen SE, Thomsen M, Reinert LS, Lappe M, Hoang HD, Gilchrist VH, Hansen AL, Ottosen R, Nielsen CG, Mller C, van der Horst D, Peri S, Balachandran S, Huang J, Jakobsen M, Svenningsen EB, Poulsen TB, Bartsch L, Thielke AL, Luo Y, Alain T, Rehwinkel J, Alcam A, Hiscott J, Mogensen TH, Paludan SR, Holm CK.SARS-CoV2-mediated suppression of NRF2-signaling reveals potent antiviral and anti-inflammatory activity of 4-octyl-itaconate and dimethyl fumarate. DRAVPR0085MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISHFSCLKDRHDFGFPEEEFDGHQFQKAQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKDInterferon alpha-4P05014IFNA41[Ref.9334213]IFN-alpha have antiviral activities. AF-P05014-F1IThere are two disulfide bonds between Cys24 and Cys122, Cys52 and Cys162.9334213aDomanski P, Fish E, Nadeau OW, Witte M, Platanias LC, Yan H, Krolewski J, Pitha P, Colamonici OR.A region of the beta subunit of the interferon alpha receptor different from box 1 interacts with Jak1 and is sufficient to activate the Jak-Stat pathway and induce an antiviral state. DRAVPR0086MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKEInterferon alpha-2P01563IFNA2(IFNA2A, IFNA2B, IFNA2C)1ITF##2HYM##2LAG##3S9D##4Z5R1[Ref.9822609]IFN-alpha have antiviral activities. AF-P01563-F1p`$There are two disulfide bonds between Cys24 and Cys121, Cys52 and Cys161.a$Glycosylation of Thr at position 129.9822609Mari I, Durbin JE, Levy DE.|Differential viral induction of distinct interferon-alpha genes by positive feedb< ack through interferon regulatory factor-7. DRAVPR0087MTNKCLLQIALLLCFSTTALSMSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRNInterferon betaP01574IFNB11AU10[Ref.6171735]IFN-beta have antiviral activities. AF-P01574-F1`$There is a disulfide bond between Cys52 and Cys162.a$Phosphorylation of Thr at position 24.b$Glycosylation of Asn at position 101.6171735,Shepard HM, Leung D, Stebbing N, Goeddel DV.IA single amino acid change in IFN-beta1 abolishes its antiviral activity. DRAVPR0088`MAASKPVEAAVVAAAVPSSGSGVGGGGTAGPGTGGLPRWQLALAVGAPLLLGAGAIYLWSRQQRRREARGRGDASGLKRNSERKTPEGRASPAPGSGHPEGPGAHLDMNSLDRAQAAKNKGNKYFKAGKYEQAIQCYTEAISLCPTEKNVDLSTFYQNRAAAFEQLQKWKEVAQDCTKAVELNPKYVKALFRRAKAHEKLDNKKECLEDVTAVCILEGFQNQQSMLLADKVLKLLGKEKAKEKYKNREPLMPSPQFIKSYFSSFTDDIISQPMLKGEKSDEDKDKEGEALEVKENSGYLKAKQYMEEENYDKIISECSKEIDAEGKYMAEALLLRATFYLLIGNANAAKPDLDKVISLKEANVKLRANALIKRGSMYMQQQQPLLSTQDFNMAADIDPQNADVYHHRGQLKILLDQVEEAVADFDECIRLRPESALAQAQKCFALYRQAYTGNNSSQIQAAMKGFEEVIKKFPRCAEGYALYAQALTDQQQFGKADEMYDKCIDLEPDNATTYVHKGLLQLQWKQDLDRGLELISKAIEIDNKCDFAYETMGTIEVQRGNMEKAIDMFNKAINLAKSEMEMAHLYSLCDAAHAQTEVAKKYGLKPPTL,Mitochondrial import receptor subunit TOM70 O94826TOMM70 7DHG##7KDTSeVe[Ref.20628368]Tom70 is found to interact specifically with MAVS during RNA virus infection and plays an essential role in the antiviral response.##[Ref.25609812]Sendai virus:Tom70 recruits IRF3/Bax complex to the mitochondrial outer membrane through Hsp90, which thus induces the release of cytochrome c into the cytosol, initiating virus-induced apoptosis. AF-O94826-F1`$Phosphorylation of Ser at position 91,96,434.a$The N-terminal is acetylation.b$The Arg at position 71 indicates Omega-N-methylarginine.c$The Lys at position 185 indicates N6-acetyllysine.20628368##25609812mLiu XY, Wei B, Shi HX, Shan YF, Wang C.##Wei B, Cui Y, Huang Y, Liu H, Li L, Li M, Ruan KC, Zhou Q, Wang C. Tom70 mediates activation of interferon regulatory factor 3 on mitochondria.##Tom70 mediates Sendai virus-induced apoptosis on mitochondria. Anti-SeV DRAVPR0089'MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTCEInterferon-induced, double-stranded RNA-activated protein kinase(PKA)P19525EIF2AK2"1QU6##2A19##2A1A##3UIU##6D3K##6D3LHCV,MeV[Ref.23399035]Hepatitis C virus(HCV):PKA inhibits the replication od HCV in Huh7.5.1 cells.##[Ref.23115276]Measles virus(MeV):PKA exhibits antiviral activity against MeV. AF-P19525-F1Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1).PKR activation correlates with enhanced IFN induction, increased mitogen-activated protein (MAP) kinase pathway activation, reduction in virus growth, and increased cytotoxicity and apoptosis of infected cells`$Phosphorylation of Ser at position 83,242,456,542.a$The N-terminal is acetylation.b$Phosphorylation of Thr at position 88,89,90,255,258,446,451.c$Phosphorylation of Tyr at position 101,162,293.23399035##23115276bZhang L, Alter HJ, Wang H, Jia S, Wang E, Marincola FM, Shih JW, Wang RY.##Okonski KM, Samuel CE.The modulation of hepatitis C virus 1a replication by PKR is dependent on NF-kB mediated interferon beta response in Huh7.5.1 cells.##Stress granule formation induced by measles virus is protein kinase PKR dependent and impaired by RNA adenosine deaminase ADAR1. Anti-HCV,MeV DRAVPR0090MGIVEPGCGDMLTGTEPMPSDEGRGPGADQQHRFFYPEPGAQDPTDRRAGSSLGTPYSGGALVPAAPGRFLGSFAYPPRAQVAGFPGPGEFFPPPA< GAEGYPPVDGYPAPDPRAGLYPGPREDYALPAGLEVSGKLRVALSNHLLWSKFNQHQTEMIITKQGRRMFPFLSFTVAGLEPTSHYRMFVDVVLVDQHHWRYQSGKWVQCGKAEGSMPGNRLYVHPDSPNTGAHWMRQEVSFGKLKLTNNKGASNNVTQMIVLQSLHKYQPRLHIVEVNDGEPEAACSASNTHVFTFQETQFIAVTAYQNAEITQLKIDNNPFAKGFRENFESMYASVDTSVPSPPGPNCQLLGGDPFSPLLSNQYPVPSRFYPDLPGQPKDMISQPYWLGTPREHSYEAEFRAVSMKPTLLPSAPGPTVPYYRGQDVLAPGAGWPVAPQYPPKMSPAGWFRPMRTLPMDPGLGSSEEQGSSPSLWPEVTSLQPEPSDSGLGEGDTKRRRISPYPSSGDSSSPAGAPSPFDKETEGQFYNYFPN T-box transcription factor TBX21Q9JKD8 Tbx21(Tbet)5T1J[Ref.27430722]B cell specific loss of T-bet prevents control of persisting viral infection.T-bet is a universal controller of antiviral immunity across multiple immune lineages. AF-Q9JKD8-F1`$Phosphorylation of Ser at position 52,224,508.a$Phosphorylation of Tyr at position 76,117,219,265,304,525.b$Phosphorylation of Thr at position 55,302.27430722Barnett BE, Staupe RP, Odorizzi PM, Palko O, Tomov VT, Mahan AE, Gunn B, Chen D, Paley MA, Alter G, Reiner SL, Lauer GM, Teijaro JR, Wherry EJ.`Cutting Edge: B Cell-Intrinsic T-bet Expression Is Required To Control Chronic Viral Infection. DRAVPR0091_MSSGLRAADFPRWKRHIAEELRRRDRLQRQAFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPSGLHVVSVDKGSRAVLWAQPAutophagy-related protein 16-1Q8C0J2Atg16l1 6SUR## 6Y09##6ZAYt[Ref.33586810]Influenza A virus(IAV):Non canonical autophagy limits IAV infection independently of phagocytic cells. AF-Q8C0J2-F1/Phosphorylation of Ser at position 139,269,287.33586810Wang Y, Sharma P, Jefferson M, Zhang W, Bone B, Kipar A, Bitto D, Coombes JL, Pearson T, Man A, Zhekova A, Bao Y, Tripp RA, Carding SR, Yamauchi Y, Mayer U, Powell PP, Stewart JP, Wileman T.mNon-canonical autophagy functions of ATG16L1 in epithelial cells limit lethal infection by influenza A virus. DRAVPR0092MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNKBeclin-1Q14457BECN1"2P1L##4DDP##5HHE##5VAY##6HOI##7BL1SBVD[Ref.9765397]Sindbis virus:Beclin protects against infection of SBV. AF-Q14457-F1{`$Phosphorylation of Ser at position 15,30,90,93,96,.a$The N-terminal is acetylation.b$Phosphorylation of Thr at position 119.9765397RLiang XH, Kleeman LK, Jiang HH, Gordon G, Goldman JE, Berry G, Herman B, Levine B.aProtection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein.Anti-SBV DRAVPR0093MGENADGDQVMENLLQLRCHFTWKLLFENNDIPDLEVRISEQVQFLDIKNPLGMHNLLAYVRHLKGQQDEALQSLKEAEALIQSEQLSKRSLATWGNCAWLHYHRGSLAEAQIYLDKVEKVCKEFSSPFRYRLECAEMDCEEGWALLKCGGGNYKQAMACFAKALKVEPENPEYNTGYAVVAYRQDLDDNFISLEPLRKAVRLNPEDPYLKVLLALKLQDLGEHVEAEAHIEEALSSTSCQSYVIRYAAKYFRRKHRVDKALHLLNRALQASPSSGYLHYQKGLCYKQQISQLRTSRNRQPRRQDNVQELAQQAIHEFQETLKLRPTFEMAYVCMAEVQAEIHQYEEAERNFQKALNNKTLVAHIEQDIHLRYGRFLQFHKQSEDKAITLYLKGLKVEEKSFAWRKLLTALEKVAERRVCQNVHLVESTSLLGLVYKLKGQEKNALFYYEKALRLTGEMNPAF;Interferon-induced protein with tetratricopeptide repeats 1Q64282Ifit1{[Ref.22589727]West Nile virus(WNV):Ifit1 restricts replication of WNV lacking 22 -O methylation in subsets of primary cells. AF-Q64282-F1Ifit1 reportedly have antiviral activity against several viruses including human papilloma, Sindbis, vesicular stomatitis, and hepatitis C viruses.22589727kSzretter KJ, Daniels BP, Cho H, Gainey MD, Yokoyama WM, Gale M<  Jr, Virgin HW, Klein RS, Sen GC, Diamond MS.2'-O methylation of the viral mRNA cap by West Nile virus evades ifit1-dependent and -independent mechanisms of host restriction in vivo. DRAVPR0094MSTNGDDHQVKDSLEQLRCHFTWELSIDDDEMPDLENRVLDQIEFLDTKYSVGIHNLLAYVKHLKGQNEEALKSLKEAENLMQEEHDNQANVRSLVTWGNFAWMYYHMGRLAEAQTYLDKVENICKKLSNPFRYRMECPEIDCEEGWALLKCGGKNYERAKACFEKVLEVDPENPESSAGYAISAYRLDGFKLATKNHKPFSLLPLRQAVRLNPDNGYIKVLLALKLQDEGQEAEGEKYIEEALANMSSQTYVFRYAAKFYRRKGSVDKALELLKKALQETPTSVLLHHQIGLCYKAQMIQIKEATKGQPRGQNREKLDKMIRSAIFHFESAVEKKPTFEVAHLDLARMYIEAGNHRKAEENFQKLLCMKPVVEETMQDIHFHYGRFQEFQKKSDVNAIIHYLKAIKIEQASLTRDKSINSLKKLVLRKLRRKALDLESLSLLGFVYKLEGNMNEALEYYERALRLAADFENSVRQGP@Interferon-induced protein with tetratricopeptide repeats 1(P56)P09914IFIT14HOU##5UDI##6C6KHPV,HCV[Ref.19008854]human papillomaviruses(HPV):P56 inhibits the DNA helicase activity of E1 and E1-mediated HPV DNA replication. ##[Ref.21976647]Hepatitis C virus(HCV):IFITM1 inhibits HCV replication in IHH or Huh7 cells AF-P09914-F1fExhibits antiviral activity against several viruses including human papilloma and hepatitis C viruses.19008854##21976647]Terenzi F, Saikia P, Sen GC.##Raychoudhuri A, Shrivastava S, Steele R, Kim H, Ray R, Ray RB. Interferon-inducible protein, P56, inhibits HPV DNA replication by binding to the viral protein E1.##ISG56 and IFITM1 proteins inhibit hepatitis C virus replication. Anti-HPV,Anti-HCV DRAVPR0095MAWDLKVKMLGGNDFLVSVTNSMTVSELKKQIAQKIGVPAFQQRLAHQTAVLQDGLTLSSLGLGPSSTVMLVVQNCSEPLSILVRNERGHSNIYEVFLTQTVDTLKKKVSQREQVHEDQFWLSFEGRPMEDKELLGEYGLKPQCTVIKHLRLRGGGGDQCAUbiquitin-like protein ISG15Q64339Isg155CHF##5TL7##6YVA SBV,HSV-1j[Ref.17227866]Sindbs virus(SBV)/herpes virus type 1 (HSV-1):ISG15 inhibits the infection of SBV and HSV-1. AF-Q64339-F1QISG15 expression has been shown to inhibit the release of HIV-1 virions in vitro.<The Cys at position 144 and 155 indicates S-nitrosocysteine.16254333##17227866Lenschow DJ, Giannakopoulos NV, Gunn LJ, Johnston C, O'Guin AK, Schmidt RE, Levine B, Virgin HW 4th.##Lenschow DJ, Lai C, Frias-Staheli N, Giannakopoulos NV, Lutz A, Wolff T, Osiak A, Levine B, Schmidt RE, Garca-Sastre A, Leib DA, Pekosz A, Knobeloch KP, Horak I, Virgin HW 4th. Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo.##IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses. Anti-SBV,Anti-HSV-1 DRAVPR0096MHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQELLSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLAEHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRKNLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL#S-phase kinase-associated protein 2Q13309SKP21FQV##1FS2##2AST##7B5R[Ref.27194766]Hepatitis C virus (HCV):SKP2 has an antiviral activity towards HCV through the ubiquitin-mediated proteasomal degradation of hepatitis C virus non-structural protein 5A. AF-Q13309-F1j`$Phosphorylation of Ser at position 64,72,75,179.a$The Lys at position 68 and 71 indicates N6-acetyllysine.27194766PXue B, Yang D, Wang J, Xu Y, Wang X, Qin Y, Tian R, Chen S, Xie Q, Liu N, Zhu H.gISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-Dependent Degradation Pathway. DRAVPR0097MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHEADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVWFVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFFISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVVPTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEGVQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFSSerine incorporator 3Q13530SERINC3m[Ref.26416733]Human immunodeficiency virus type 1(HIV-1):SERINC3 restricts HIV-1 infectivity and r< eplication. AF-Q13530-F1HIV-1 Nef and MLV glycoGag efficiently down-regulate SERINC3 form the cell surface, which prevents their incorporation into HIV-1 virions and consequently counteracts their inhibitory effect on HIV-1 infectivity.M`$Phosphorylation of Ser at position 371.a$Glycosylation of Asn at position 34.26416733Usami Y, Wu Y, Gttlinger HG.KSERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef. DRAVPR0098MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLCLLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSLLIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFSPGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLASLYVMMTVTNWFNHVRSAFHLLPSerine incorporator 5 Q86VE9SERINC5m[Ref.26416733]Human immunodeficiency virus type 1(HIV-1):SERINC5 restricts HIV-1 infectivity and replication. AF-Q86VE9-F1HIV-1 Nef and MLV glycoGag efficiently down-regulate SERINC5 form the cell surface, which prevents their incorporation into HIV-1 virions and consequently counteracts their inhibitory effect on HIV-1 infectivity.-Glycosylation of Asn at position 113 and 183. DRAVPR0099MAWASSFDAFFKNFKRESKIISEYDITLIMTYIEENKLQKAVSVIEKVLRDIESAPLHIAVTGETGAGKSTFINTLRGVGHEEKGAAPTGAIETTMKRTPYPHPKLPNVTIWDLPGIGTTNFTPQNYLTEMKFGEYDFFIIISATRFKENDAQLAKAIAQMGMNFYFVRTKIDSDLDNEQKFKPKSFNKEEVLKNIKDYCSNHLQESLDSEPPVFLVSNVDISKYDFPKLETKLLQDLPAHKRHVFSLSLQSLTEATINYKRDSLKQKVFLEAMKAGALATIPLGGMISDILENLDETFNLYRSYFGLDDASLENIAQDLNMSVDDFKVHLRFPHLFAEHNDESLEDKLFKYIKHISSVTGGPVAAVTYYRMAYYLQNLFLDTAANDAIALLNSKALFEKKVGPYISEPPEYWEAAT-cell-specific guanine nucleotide triphosphate-binding protein 2Q3T9E4Tgtp2 7VES##7VEXw[Ref.9725230]vesicular stomatitis virus (VSV):TGTP conferred an antiviral state for the negative strand RNA virus, VSV. AF-Q3T9E4-F19TGTP has no antiviral activity against DNA virus, Herpes.9725230Carlow DA, Teh SJ, Teh HS.iSpecific antiviral activity demonstrated by TGTP, a member of a new family of interferon-induced GTPases. DRAVPR0100AT-cell-specific guanine nucleotide triphosphate-binding protein 1Q62293Tgtp1 AF-Q62293-F1 DRAVPR0101MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPICERSEHWTHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALISELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDNPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETANRKEKGELSAGNGFWILVFLGSFYNSNEPAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETLFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ"E3 ubiquitin-protein ligase TRIM11Q99PQ2Trim11_[Ref.18248090]Human immunodeficiency virus type 1(HIV-1):TRIM11 inhibits the virus entry of HIV AF-Q99PQ2-F1&Phosphorylation of Ser at position 85.182480901Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W.STRIM E3 ligases interfere with early and late stages of the retroviral life cycle. DRAVPR0102vMAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQARPQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCLVCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICLVEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQLQQEYTEMKALLDASETTSTRKIKEEEKRVNSKFDTIYQILLKKKSEIQTLKEEIEQSLTKRDEFEFLEKASKLRGISTKPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTPSSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGLEAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRVDFTEALYPAFWVFSAGATLSICSPK E3 ubiquitin/ISG15 ligase TRIM25Q14258TRIM254CFG##5EYA##5NT1##6FLN,[Ref.18248090]TRIM25 inhibits viral release. AF-Q14258-F1sTRIM25 acts as a K63 specific ubiquitin E3 ligase activating RIG-I and regulate innate immunity to viral infection.`$The Lys at position 273 and 567 indicates N6-acetyllysine.a$Phosphorylation of Tyr at position 278.b$Phosphorylation of Thr at position 91.c$< Phosphorylation of Ser at position 100. DRAVPR0103CMAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP(Transcription intermediary factor 1-betaQ13263TRIM281FP0##2RO1##6H3A##6QU1MLV[Ref.18248090]murine leukemia virus (MLV):TRIM28 restricts MLV in cells of germline origin by inhibiting LTR-driven transcription. AF-Q13263-F1`TRIM28 was shown to repress transcription from a retroviral promoter by binding to proviral DNA./`$The Lys at position 266,304,340,377,770,779 indicates N6-acetyllysine.a$Phosphorylation of Tyr at position 755.b$Phosphorylation of Thr at position 498,541.c$Phosphorylation of Ser at position 19,26,50,138,417,437,439,453,471,473,479,489,501,594,683,689,697,752,757,784,824.d$The N-terminal is acetylation.18248090##18389079RUchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W.##Barr SD, Smiley JR, Bushman FD.TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.##The interferon response inhibits HIV particle production by induction of TRIM22. Anti-MLV DRAVPR0104MAAAAASHLNLDALREVLECPICMESFTEEQLRPKLLHCGHTICRQCLEKLLASSINGVRCPFCSKITRITSLTQLTDNLTVLKIIDTAGLSEAVGLLMCRSCGRRLPRQFCRSCGLVLCEPCREADHQPPGHCTLPVKEAAEERRRDFGEKLTRLRELMGELQRRKAALEGVSKDLQARYKAVLQEYGHEERRVQDELARSRKFFTGSLAEVEKSNSQVVEEQSYLLNIAEVQAVSRCDYFLAKIKQADVALLEETADEEEPELTASLPRELTLQDVELLKVGHVGPLQIGQAVKKPRTVNVEDSWAMEATASAASTSVTFREMDMSPEEVVASPRASPAKQRGPEAASNIQQCLFLKKMGAKGSTPGMFNLPVSLYVTSQGEVLVADRGNYRIQVFTRKGFLKEIRRSPSGIDSFVLSFLGADLPNLTPLSVAMNCQGLIGVTDSYDNSLKVYTLDGHCVACHRSQLSKPWGITALPSGQFVVTDVEGGKLWCFTVDRGSGVVKYSCLCSAVRPKFVTCDAEGTVYFTQGLGLNLENRQNEHHLEGGFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKEILHFPKGGGYSVLIREGLTCPVGIALTPKGQLLVLDCWDHCIKIYSYHLRRYSTP"E3 ubiquitin-protein ligase TRIM32Q13049TRIM32 2CT2##5FEYL[Ref.18248090]TRIM22 was reported to attenuate transcription of the HIV LTR. AF-Q13049-F1O`$The N-terminal is acetylation.a$Phosphorylation of Ser at position 328,335,339. DRAVPR0105rMEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS Protein PMLP29590 PML(TRIM19)1BOR##2MVW##4WJO##5YUF##6UYP[Ref.18248090]The list of viruses inhibited by TRIM19 includes vesicular stomatitis virus, influenza A virus, human cytomegalovirus, herpes simplex type 1, Ebola virus, Lassa fever virus, lymphocytic choriomeningitis virus, human foamy virus and HIV. AF-P29590-F1=Exhibits antiviral activity against both DNA and RNA viruses.`$The Lys at posistion 487,515 indicates N6-acetyllysine.a$Phosphorylation of Ser at position 8,36,38,48,117,403,493,504,505,512,< 518,527,530,565.b$Phosphorylation of Thr at position 867. DRAVPR0106MDFSVKVDIEKEVTCPICLELLTEPLSLDCGHSFCQACITAKIKESVIISRGESSCPVCQTRFQPGNLRPNRHLANIVERVKEVKMSPQEGQKRDVCEHHGKKLQIFCKEDGKVICWVCELSQEHQGHQTFRINEVVKECQEKLQVALQRLIKEDQEAEKLEDDIRQERTAWKNYIQIERQKILKGFNEMRVILDNEEQRELQKLEEGEVNVLDNLAAATDQLVQQRQDASTLISDLQRRLRGSSVEMLQDVIDVMKRSESWTLKKPKSVSKKLKSVFRVPDLSGMLQVLKELTDVQYYWVDVMLNPGSATSNVAISVDQRQVKTVRTCTFKNSNPCDFSAFGVFGCQYFSSGKYYWEVDVSGKIAWILGVHSKISSLNKRKSSGFAFDPSVNYSKVYSRYRPQYGYWVIGLQNTCEYNAFEDSSSSDPKVLTLFMAVPPCRIGVFLDYEAGIVSFFNVTNHGALIYKFSGCRFSRPAYPYFNPWNCLVPMTVCPPSS"E3 ubiquitin-protein ligase TRIM22Q8IYM9TRIM22 HIV,EMCV,HBV [Ref.18389079]Human immunodeficiency virus(HIV):TRIM22 inhibits the replication of HIV.##[Ref.19218198]encephalomyocarditis virus(EMCV):Trim22 inhibits the infection of EMCV.##[Ref.19585648]Hepatitic B virus(HBV):TRIM22 exhibits anti-HBV activity by acting as a transcriptional suppressor AF-Q8IYM9-F118389079##19218198##19585648{Barr SD, Smiley JR, Bushman FD.##Eldin P, Papon L, Oteiza A, Brocchi E, Lawson TG, Mechti N.##Gao B, Duan Z, Xu W, Xiong S.RThe interferon response inhibits HIV particle production by induction of TRIM22.##TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus. ##Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain. Anti-HIV,Anti-EMCV,Anti-HBV DRAVPR0107MASKILLNVQEEVTCPICLELLTEPLSLDCGHSLCRACITVSNKEAVTSMGGKSSCPVCGISYSFEHLQANQHLANIVERLKEVKLSPDNGKKRDLCDHHGEKLLLFCKEDRKVICWLCERSQEHRGHHTVLTEEVFKECQEKLQAVLKRLKKEEEEAEKLEADIREEKTSWKYQVQTERQRIQTEFDQLRSILNNEEQRELQRLEEEEKKTLDKFAEAEDELVQQKQLVRELISDVECRSQWSTMELLQDMSGIMKWSEIWRLKKPKMVSKKLKTVFHAPDLSRMLQMFRELTAVRCYWVDVTLNSVNLNLNLVLSEDQRQVISVPIWPFQCYNYGVLGSQYFSSGKHYWEVDVSKKTAWILGVYCRTYSRHMKYVVRRCANRQNLYTKYRPLFGYWVIGLQNKCKYGVFEESLSSDPEVLTLSMAVPPCRVGVFLDYEAGIVSFFNVTSHGSLIYKFSKCCFSQPVYPYFNPWNCPAPMTLCPPSS&Tripartite motif-containing protein 34Q9BYJ4TRIM342EGPSIV_[Ref.17156811]simian immunodeficiency virus(SIV):TRIM34 inhibits simian immunodeficiency virus. AF-Q9BYJ4-F117156811Li X, Gold B, O'hUigin C, Diaz-Griffero F, Song B, Si Z, Li Y, Yuan W, Stremlau M, Mische C, Javanbakht H, Scally M, Winkler C, Dean M, Sodroski J.OUnique features of TRIM5alpha among closely related human TRIM family members.Anti-SIV DRAVPR0108MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGVDGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS%Tripartite motif-containing protein 5Q9C035TRIM5 2ECV##2YRG=[Ref.17156811]TRIM5 exhibited potent antiretroviral activity. AF-Q9C035-F1Restricts infection by N-tropic murine leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV)0F`$The N-terminal is acetylation.a$Phosphorylation of Ser at position 86.25127057##171568110Mandell MA, Jain A, Arko-Mensah J, Chauhan S, Kimura T, Dinkins C, Silvestri G, Mnch J, Kirchhoff F, Simonsen A, Wei Y, Levine B, Johansen T, Deretic V.##Li X, Gold B, O'hUigin C, Diaz-Griffero F, Song B, Si Z, Li Y, Yuan W, Stremlau M, Mische C, Javanbakht H, Scally M, Winkler C, Dean M, Sodroski J. TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition.##Unique features of TRIM5alpha among closely related human TRIM family members. DRAVPR0109MASGILLNVKEEVTCPICLELLTEPLSLHCGHSFCQACITANHKKSMLYKEGERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISELEHRLQGSMMDLLQGVDGIIKRIENMTLKKPK< TFHKNQRRVFRAPDLKGMLDMFRELTDARRYWVDVTLAPNNISHAVIAEDKRQVSSRNPQIMYQAPGTLFTFPSLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQSDAMYNIEQNENYQPKYGYWVIGLQEGVKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS1Tripartite motif-containing protein 5(TRIM5alpha)Q0PF162LM3##3UV9##4TKP##5K3Q[Ref.18389079]Human immunodeficiency virus type 1(HIV-1):RhTRIM5 blocks early replication steps of HIV-1 and inhibits the replication. AF-Q0PF16-F1DRhTRIM5 can restrics the replication of retroviruses such as HIV-1.F`$The N-terminal is acetylation.a$Phosphorylation of Ser at position 87.18389079Barr SD, Smiley JR, Bushman FD.PThe interferon response inhibits HIV particle production by induction of TRIM22. DRAVPR0110MATSAPLRSLEEEVTCSICLDYLRDPVTIDCGHVFCRSCTTDVRPISGSRPVCPLCKKPFKKENIRPVWQLASLVENIERLKVDKGRQPGEVTREQQDAKLCERHREKLHYYCEDDGKLLCVMCRESREHRPHTAVLMEKAAQPHREKILNHLSTLRRDRDKIQGFQAKGEADILAALKKLQDQRQYIVAEFEQGHQFLREREEHLLEQLAKLEQELTEGREKFKSRGVGELARLALVISELEGKAQQPAAELMQDTRDFLNRYPRKKFWVGKPIARVVKKKTGEFSDKLLSLQRGLREFQGKLLRDLEYKTVSVTLDPQSASGYLQLSEDWKCVTYTSLYKSAYLHPQQFDCEPGVLGSKGFTWGKVYWEVEVEREGWSEDEEEGDEEEEGEEEEEEEEAGYGDGYDDWETDEDEESLGDEEEEEEEEEEEVLESCMVGVARDSVKRKGDLSLRPEDGVWALRLSSSGIWANTSPEAELFPALRPRRVGIALDYEGGTVTFTNAESQELIYTFTATFTRRLVPFLWLKWPGTRLLLRP&Tripartite motif-containing protein 26Q12899TRIM26d[Ref.18248090]TRIM26 inhibits both HIV(human immunodeficiency virus) and MLV(murine leukemia virus). AF-Q12899-F1 DRAVPR0111MGESPASVVLNASGGLFSLKMETLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILVSSCSSGESIEPITAFQCPTCRYVISLNHRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSESRRERTYRPTTAMSSERIACQFCEQDPPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEPVPDTHLRGITCLDHENEKVNMYCVSDDQLICALCKLVGRHRDHQVASLNDRFEKLKQTLEMNLTNLVKRNSELENQMAKLIQICQQVEVNTAMHEAKLMEECDELVEIIQQRKQMIAVKIKETKVMKLRKLAQQVANCRQCLERSTVLINQAEHILKENDQARFLQSAKNIAERVAMATASSQVLIPDINFNDAFENFALDFSREKKLLEGLDYLTAPNPPSIREELCTASHDTITVHWISDDEFSISSYELQYTIFTGQANFISKSWCSWGLWPEIRKCKEAVSCSRLAGAPRGLYNSVDSWMIVPNIKQNHYTVHGLQSGTRYIFIVKAINQAGSRNSEPTRLKTNSQPFKLDPKMTHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVMGSSTWYAIGIAYKSAPKNEWIGKNASSWVFSRCNSNFVVRHNNKEMLVDVPPHLKRLGVLLDYDNNMLSFYDPANSLHLHTFDVTFILPVCPTFTIWNKSLMILSGLPAPDFIDYPERQECNCRPQESPYVSGMKTCH)Probable E3 ubiquitin-protein ligase MID2Q9UJV3 MID2(TRIM1) 2DJA##2DMK[Ref.18389079]TRIM1 has been shown to target the capsid protein at an early stage pre-reverse transcription,which forms the protein shell of the viral core. AF-Q9UJV3-F1 DRAVPR0112uMEDRRPHLEARPRNPPANHRGPMDGELPPRARNQTNNPAATNHAGRHLRASNHPAPFRQREERFRAMGRNPHQGRRNQEGHTSDEARDQRQSQNDTRRRNDDQEGRSHRPPWSSDTFQQWHTPPQKPGEQPQQTKRLGYKFLESLLQKEPSEVAITLATSLGLKELLSHSSMKPSFLQLICQVLRKACSSRIDRQSILHVLGILNNSKFLRVCLPAYVVGMITEPSPDIRNQYPEHISNIISLLQDLVSVFPASSMQETSMLISLLPTSLNALRASGVDIEEETEKNLEKVQAIIKYLQEKRRQGSLRVDTYTLVQAEAEGEVESYRAMPIYPTYNEVHLDEKPFLRPNIISGKYESTAVYLDTHFRLLREDFVRPLREGILKLLQSFEDQCLRKRKFDDIRIYFDARIITPMCSASGIVYKVQFDTKPLKLVRWQNSKRLLYGSLVCMSKDNFETFLFATVSNREHEDLCQGIVQLCFNEQSQQLLADVQPSDSFLMVETTAYFEAYRHVLEGLQEVQEEDVPFQRNIVQCDSYVRNPRYLLMGGRYDFTPLMENPSAMRKSLRGAEALRHPRINVFDFGQWPSKEALKLDDSQMEALQFALTKELAIIQGPPGTGKTYVGLKIVQALLTNKSVWQINTQTFPILVVCYTNHALDQFLEGIYGCQKTSIVRVGGRSNSEILKQFTLRELRNKREFRRTLPMHLRRAYMSIVTEMKESEQKLQEGAQTLECTMHGVLREQHLEKYISAQHWESLMSGPVQDADWVCVQPSKHSMILEWLGLGVGSFTQSASPAGPENTAQAEGEEEEEGEEEGSLIEIAEEADLIQADRVIEEEEVVRPRRRKKEENGTDQELAKMLLAMRLDQEVPGTTAGPEQATEEWETQRGQKKKMKRRVKVELRKLNTMTKAEANGIQDVWQLDLSSRWQLYRLWLQMYQADTRRRILSYERQYRTWAERMAELRLQEDLHILKDAEVVGMTTTGAAKYRQILQQVEPRIVIVEEAAEVLEAHTIATLSKACQHLILIGDHQQLRPSANVYDLAKNFNLEVSLFERLVKVNIPFVRLNYQHRMRPEIARLLTPHIYQDLENHPSVLKYEQIKGVSSNLFFVEHNFPEQEIQEGKSHQNQHEAHFVVELCQYLLCQEYLPSQITILTTYTGQLFCLRKLMPVKTFAGIKVHVVDKYQGEENDIILLSLVRSNQEGKVGFLQIPNRICVALSRAKKGMYCIGNMQMLAKVPLWSRIIHTLRENNQIGPSLRLCCQNHPETHTLVSKASDFQKVPEGGCSRPCEFRLACGHVCTRACHPYDSSHKEFQCMKPCQKVLCQDGHRCPNVCFQECQPCQVKVPKIILKCGHKQMVPCSMSESEFCCQEPCSKILRCGHRCSHLCGEDCVRLCSERVTVELKCGHSQLVKCGNVEDIKYGLPVKCTTKCDTTLDCGHPCPGSCHSCFEGRFHERCQQPCKRLLICSHKCQEPCTGECPPCQRTCQNRCVHSQCKKKCGELCSPCVEPCVWRCQHYQCTKLCSEPCNRPPCYVPCTKLLACGHPCIGLCGEPCPKKCRVCQPDEVTQIFFGFEDEPDARFVQLEDCSHIFEVQALDRFMNEQKDDEVAIKLKVCPICQVPIRKNLRYGTSIKQRLEEIEIVKEKIQGSAGEISTSQEQLKA< LLKSKTLFHQLRPEEFLILQEKLAQKNLSVKDLGLVENSIRFYDHLANLEGSLEKVHCGEQQSVRTRLEQVHEWLAKKRLSFSSQELSDLQSEIQRLTYLVNLLMRCKMAEKVKGSIAEEVSSIRNILEKTSKFTQEDEQLVQKKMDALKTTLPCSGLGISDEERVQIVTAMGVPRGHWFKCPNGHIYVITECGGAMQRSTCPECQEVIGGENHTLERSNHLASEMDGAQHPAWSNTANNFMNFEEIHRMM*NFX1-type zinc finger-containing protein 1Q8R151Znfx1VSV, EMCV, SeV[Ref.31685995]vesicular stomatitis virus (VSV)/encephalomyocarditis virus (EMCV)/Senda virus (SeV): ZNFX1 directly binds to viral RNA and specifically restricts the replication of viruses. AF-Q8R151-F1zinc finger NFX1-type containing 1 (ZNFX1), a helicase SF1, is an interferon (IFN)-stimulated, mitochondrial-localised dsRNA sensor that specifically restricts the replication of RNA viruses.31685995AWang Y, Yuan S, Jia X, Ge Y, Ling T, Nie M, Lan X, Chen S, Xu A. fMitochondria-localised ZNFX1 functions as a dsRNA sensor to initiate antiviral responses through MAVS.Anti-VSV, Anti-EMCV, Anti-SeV DRAVPR0113MASETTEARAPFQPDGAYGWRCPEHSERPAELFCRRCGRCVCALCPVLGAHRGHPVGLAEEEAVRVQKLIQDCLECLATKKRQHADNIAHLEDAGERLKVYADSSKAWLTQKFTELRLLLDEEEVLAKKFIDKSTQLTLQVYREQAETCGKQIEVMDDFSTRVWGIGQEPNPVQLLQAYIATKTEMGQQMSPSELSHPVPLSFEPVKNFFKEFVEAIGNTLQTPMDTRLKENINCQLSNSSSTKPGALLKTSPSPERALFLKYARTPTLDPDTMHARLRLSPDGLTVRCSLLGRLGPRPAPRFDALRQVLGRDGFAAGRHYWEVDVQEAGVGWWVGAAYPSLRRRGASAAARLGCNRESWCVKRYDLEYWAFHDGQRSRLRPRRDPHRLGVFLDYEAGILAFYDVAGGMSHLHTFHAAFQEPLYPALRLWEGPISIPRLP&Tripartite motif-containing protein 14Q8BVW3Trim14HSV-1c[Ref.27666593]herpes simplex virus type 1 (HSV-1):TRIM14 Protects Mice from HSV-1 Infection In Vivo AF-Q8BVW3-F1TRIM14 enhances RIG-I-mediated activation of type I IFN responses against RNA viruses. TRIM14 deficiency resulted in impaired activation of type I IFN responses by causing fewer IFNs and ISGs to be produced upon VSV infection in murine primary cells. 27666593UChen M, Meng Q, Qin Y, Liang P, Tan P, He L, Zhou Y, Chen Y, Huang J, Wang RF, Cui J.pTRIM14 Inhibits cGAS Degradation Mediated by Selective Autophagy Receptor p62 to Promote Innate Immune Responses Anti-HSV-1 DRAVPR0114MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGESInterferon regulatory factor 3 Q14653IRF3.1J2F##1T2K##1ZOQ##2PI0##3A77##5JEL##6SJA##7JFL[Ref.33440148]SARS-CoV-2:Activated upon coronavirus SARS-CoV-2 infection and regulate interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against viruse. AF-Q14653-F1`$Phosphorylation of Thr at position 3, 75, 180, 237, 244, 253, 404.a$Phosphorylation of Ser at position 14, 97, 123, 175, 188, 385, 386, 396, 398, 427.b$There is a disulfide bonds between Cys267 and Cys289.33440148Yin X, Riva L, Pu Y, Martin-Sancho L, Kanamune J, Yamamoto Y, Sakai K, Gotoh S, Miorin L, De Jesus PD, Yang CC, Herbert KM, Yoh S, Hultquist JF, Garca-Sastre A, Chanda SK. NMDA5 Governs the Innate Immune Response to SARS-CoV-2 in Lung Epithelial Cells DRAVPR0115MLKLVQYIAPRVGGATPRPTACGWGNLLLISPRSGASSEKCITQRRHFLFSSASSSGTFASSSSLCTEQRQQFHGSRRNRETILFPSTYSSLQAQSQRAFRDSSKPDSDDYVDSIPKAEQRTRTRKSLFNDPDERTEEIKIEGVMAPHDRDFGHSGRGGRGGDRGGDDRRGGGGGGNRFGGGGGGGDYHGIRNGRVEKRRDDRGGGNRFGGGGGFGDRRGGGGGGSQDLPMRPVDFSNLAPFKKNFYQEHPNVANRSPYEVQRYREEQEITVRGQVPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTKNNAKQAKALVDVLREANQEINPALENLARNSRYDGGGGRSRYGGGGGGGRFGGGGFKKGSLSNGRGFGGGGGGGGEGRHSRFDATP-dependent RNA helicase p62P19109Rm62 (Dmp68, p62)RVFVl[Ref.25126784]Rift Valley fever virus (RVFV): Rm62 specificall< y restricts bunyaviral infection in Drosophila  AF-P19109-F1vRm62 controls the replication of RVFV but not VSV, SINV or DCV, viruses that are restricted by antiviral RNAi in flies25126784lMoy RH, Cole BS, Yasunaga A, Gold B, Shankarling G, Varble A, Molleston JM, tenOever BR, Lynch KW, Cherry S.QStem-loop recognition by DDX17 facilitates miRNA processing and antiviral defense Anti-RVFV DRAVPR0116MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQQ96F44TRIM11 AF-Q96F44-F1pUpon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. DRAVPR0117MDPFPDLYATPGDSLDHFLEHSLQPQRDWKEEGQDAWERIERFFREQCFRDELLLDQEVRVIKVVKGGSSGKGTTLNHRSDQDMILFLSCFSSFEEQARNREVVISFIKKRLIHCSRSLAYNIIVLTHREGKRAPRSLTLKVQSRKTDDIIWMDILPAYDALGPISRDSKPAPAIYETLIRSKGYPGDFSPSFTELQRHFVKTRPVKLKNLLRLVKFWYLQCLRRKYGRGAVLPSKYALELLTIYAWEMGTESSDSFNLDEGFVAVMELLVNYRDICIYWTKYYNFQNEVVRNFLKKQLKGDRPIILDPADPTNNLGRRKGWEQVAAEAAFCLLQVCCTTVGPSERWNVQRARDVQVRVKQTGTVDWTLWTNPYSPIRKMKAEIRREKNFGGELRISFQEPGGERQLLSSRKTLADYGIFSKVNIQVLETFPPEILVFVKYPGGQSKPFTIDPDDTILDLKEKIEDAGGPCAEDQVLLLDDEELEDDESLKELEIKDCDTIILIRVID62'-5'-oligoadenylate synthase-like protein 2(p54 OASL)Q9Z2F2Oasl2[Ref.12799444]mOasl2 can active Rnase L. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. AF-Q9Z2F2-F1mOasl2 protein is Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response.127994442Eskildsen S, Justesen J, Schierup MH, Hartmann R. MCharacterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like family DRAVPR0118MASDTPGFYMDKLNKYRQMHGVAITYKELSTSGPPHDRRFTFQVLIDEKEFPEAKGRSKQEARNAAAKLAVDILDNENKVDCHTSASEQGLFVGNYIGLVNSFAQKKKLSVNYEQCEPNSELPQRFICKCKIGQTMYGTGSGVTKQEAKQLAAKEAYQKLLKSPPKTAGTSSSVVTSTFSGFSSSSSMTSNGVSQSAPGSFSSENVFTNGLGENKRKSGVKVSPDDVQRNKYTLDARFNSDFEDIEEIGLGGFGQVFKAKHRIDGKRYAIKRVKYNTEKAEHEVQALAELNHVNIVQYHSCWEGVDYDPEHSMSDTSRYKTRCLFIQMEFCDKGTLEQWMRNRNQSKVDKALILDLYEQIVTGVEYIHSKGLIHRDLKPGNIFLVDERHIKIGDFGLATALENDGKSRTRRTGTLQYMSPEQLFLKHYGKEVDIFALGLILAELLHTCFTESEKIKFFESLRKGDFSNDIFDNKEKSLLKKLLSEKPKDRPETSEILKTLAEWRNISEKKKRNTCEInterferon-induced, double-stranded RNA-activated protein kinase(PKR)Q03963Eif2ak2 1X48##1X49RSV, LCMV, SFV[Ref.21994357]respiratory syncytial virus(RSV):a lack of PKR in vivo results in altered immunoglobulin G secretion in response to respiratory syncytial virus (RSV) infection.##[Ref.20585572]lymphocytic choriomeningitis virus (LCMV):PKR activity could be a distinguishing feature between Type I IFN actions that mediate viral control or stimulate CD8 T cell expansion during an acute infection with lymphocytic choriomeningitis virus (LCMV).[Ref.19264662]Semliki Forest virus(SFV):In mouse embryo fibroblasts (MEFs), PKR delayed virus protein synthesis, production of infectious virus and caspase-3-activated cell death and reduced the yield of infectious virus by 90 %. AF-Q03963-F1~In response to SFV, PKR exerts an early antiviral effect that delays virus protein production and release of infectious virus.`$The N-terminal is acetylation.a$Phosphorylation of Thr at position 84, 233, 409, 414.b$Phosphorylation of Tyr at position 96, 157, 268.c$Phosphorylation of Ser at position 419.21994357##20585572##19264662Thakur SA, Zalinger ZB, Johnson TR, Imani F.##Nakayama Y, Plisch EH, Sullivan J, Thomas C, Czuprynski CJ, Williams BR, Suresh M.##Barry G, Breakwell L, Fragkoudis R, Attarzadeh-Yazdi G, Rodriguez-Andres J, Kohl A, Fazakerley JK.{Protein kinase R is a novel mediator of CD40 signaling and plays a critical role in modulating immunoglobulin expressio< n during respiratory syncytial virus infection.##Role of PKR and Type I IFNs in viral control during primary and secondary infection. ##PKR acts early in infection to suppress Semliki Forest virus production and strongly enhances the type I interferon responseAnti-RSV, Anti-LCMV, Anti-SFV DRAVPR0119MARSFSLLMVVLVLSYKSICSLGCDLPQTHSLRNRRALILLAQMGRISPFSCLKDRHEFRFPEEEFDGHQFQKTQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDFILAVRKYFQRITLYLMEKKYSPCAWEVVRAEIMRSFSFSTNLKKGLRRKDInterferon alpha-7P01567IFNA70[Ref.9334213]IFN-alpha have antiviral activities AF-P01567-F1JThere are five disulfide bonds between Cys24 and Cys122, Cys52 and Cys162.bDomanski P, Fish E, Nadeau OW, Witte M, Platanias LC, Yan H, Krolewski J, Pitha P, Colamonici OR. A region of the beta subunit of the interferon alpha receptor different from box 1 interacts with Jak1 and is sufficient to activate the Jak-Stat pathway and induce an antiviral state DRAVPR0120MSTTSKESLVCNLRQLKCHFTWNLIAEDESLDEFEDRVFNKDEFQNSEFKATMCNILAYVKHCRGLNEAALQCLGEAEGFIQQQHPDQVEIRSLVTWGNYAWVYYHMGQFSKAQAYLDKVKQVCKKFSSPYRIENPALDCEEGWARLKCTKNQNERVKVCFQKALEKDPKNPEFTSGWAIAFYRLDDWPARNYCIDSLEQAIQLSPDNTYVKVLLALKLDAVHVHKNQAMALVEEALKKDPSAIDTLLRAARFYCKVYDTDRAIQLLRKALEKLPNNAYVHYYMGCCYRSKVHHMLNRREMVFSGDRKKLEELIQLAVNHLRKAEEIKEMLEYSCSFLADLYIIAKKYDEADYYFQKELSKDLPPGPKQLLHLRYGNFQFFQMKRQDKAIYHYMEGVKIKKKTIPQKKMREKLQRIALRRLHEDESDSEALHILAFLQENGGGQQADKDSERGVDSANQVPSASLDEDGAEY;Interferon-induced protein with tetratricopeptide repeats 2Q64112Ifit2[Ref.22615570]vesicular stomatitis virus (VSV):Ifit2 protects mice from lethal intranasal VSV infection, Ifit2 suppresses replication of VSV in the brain after intranasal infection.  AF-Q64112-F1Ifit2 failed to protect mice from another neurotropic virus, encephalomyocarditis virus, nor was it necessary for protecting organs other than brain from infection by VSV. 22615570hFensterl V, Wetzel JL, Ramachandran S, Ogino T, Stohlman SA, Bergmann CC, Diamond MS, Virgin HW, Sen GC.OInterferon-induced Ifit2/ISG54 protects mice from lethal VSV neuropathogenesis. DRAVPR0121rMDLFHTPAGALDKLVAHNLHPAPEFTAAVRGALGSLNITLQQHRARGSQRPRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKTCHSETLGAMRMLLESWGGHPGPGLTFEFSQSKASRILQFRLASADGEHWIDVSLVPAFDVLGQPRSGVKPTPNVYSSLLSSHCQAGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWEQGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQEAESSFSQQCFKQASGVLVQPWEGPGLPRAGILDLGHPIYQGPNQALEDNKGHLAVQSKERSQKPSNSAPGFPEAATKIPAMPNPSANKTRKIRKKAAHPKTVQEAALDSISSHVRITQSTASSHMPPDRSSISTAGSRMSPDLSQIPSKDLDCFIQDHLRPSPQFQQQVKQAIDAILCCLREKSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKTLGDFKGQKPHQAEILRDMQAQLRHWCQNPVPGLSLQFIEQKPNALQLQLASTDLSNRVDLSVLPAFDAVGPLKSGTKPQPQVYSSLLSSGCQAGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGEAAGDAPPPAYALELLTIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGDWKLLAQEAAALGSQVCLQSGDGTLVPPWDVTPALLHQTLAEDLDKFISEFLQPNRHFLTQVKRAVDTICSFLKENCFRNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFRQFSEQGSHRAEIISEIQAHLEACQQMHSFDVKFEVSKRKNPRVLSFTLTSQTLLDQSVDFDVLPAFDALGQLRSGSRPDPRVYTDLIHSCSNAGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKGKGSLPPQHGLELLTVYAWEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNARWDLLAKEATVYASALCCVDRDGNPIKPWPVKAAVQ8VI93 Oas3 (oasl10)[Ref.12396720]mOas3 can active Rnase L. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. AF-Q8VI93-F112396720Kakuta S, Shibata S, Iwakura Y.KGenomic structure of the mouse 2',5'-oligoadenylate synthetase gene family. DRAVPR0122'MAENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDSGLVRCPECNQAYNQKPGLEKNLKLTNIVEKFNALHVEKPPTALHCVFCRRGPPLPAQKVCLRCEAPCCQSHVQTHLQQPSTARGHLLVEADDVRAWSCPQHNAYRLYHCEAEQVAVCQYCCYYSGAHQGHSVCDVEIRRNEIRKMLMKQQERLEEREQDIEDQLYKLESDKRLVEEKVSQLKEEVRLQYEKLHQLLDEDLRQTVEVLDKAQAKFCSENAAQALHLGERMQEAKKLLGSLQRLFDKTEDVGFMKNTKSVKILMDRTQTCTGSSLSPPKIGHLNSKLFLNEVAKKEKQLRKMLEGPFSTPVPFLQSVPLYPCGVNSSGAEKRKHSTAFPEASFLETSSGPVGGQYGAAGTASSEGQSGQPLGPCSSTQHLVALPGGTQPVHSSPVFPPSQYPNGSTTQQPMLPQYGGRKILVCSVDNCYCSSVANHGGHQPYPRSGHFPWTVPSQEYSHPLPPTPSVPQ< SLPGLAVRDWLDASQQPGHQDFYRVYGQPSTKHYVTS!E3 ubiquitin-protein ligase TRIM8Q99PJ2Trim8O[Ref.18248090]Human immunodeficiency virus(HIV):Mouse TRIM8 inhibited HIV entry AF-Q99PJ2-F1 DRAVPR0123MPATPSLKVVHELPACTLCAGPLEDAVTIPCGHTFCRLCLPALSQMGAQSSGKILLCPLCQEEEQAETPMAPVPLGPLGETYCEEHGEKIYFFCENDAEFLCVFCREGPTHQAHTVGFLDEAIQPYRDRLRSRLEALSTERDEIEDVKCQEDQKLQVLLTQIESKKHQVETAFERLQQELEQQRCLLLARLRELEQQIWKERDEYITKVSEEVTRLGAQVKELEEKCQQPASELLQDVRVNQSRCEMKTFVSPEAISPDLVKKIRDFHRKILTLPEMMRMFSENLAHHLEIDSGVITLDPQTASRSLVLSEDRKSVRYTRQKKSLPDSPLRFDGLPAVLGFPGFSSGRHRWQVDLQLGDGGGCTVGVAGEGVRRKGEMGLSAEDGVWAVIISHQQCWASTSPGTDLPLSEIPRGVRVALDYEAGQVTLHNAQTQEPIFTFTASFSGKVFPFFAVWKKGSCLTLKG&Tripartite motif-containing protein 15Q9C019TRIM15[Ref.18248090]murine leukemia virus (MLV):TRIM15 interferes with MLV release by directly or indirectly binding the MLV Gag precursor protein via its B-box. AF-Q9C019-F1tThe antiviral activity of TRIM15 depends on the ability of its B-box to Interact with the MLV Gag precursor protein. DRAVPR0124MPADVNLSQKPQVLGPEKQDGSCEASVSFEDVTVDFSREEWQQLDPAQRCLYRDVMLELYSHLFAVGYHIPNPEVIFRMLKEKEPRVEEAEVSHQRCQEREFGLEIPQKEISKKASFQKDMVGEFTRDGSWCSILEELRLDADRTKKDEQNQIQPMSHSAFFNKKTLNTESNCEYKDPGKMIRTRPHLASSQKQPQKCCLFTESLKLNLEVNGQNESNDTEQLDDVVGSGQLFSHSSSDACSKNIHTGETFCKGNQCRKVCGHKQSLKQHQIHTQKKPDGCSECGGSFTQKSHLFAQQRIHSVGNLHECGKCGKAFMPQLKLSVYLTDHTGDIPCICKECGKVFIQRSELLTHQKTHTRKKPYKCHDCGKAFFQMLSLFRHQRTHSREKLYECSECGKGFSQNSTLIIHQKIHTGERQYACSECGKAFTQKSTLSLHQRIHSGQKSYVCIECGQAFIQKAHLIVHQRSHTGEKPYQCHNCGKSFISKSQLDIHHRIHTGEKPYECSDCGKTFTQKSHLNIHQKIHTGERHHVCSECGKAFNQKSILSMHQRIHTGEKPYKCSECGKAFTSKSQFKEHQRIHTGEKPYVCTECGKAFNGRSNFHKHQITHTRERPFVCYKCGKAFVQKSELITHQRTHMGEKPYECLDCGKSFSKKPQLKVHQRIHTGERPYVCSECGKAFNNRSNFNKHQTTHTRDKSYKCSYSVKGFTKQ2Zinc finger protein 175(Zinc finger protein OTK18)Q9Y473ZNF175[Ref.14688346]Human immunodeficiency virus type 1(HIV-1):Interferes with HIV-1 replication by suppressing Tat-induced viral LTR promoter activity. AF-Q9Y473-F114688346ZCarlson KA, Leisman G, Limoges J, Pohlman GD, Horiba M, Buescher J, Gendelman HE, Ikezu T.UMolecular characterization of a putative antiretroviral transcriptional factor, OTK18 DRAVPR0125MSEVTKNSLEKILPQLKCHFTWNLFKEDSVSRDLEDRVCNQIEFLNTEFKATMYNLLAYIKHLDGNNEAALECLRQAEELIQQEHADQAEIRSLVTWGNYAWVYYHLGRLSDAQIYVDKVKQTCKKFSNPYSIEYSELDCEEGWTQLKCGRNERAKVCFEKALEEKPNNPEFSSGLAIAMYHLDNHPEKQFSTDVLKQAIELSPDNQYVKVLLGLKLQKMNKEAEGEQFVEEALEKSPCQTDVLRSAAKFYRRKGDLDKAIELFQRVLESTPNNGYLYHQIGCCYKAKVRQMQNTGESEASGNKEMIEALKQYAMDYSNKALEKGLNPLNAYSDLAEFLETECYQTPFNKEVPDAEKQQSHQRYCNLQKYNGKSEDTAVQHGLEGLSISKKSTDKEEIKDQPQNVSENLLPQNAPNYWYLQGLIHKQNGDLLQAAKCYEKELGRLLRDAPSGIGSIFLSASELEDGSEEMGQGAVSSSPRELLSNSEQLNCInterferon-induced protein with tetratricopeptide repeats 3(IFIT-3)O14879IFIT36C6K>[Ref.21813773]IFIT3 enhances MAVS-mediated antiviral responses AF-O14879-F11Phosphorylation of Ser at position 203, 237, 478.21813773'Liu XY, Chen W, Wei B, Shan YF, Wang C.XIFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging MAVS and TBK1. DRAVPR0126MPTGFVAPILCVLLPSPTREAATVASATGDSASERESAAPAAAPTAEAPPPSVVTRPEPQALPSPAIRAPLPDLYPFGTMRGGGFGDRDRDRDRGGFGARGGGGLPPKKFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARLTPYEVDELRRKKEITVRGGDVCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSANHNILQIVDVCMESEKDHKLIQLMEEIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTFFTPGNLKQARELIKVLEEANQAINPKLMQLVDHRGGGGGGGGRSRYRTTSSANNPNLMYQDECDRRLRGVKDGGRRDSASYRDRSETDRAGYANGSGYGSPNSAFGAQAGQYTYGQGTYGAAAYGTSSYTAQEYGAGTYGASSTTSTGRSSQSSSQQFSGIGRSGQQPQPLMSQQFAQPPGATNMIGYMGQTAYQYPPPPPPPPPSRK)Probable ATP-dependent RNA helicase DDX17Q92841DDX176UV0##6UV1##6UV2##6UV3##6UV4b[Ref.25126784]Rift Valley fever virus (RVFV): DDX17 binds RVFV RNAs to restrict viral replication. AF-Q92841-F1kDDX17 targets a structured stem loop, either to facilitate miRNA processing or to mediate virus inhibition.`$Phosphorylation of Ser at position 64.a$The Lys at position 108< , 109, 121 indicates N6-acetyllysine.b$Phosphorylation of Thr at position 523.c$The Arg at position 684 indicates Omega-N-methylarginine. DRAVPR0127~MEERRPHLDARPRNSHTNHRGPVDGELPPRARNQANNPPANALRGGASHPGRHPRANNHPAAYWQREERFRAMGRNPHQGRRNQEGHASDEARDQRHDQENDTRWRNGNQDCRNRRPPWSNDNFQQWRTPHQKPTEQPQQAKKLGYKFLESLLQKDPSEVVITLATSLGLKELLSHSSMKSNFLELICQVLRKACSSKMDRQSVLHVLGILKNSKFLKVCLPAYVVGMITEPIPDIRNQYPEHISNIISLLQDLVSVFPASSVQETSMLVSLLPTSLNALRASGVDIEEETEKNLEKVQTIIEHLQEKRREGTLRVDTYTLVQPEAEDHVESYRTMPIYPTYNEVHLDERPFLRPNIISGKYDSTAIYLDTHFRLLREDFVRPLREGILELLQSFEDQGLRKRKFDDIRIYFDTRIITPMCSSSGIVYKVQFDTKPLKFVRWQNSKRLLYGSLVCMSKDNFETFLFATVSNREQEDLCRGIVQLCFNEQSQQLLAEVQPSDSFLMVETTAYFEAYRHVLEGLQEVQEEDVPFQRNIVECNSHVKEPRYLLMGGRYDFTPLIENPSATGEFLRNVEGLRHPRINVLDPGQWPSKEALKLDDSQMEALQFALTRELAIIQGPPGTGKTYVGLKIVQALLTNESVWQISLQKFPILVVCYTNHALDQFLEGIYNCQKTSIVRVGGRSNSEILKQFTLRELRNKREFRRNLPMHLRRAYMSIMTQMKESEQELHEGAKTLECTMRGVLREQYLQKYISPQHWESLMNGPVQDSEWICFQHWKHSMMLEWLGLGVGSFTQSVSPAGPENTAQAEGDEEEEGEEESSLIEIAEEADLIQADRVIEEEEVVRPQRRKKEESGADQELAKMLLAMRLDHCGTGTAAGQEQATGEWQTQRNQKKKMKKRVKDELRKLNTMTAAEANEIEDVWQLDLSSRWQLYRLWLQLYQADTRRKILSYERQYRTSAERMAELRLQEDLHILKDAQVVGMTTTGAAKYRQILQKVEPRIVIVEEAAEVLEAHTIATLSKACQHLILIGDHQQLRPSANVYDLAKNFNLEVSLFERLVKVNIPFVRLNYQHRMCPEIARLLTPHIYQDLENHPSVLKYEKIKGVSSNLFFVEHNFPEQEIQEGKSHQNQHEAHFVVELCKYFLCQEYLPSQITILTTYTGQLFCLRKLMPAKTFAGVRVHVVDKYQGEENDIILLSLVRSNQEGKVGFLQISNRICVALSRAKKGMYCIGNMQMLAKVPLWSKIIHTLRENNQIGPMLRLCCQNHPETHTLVSKASDFQKVPEGGCSLPCEFRLGCGHVCTRACHPYDSSHKEFQCMKPCQKVICQEGHRCPLVCFQECQPCQVKVPKTIPRCGHEQMVPCSVPESDFCCQEPCSKSLRCGHRCSHPCGEDCVQLCSEMVTIKLKCGHSQPVKCGHVEGLLYGGLLVKCTTKCGTILDCGHPCPGSCHSCFEGRFHERCQQPCKRLLICSHKCQEPCIGECPPCQRTCQNRCVHSQCKKKCGELCSPCVEPCVWRCQHYQCTKLCSEPCNRPPCYVPCTKLLVCGHPCIGLCGEPCPKKCRICHMDEVTQIFFGFEDEPDARFVQLEDCSHIFEVQALDRYMNEQKDDEVAIRLKVCPICQVPIRKNLRYGTSIKQRLEEIEIIKEKIQGSAGEIATSQERLKALLERKSLLHQLLPEDFLMLKEKLAQKNLSVKDLGLVENYISFYDHLASLWDSLKKMHVLEEKRVRTRLEQVHEWLAKKRLSFTSQELSDLRSEIQRLTYLVNLLTRYKIAEKKVKDSIAVEVYSVQNILEKTCKFTQEDEQLVQEKMEALKATLPCSGLGISEEERVQIVSAIGYPRGHWFKCRNGHIYVIGDCGGAMERGTCPDCKEVIGGTNHTLERSNQLASEMDGAQHAAWSDTANNLMNFEEIQGMMQ9P2E3ZNFX1 (KIAA1404)[Ref.33872655]RNA-binding protein that initiates the antiviral response and is required to restrict the replication of RNA viruses AF-Q9P2E3-F133872655Vavassori S, Chou J, Faletti LE, Haunerdinger V, Opitz L, Joset P, Fraser CJ, Prader S, Gao X, Schuch LA, Wagner M, Hoefele J, Maccari ME, Zhu Y, Elakis G, Gabbett MT, Forstner M, Omran H, Kaiser T, Kessler C, Olbrich H, Frosk P, Almutairi A, Platt CD, Elkins M, Weeks S, Rubin T, Planas R, Marchetti T, Koovely D, Klmbt V, Soliman NA, von Hardenberg S, Klemann C, Baumann U, Lenz D, Klein-Franke A, Schwemmle M, Huber M, Sturm E, Hartleif S, Hffner K, Gimpel C, Brotschi B, Laube G, Gngr T, Buckley MF, Kottke R, Staufner C, Hildebrandt F, Reu-Hofer S, Moll S, Weber A, Kaur H, Ehl S, Hiller S, Geha R, Roscioli T, Griese M, Pachlopnik Schmid J.YMultisystem inflammation and susceptibility to viral infections in human ZNFX1 deficiency DRAVPR0128IMSATSVDQRPKGQGNKVSVQNGSIHQKDAVNDDDFEPYLSSQTNQSNSYPPMSDPYMPSYYAPSIGFPYSLGEAAWSTAGDQPMPYLTTYGQMSNGEHHYIPDGVFSQPGALGNTPPFLGQHGFNFFPGNADFSTWGTSGSQGQSTQSSAYSSSYGYPPSSLGRAITDGQAGFGNDTLSKVPGISSIEQGMTGLKIGGDLTAAVTKTVGTALSSSGMTSIATNSVPPVSSAAPKPTSWAAIARKPAKPQPKLKPKGNVGIGGSAVPPPPIKHNMNIGTWDEKGSVVKAPPTQPVLPPQTIIQQPQPLIQPPPLVQSQLPQQQPQPPQPQQQQGPQPQAQPHQVQPQQQQLQNRWVAPRNRGAGFNQNNGAGSENFGLGVVPVSASPSSVEVHPVLEKLKAINNYNPKDFDWNLKNGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDAAYRSLNGKGPLYLLFSVNGSGHFCGVAEMKSVVDYNAYAGVWSQDKWKGKFEVKWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIIATFKHTTSIFDDFAHYEKRQEEEEAMRRERNRNKQ&YTH domain-containing family protein 3Q7Z739YTHDF36ZOT[Ref.32053707]Human immunodeficiency virus(HIV):YTHDF3 is incorporated into HIV particles in a nucleocapsid-dependent manner and reduces viral infectivity in the next cycle of infection. AF-Q7Z739-F1F`$The N-terminal is acetylation.a$Phosphorylation of Ser at position 23.32053707tJurczyszak D, Zhang W, Terry SN, Kehrer T, Bermdez Gonzlez MC, McGregor E, Mulder LCF, Eckwahl MJ, Pan T, Simon V.RHIV protease cleaves the antiviral m6A reader protein YTHDF3 in<  the viral particle DRAVPR0129MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLGQMGRISPFSCLKDRHDFRIPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDSILAVRKYFQRITLYLIERKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKDInterferon alpha-10P01566IFNA10 AF-P01566-F1 DRAVPR0130_GSGPTYCWNEANNPGGPNRCSNNKQCDGARTCSSSGFCQGTSRKPDPGPKGPTYCWDEAKNPGGPNRCSNSKQCDGARTCSSSGFCQGTAGHAAAScytovirin(SVN)Scytonema variumP860412JMV##2QSK##2QT4[Ref.12614152]Human immunodeficiency virus(HIV):The protein displayed potent anticytopathic activity against laboratory strains and primary isolates of HIV-1 with EC50 values ranging from 0.3 to 22 nM. AF-P86041-F1yScytovirin binds to viral coat proteins gp120, gp160, and gp41 but not to cellular receptor CD4 or other tested proteins.zThere are five disulfide bonds between Cys7 and Cys55, Cys20 and Cys32, Cys26 and Cys38, Cys68 and Cys80, Cys74 and Cys86.12614152Bokesch HR, O'Keefe BR, McKee TC, Pannell LK, Patterson GM, Gardella RS, Sowder RC 2nd, Turpin J, Watson K, Buckheit RW Jr, Boyd MR. RA potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium. DRAVPR0131MTFAEDKTYKYIRDNHSKFCCVDVLEILPYLSCLTASDQDRLRASYRQIGNRDTLWGLFNNLQRRPGWVEVFIRALQICELPGLADQVTRVYQSYLPPGTSLRSLEPLQLPDFPAAVSGPSAFAPGHNIPDHGLRETPSCPKPVQDTQPPESPVENSEQLLQTNSGAVARMSGGSLIPSPNQQALSPQPSREHQEQEPELGGAHAANVASVPIATYGPVSPTVSFQPLPRTALRTNLLSGVTVSALSADTSLSSSSTGSAFAKGAGDQAKAATCFSTTLTNSVTTSSVPSPRLVPVKTMSSKLPLSSKSTAAMTSTVLTNTAPSKLPSNSVYAGTVPSRVPASVAKAPANTIPPERNSKQAKETPEGPATKVTTGGNQTGPNSSIRSLHSGPEMSKPGVLVSQLDEPFSACSVDLAISPSSSLVSEPNHGPEENEYSSFRIQVDESPSADLLGSPEPLATQQPQEEEEHCASSMPWAKWLGATSALLAVFLAVMLYRSRRLAQ)Mitochondrial antiviral-signaling proteinQ8VCF0Mavs4GHU0[Ref.24037184]Acts downstream of DHX33, DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5) AF-Q8VCF0-F1`$Phosphorylation of Ser at position 152, 157, 172, 186, 220, 251, 256, 384, 418.a$The Arg at positio 234 indicates Asymmetric dimethylarginine.240371846Liu Y, Lu N, Yuan B, Weng L, Wang F, Liu YJ, Zhang Z. The interaction between the helicase DHX33 and IPS-1 as a novel pathway to sense double-stranded RNA and RNA viruses in myeloid dendritic cells DRAVPR0132MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWEQSLLEKFSTELNQQLNDLEACVIQEVGVEETPLMNVDSILAVKKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSKIFQERLRRKEInterferon alpha-21P01568IFNA210[Ref.1634550]IFN-alpha have antiviral activities AF-P01568-F11634550KZoon KC, Miller D, Bekisz J, zur Nedden D, Enterline JC, Nguyen NY, Hu RQ. cPurification and characterization of multiple components of human lymphoblastoid interferon-alpha. DRAVPR0133MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISPFSCLKDRHDFGLPQEEFDGNQFQKTQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNNLEACVIQEVGMEETPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSLSFSTNLQKILRRKDInterferon alpha-17P01571IFNA17 AF-P01571-F1 DRAVPR0134MALPFALMMALVVLSCKSSCSLGCNLSQTHSLNNRRTLMLMAQMRRISPFSCLKDRHDFEFPQEEFDGNQFQKAQAISVLHEMMQQTFNLFSTKNSSAAWDETLLEKFYIELFQQMNDLEACVIQEVGVEETPLMNEDSILAVKKYFQRITLYLMEKKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKDInterferon alpha-14P01570IFNA14 AF-P01570-F1p`$There are five disulfide bonds between Cys24 and Cys122, Cys52 and Cys162.a$Glycosylation of Asn at position 95. DRAVPR0135,MAGIPEVVAMDCEMVGLGPQRVSGLARCSIVNIHGAVLYDKYIRPEGEITDYRTQVSGVTPQHMVRATPFGEARLEILQLLKGKLVVGHDLKHDFNALKEDMSKYTIYDTSTDRLLWHEAKLQYYSRVSLRLLCKRLLHKNIQVLPGSLLGVGGCILPGTDILHLLLYVGMVRIADLRLLTPFLPPSCLACPLLPESLASARSHAVISALSSSSHLLTPLPNPSQGPQGHVDRLSGQLQDWGGSPLAPALPVSAEQLAGPLLCGRCQGHNGALQNLSATQSPARAALPWDVRLNFILIQG)Interferon-stimulated gene 20 kDa proteinQ9JL16Isg20[Ref.30232164]Ectopic expression of the interferon-induced 20-kDa exonuclease ISG20 suppressed replication of chikungunya virus and Venezuelan equine encephalitis virus, two mosquito-vectored RNA alphaviruses. AF-Q9JL16-F1QISG20 upregulated IFIT1 genes and inhi< bited translation of the alphavirus genome.30232164KWeiss CM, Trobaugh DW, Sun C, Lucas TM, Diamond MS, Ryman KD, Klimstra WB. ~The Interferon-Induced Exonuclease ISG20 Exerts Antiviral Activity through Upregulation of Type I Interferon Response Proteins DRAVPR0136MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGEP09913#IFIT2 (CIG-42, G10P2, IFI54, ISG54)4G1T[Ref.21190939]IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. AF-P09913-F121190939-Stawowczyk M, Van Scoy S, Kumar KP, Reich NC.5The interferon stimulated gene 54 promotes apoptosis. DRAVPR0137MSIVCSAEDSFRNLILFFRPRLKMYIQVEPVLDHLIFLSAETKEQILKKINTCGNTSAAELLLSTLEQGQWPLGWTQMFVEALEHSGNPLAARYVKPTLTDLPSPSSETAHDECLHLLTLLQPTLVDKLLINDVLDTCFEKGLLTVEDRNRISAAGNSGNESGVRELLRRIVQKENWFSTFLDVLRQTGNDALFQELTGGGCPEDNTDLANSSHRDGPAANECLLPAVDESSLETEAWNVDDILPEASCTDSSVTTESDTSLAEGSVSCFDESLGHNSNMGRDSGTMGSDSDESVIQTKRVSPEPELQLRPYQMEVAQPALDGKNIIICLPTGSGKTRVAVYITKDHLDKKKQASESGKVIVLVNKVMLAEQLFRKEFNPYLKKWYRIIGLSGDTQLKISFPEVVKSYDVIISTAQILENSLLNLESGDDDGVQLSDFSLIIIDECHHTNKEAVYNNIMRRYLKQKLRNNDLKKQNKPAIPLPQILGLTASPGVGAAKKQSEAEKHILNICANLDAFTIKTVKENLGQLKHQIKEPCKKFVIADDTRENPFKEKLLEIMASIQTYCQKSPMSDFGTQHYEQWAIQMEKKAAKDGNRKDRVCAEHLRKYNEALQINDTIRMIDAYSHLETFYTDEKEKKFAVLNDSDKSDDEASSCNDQLKGDVKKSLKLDETDEFLMNLFFDNKKMLKKLAENPKYENEKLIKLRNTILEQFTRSEESSRGIIFTKTRQSTYALSQWIMENAKFAEVGVKAHHLIGAGHSSEVKPMTQTEQKEVISKFRTGEINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVTSSGSGVTEREIVNDFREKMMYKAINRVQNMKPEEYAHKILELQVQSILEKKMKVKRSIAKQYNDNPSLITLLCKNCSMLVCSGENIHVIEKMHHVNMTPEFKGLYIVRENKALQKKFADYQTNGEIICKCGQAWGTMMVHKGLDLPCLKIRNFVVNFKNNSPKKQYKKWVELPIRFPDLDYSEYCLYSDED9Interferon-induced helicase C domain-containing protein 1Q8R5F7Ifih1"3TS9##6G19##6GKM##7BKQ##7NGA##7BKP[Ref.19656871]plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons AF-Q8R5F7-F1@Phosphorylation of Ser at position 289, 291, 302, 645, 648, 828.19656871##17942531Pichlmair A, Schulz O, Tan CP, Rehwinkel J, Kato H, Takeuchi O, Akira S, Way M, Schiavo G, Reis e Sousa C.##Loo YM, Fornek J, Crochet N, Bajwa G, Perwitasari O, Martinez-Sobrido L, Akira S, Gill MA, Garca-Sastre A, Katze MG, Gale M Jr.Activation of MDA5 requires higher-order RNA structures generated during virus infection.##Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity. DRAVPR0138MARLCAFLMVLAVLSYWPTCSLGCDLPQTHNLRNKRALTLLVQMRRLSPLSCLKDRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLDSFCNDLHQQLNDLQGCLMQQVGVQEFPLTQEDALLAVRKYFHRITVYLREKKHSPCAWEVVRAEVWRALSSSANVLGRLREEKInterferon alpha-1P01572Ifna10[Ref.9794439]IFN-alpha have antiviral activities AF-P01572-F1q`$There are five disulfide bonds between Cys24 and Cys122, Cys52 and Cys162.a$Glycosylation of Asn at position 101.9794439cAkwa Y, Hassett DE, Eloranta ML, Sandberg K, Masliah E, Powell H, Whitton JL, Bloom FE, Campbell ILTransgenic expression of IFN-alpha in the central nervous system of mice protects against lethal neurotropic viral infection but induces inflammation and neurodegeneration DRAVPR0139ySLTHRKFGGSGGSPFSGLSSIAVRSGSYLDAIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQYGriffithsin(GRFT)+Griffithsia sp. (strain Q66D336) (Red alga)P848012GTY##2GUD##2NUO##3LL2V[Ref.20032190]Human immunodeficiency virus type 1(HIV-1) RF:The potent cytoprotective and anti-replicative activities of GRFT in CEM-SS cells(EC50= 0.043 nM);##Human immunodeficiency virus type 1(HIV-1) ROJO:The potent cytoprotective and anti-replicative activities of GRFT in CEM-SS cells(EC50= 0.63 nM);##Human immunodeficienc< y virus type 1(HIV-1) ADA:The potent cytoprotective and anti-replicative activities of GRFT in CEM-SS cells(EC50= 0.50 nM);##Human immunodeficiency virus type 1(HIV-1) BaL:The potent cytoprotective and anti-replicative activities of GRFT in CEM-SS cells(EC50= 0.098 nM).GRFT blocked CD4-dependent glycoprotein (gp) 120 binding to receptor-expressing cells and bound to viral coat glycoproteins (gp120, gp41, and gp160) in a glycosylation-dependent manner.20032190}Mori T, O'Keefe BR, Sowder RC 2nd, Bringans S, Gardella R, Berg S, Cochran P, Turpin JA, Buckheit RW Jr, McMahon JB, Boyd MR.Broad-spectrum in vitro activity and in vivo efficacy of the antiviral protein griffithsin against emerging viruses of the family Coronaviridae DRAVPR0140VNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVGGSCQTTPokeweed antiviral Protein(PAP)leaves of pokeweed1QCGh[Ref:10493577]TMV:Possesses antiviral potency. Inhibits viral infection of plants (tobacco mosaic virus)10493577##10403789Kurinov, I. V., Myers, D. E., Irvin, J. D., & Uckun, F. M##Rajamohan, F., Venkatachalam, T. K., Irvin, J. D., & Uckun, F. M. (1999).$X-ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA substrate analogs##Pokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1 DRAVPR0141MQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSGGSGGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGSSGGQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSGGSGGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGSSGGQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSSSGGHHHHHH RSV F5-HBSynthetic constructNone /[Ref:38177138]SARS-CoV-2:IC50=250 nM,IC90=785nM38177138Bird, G. H., Patten, J. J., Zavadoski, W., Barucci, N., Godes, M., Moyer, B. M., Owen, C. D., DaSilva-Jardine, P., Neuberg, D. S., Bowen, R. A., Davey, R. A., & Walensky, L. D. (2024).jA stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential DRAVPR0142YPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAKHMGN2'Human mononuclear leukocyte, H. sapiensP05204HBV[Ref:19150374]HBV:At the concentrations of HMGN2 protein (100, 20, 5, and 1g/ml), the reduction of HBsAg was after 144h 31.63.0%, 11.21.8%, 6.01.6%, 4.441.3% after 72h, and 36.95.0%, 30.14.1%, 17.82.9%, 14.92.8%, respectively. HBeAg decreased after 72h to 66.74.1%, 522.8%, 40.84.9% and 10.82.7%, respectively, after 144h to 68.63.1%, 57.14.9%, 42.13.8% and 15.51.8%, respectively19150374QFeng Y, He F, Zhang P, Wu Q, Huang N, Tang H, Kong X, Li Y, Lu J, Chen Q, Wang B.tInhibitory effect of HMGN2 protein on human hepatitis B virus expression and replication in the HepG2.2.15 cell lineAnti-HBV DRAVPR0143MQSSILLIFAAFVACTYAQVSLPPGYAQKYPQYKYSKVARHPRDTTWEHNVGRGKIFGTLGSNDDSVFGRGGYKQDIFNDHRGRLSGQAYGSRVINDYGGSSILGGKLDWSNDNARAALDVHKEIGRGSGMKLSGDGVWKLDHNTRFSAGGNLQKNFGHNRPEFGIQGKIEHDFTnGlv2hemocytes,Trichoplusia niQ9GQM3T. ni gloverin AcMNPV-BVa[Ref:22401766]BV:When BV was incubated with gloverin-containing supernatants, the quantity of infectious BV, as measured by PFU, was reduced to 26.6 3.4 % and 8.3 1.6 % for TnGlv1 and TnGlv2, relative to that of BV incubated in the presence of vehicle (Figure DAB). A higher quantity of infectious virus was detected for BV incubated in the presence of TnGlv1 and TnGlv2 purified using Ni-NTA affinity columns (60.8 4.5 % and 36.3 5.8 % of vehicle, respectively. These results suggest that TnGlv1 and TnGlv2 inactivate baculovirus BV in vitro and that TnGlv2 has greater antiviral activity than TnGlv1Reverse PCR primers were designed to remove the stop codon while maintaining the sequence in frame for fusion of a C-terminal V5 epitope and 6x-His tag.< 22401766WMoreno-Habel DA, Biglang-awa IM, Dulce A, Luu DD, Garcia P, Weers PM, Haas-Stapleton EJ]Inactivation of the budded virus ofAutographa californicaM nucleopolyhedrovirus by gloverinAnti-BV DRAVPR0144MQLSTIFCFAVLIACARAQVFVKPGHKDEDLAWMRSMGKGHVFGTLGSTDGSLIGKLGYKQNIYNDQRGNLGGTAYGSRVINEYGGTSSFGGKLDWKNANDNARASLDVHKQVGGSSGMTLTGDGVWKLDSKTRLVAGGNLDKTFGYSKPELGIQAKIEHDFKTnGlv1 DRAVPR0145qGHMDIKKEIEAIKKEQEAIKKKIEAIEKELRQLANETTQ(A/D)LQLFLR(A/D)TTELRTFSILNRK(A/D)IDFLLQRMKQIEDKIEEIESKQKKIENEIARIKKLIGERY eboIZN39IQ Not AvailableEBOV-Z{[Ref:25287718]EBOV:IC50 = 320 nM/IC67 = 10 microM.The peptide mimic eboIZN39IQ combats Ebola virus by targeting its highly conserved N-trimer region within the GP protein, crucial for viral entry. It interferes with prehairpin intermediate formation during fusion, impeding membrane fusion essential for viral entry, offering promise for novel antiviral strategies against Ebola.25287718%Clinton TR, Weinstock MT, Jacobsen MT[Design and characterization of ebolavirus GP prehairpin intermediate mimics as drug targets DRAVPR01468AASFNKAMTNIVDAFTGVNDAITQTSQALQTVATALNKIQDVVNQQGNSLNHLTSQ 229E-HR1PS2 subunit of HCoV-229EP15423S2 5YL9##5ZHYSARS-CoV[Ref:29415501]SARS-CoV:5.7,13.2 M (IC50). Neither 229E-HR1P nor 229E-HR2P had significant cytotoxicity to these cells at concentrations up to 1,000 M29415501PXia, S., Xu, W., Wang, Q., Wang, C., Hua, C., Li, W., Lu, L., & Jiang, S. (2018)^Peptide-Based Membrane Fusion Inhibitors Targeting HCoV-229E Spike Protein HR1 and HR2 Domains Anti-SARS-CoV DRAVPR0147HRPYCGSKGGIGGGHGGGSGGFGGGGGFGGGGLGGGKPIGIGGGGGFGGGSGFGGGVGLKPNVGGGGGFGGGGGGFGGGIGLKPNVGGGGGFGGGIGLKPNVGGGGGFGGGGGGFGGGGGGFGGGFGGGKLIGGGIGWRRWWLCRKQRLRKVNHL ProcambarincrayfishProcambarus clarkii.WSSV[Ref:23685011]WSSV:led to lower viral replication and a partial protection against a subsequent challenge with the active virus23685011Zeng YProcambarin: a glycine-rich peptide found in the haemocytes of red swamp crayfish Procambarus clarkii and its response to white spot syndrome virus challenge. Anti-WSSV DRAVPR0148KPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRIRNase 2TLiver, lung, spleen, eosinophilic leukocytes; neutrophils, and monocytes, H. sapiensP10153RNASE2 1GQV##6SSORSV[Ref:9826755]RSV:IC50=35nM98267553Domachowske JB, Bonville CA, Dyer KD, Rosenberg HF.Evolution of antiviral activity in the ribonuclease A gene superfamily: evidence for a specific interaction between eosinophil-derived neurotoxin (EDN/RNase 2) and respiratory syncytial virusAnti-RSV DRAVPR0149RPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCTYADRPGRRFYVVACDNRDPRDSPRYPVVPVHLDTTIRNase 3#Eosinophilic leukocytes, H. sapiensP12724RNASE3 1DYT##1H1H RSV-group-B[Ref:9649619201]RSV:IC50=201nM96496199Domachowske JB, Dyer KD, Adams AG, Leto TL, Rosenberg HF.iEosinophil cationic protein/RNase 3 is another RNase A-family ribonuclease with direct antiviral activity DRAVPR0150kSGKSFKAGVCPPKKSAQCLRYKKPECQSDWQCPGKKRCCPDTCGIKCLDPVDTPNPTRRKPGKCPVTYGQCLMLNPPNFCEMDGQCKRDLKCCMGMCGKSCVSPVKAAntileukoproteinaseCTears, saliva, airway, gastrointestines, genital tracts,H. sapiensP03973SLPI4DOQ%[Ref:12108760]HIV-1:It inhibits HIV-112108760(Skott P, Lucht E, Ehnlund M, Bjrling E.Inhibitory function of secretory leukocyte proteinase inhibitor (SLPI) in human saliva is HIV-1 specific and varies with virus tropism DRAVPR0151_YETLIASVLGKLTGLWHNNSVDFMGHTCHFRRRPKVRKFKLYHEGKFWCPGWAPFEGRSRTKSRSGSSREAIKDFVRKALQNGLITQQDATVWVNSp-ALF1Scylla paramamosain (Mud crab)I1VGP3ALF1[Ref:22538350]WSSV:a significant reduction of IE1 transcript was detected when the crayfish Hpt cells incubated with WSSV pretreated with 5 or 10M of rSp-ALFs22538350MLiu HP, Chen RY, Zhang QX, Wang QY, Li CR, Peng H, Cai L, Zheng CQ, Wang KJ.pCharacterization of two isoforms of antiliopolysacchride factors (Sp-ALFs) from the mud crab Scylla paramamosain DRAVPR0152_YEALVASILGKLSGLWHSDTVDFMGHTCHIRRRPKFRK< FKLYHEGKFWCPGWTHLEGNSRTKSRSGSARDAIKDFVYKALQNKLITENNAAAWLKSp-ALF2A4ZPI9[Ref:22538350]WSSVa significant reduction of IE1 transcript was detected when the crayfish Hpt cells incubated with WSSV pretreated with 5 or 10M of rSp-ALFs DRAVPR0153QKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSGGSGGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGSSGGQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSGGSGGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGSSGGQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSSSGGHHHHHHSpike protein S2',5HB-H2P0DTC27Y9N SARS CoV-2[Ref:35757908]SARS-CoV-25Hb inhibits SARS-CoV-2 pseudovirus entry with sub-micromolar IC50. Unlike HR2-based peptides that cannot bind spike in the pre-fusion conformation, 5HB features with the capability of binding to pre-fusion spike. Furthermore, 5HB binds viral HR2 at both serological- and endosomal-pH, highlighting its entry-inhibition capacity when SARS-CoV-2 enters via either cell membrane fusion or endosomal route. Finally, we show that 5HB could neutralize S-mediated entry of the predominant SARS-CoV-2 variants and a wide spectrum of sarbecoviruses. These data provide proof-of-concept evidence that 5HB might be developed for the prevention and treatment of SARS-CoV-2 and other emerging sarbecovirus infections.35757908Lin, X.,Guo, L.,Lin, S.,Chen, Z.,Yang, F.,Yang, J.,Wang, L.,Wen, A.,Duan, Y.,Zhang, X.,Dai, Y.,Yin, K.,Yuan, X.,Yu, C.,He, B.,Cao, Y.,Dong, H.,Li, J.,Zhao, Q.,Lu, G.An engineered 5-helix bundle derived from SARS-CoV-2 S2 pre-binds sarbecoviral spike at both serological- and endosomal-pH to inhibit virus entry. DRAVPR0154bQGWEAVAAAVASKIVGLWRNEKTELLGHECKFTVKPYLKRFQVYYKGRMWCPGWTAIRGEASTRSQSGVAGKTAKDFVRKAFQKGLISQQEANQWLSSALFpm3&The black tiger shrimp, PenaeusmonodonA5A3I52JOB[Ref:27919648]WSSV:esults indicated that each of ALFPm3 interacting WSSV protein hindered the neutralizing ALFPm3antiviral activityresulting in lower shrimp survival.27919648UMethatham, T., Boonchuen, P., Jaree, P., Tassanakajon, A., & Somboonwiwat, K. (2017).kAntiviral action of the antimicrobial peptide ALFPm3 from Penaeus monodon against white spot syndrome virus DRAVPR0155VNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYV chCATH-B17the epithelium of the bursa of Fabricius,Gallus gallus 1D6A##1PAF ZIKV,HIV-1[Ref:10403789]ZIKV:similar to human cathelicidin against Zika virus, it directly Interact with the virus and TLR4/JNK/IRF3-Mediated Interferon Activation.HIV-1:Inhibits the replication of HIV-1 in human peripheral blood mononuclear cells with IC50 value of 14 nM8Rajamohan F.,Venkatachalam T.K.,Irvin J.D.,Uckun F.M.vPokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1.Anti-ZIKV,Anti-HVI DRAVPR0156[SNAMDGQKSRQLQRQLEWIGAWNAPGLGKDAYTVEAASVLQAVYETNARTLAARIQSIYEFAFTEPIPFPHCLKLARRLLELKQAASCPLPHB36.6 IAV(H1N1)HAIAV-H1N1[Ref;26845438]Influenza A/California/2009 (H1N1) IC50 = 0.18 g/mL, A/Puerto Rico/1934 (H1N1) IC50 = 0.58 g/mL, A/New Caledonia/1999 (H1N1) IC50 = 1.26 g/mL, A/Hong Kong/2003 (H5N1) IC50 = 12 g/mLThese changes in the sequence make HB36.6 present a much higher affinity with the HA segment of the influenza virus than its precursor26845438^P. S., Ward, A. B., Wilson, I. A., Dagley, A., Smee, D. F., Baker, D., & Fuller, D. H. (2016).A Computationally Designed Hemagglutinin Stem-Binding Protein Provides In Vivo Protection from Influenza Independent of a Host Immune Response DRAVPR0157NQGGIASCCRRHSKTQINREHLTHYEQHRPPCPIKAVVFYVIGGARICADPNKVWTKTSKAFLDGVHYQRQHTSSKVSFCsCCL17Spleen (high), liver, heart, gill and HK (moderate), and low in muscle, brain and intestine, half-smooth tongue sole,Cynoglossus semilaevisMV Not Avaialble26052018Hu YH, Zhang JCsCCL17, a CC chemokine of Cynoglossus semilaevis, induces leukocyte trafficking and promotes immune defense against viral<  infectionAnti-MV DRAVPR0158NQEFYGNCCLGHVKPMKIKGKRIESYRMQETDGDCHISAVVFLIKKKPSHVKQKTICANPQEAWVQELMAAVDSRNPKNCsCCL21@Induced in kidney, spleen, and liver, tongue sole,C. semilaevis DRAVPR0159*DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAA 1-42 H. sapiens HSV-1,IAV[Ref:25376108]HIV-1:59% reduction of viral replication was observed.[Ref:24988208]IAV:reduced IAV-induced interleukin-6 production25376108##24988208Bourgade K, Garneau H, Giroux G, Le Page AY, Bocti C, Dupuis G, Frost EH, Flp T Jr##White MR, Kandel R, Tripathi S, Condon D, Qi L, Taubenberger J, Hartshorn KL-Amyloid peptides display protective activity against the human Alzheimer's disease-associated herpes simplex virus-1##Alzheimer's associated -amyloid protein inhibits influenza A virus and modulates viral interactions with phagocytesAnti-HSV,Anti-IAV DRAVPR0160SMPFPKDCSQAMLNGDTTSGLYTIYLNGDKAQALEVFCDMTSDGGGWIVFLRRKNGRENFYQNWKAYAAGFGDRREEFWLGLDNLNKITAQGQYELRVDLRDHGETAFAVYDKFSVGDAKTRYKLKVEGYSGTAGDSMAYHNGRSFSTFDKDTDSAITNCALSYKGAFWYRNCHRVNLMGRYGDNNHSQGVNWFHWKGHEHSIQFAEMKLRPSNFRNLEG Tenascin-CHuman glioblastoma cellsP24821TNC6QNVHIV, SARS-CoV-2[Ref:36458980]36458980/Zuliani-Alvarez, L., & Piccinini, A. M. (2023).-A virological view of tenascin-C in infectionAnti-HIV,Anti-SARS-CoV-2 DRAVPR0161aAACARFIDDFCDTLTPNIYRPRDNGQRCYAVNGHRCDFTVFNTNNGGNPIRASTPNCKTVLRTAANRCPTGGRGKINPNAPFLFAIDPNDGDCSTNFY31Golden oyster mushroom,Pleurotus citrinopileatusP83811Antiviral protein CAPTMVoAntiviral protein Y3: at 2.0 ug/ml achieved 50.0% inhibition of tobacco mosaic virus (TMV, 20 ug/ml) lesions in Nicotiana glutinosa leaves. (provided by Chunfeng Wang). Submitted OCT-2002 to the SWISS-PROT data bank. It shows antiviral activity against Tobacco mosaic virus and antitumor activity against stomach cancer cells in vitro. Full sequence updated 03/12 GW.;Wu,L.-P., Wu,Z.-J., Lin,D, Fang F, Lin Q.-Y., Xie,L.-H.2002cCharacterization and amino acid sequence of y3, an antiviral protein from mushroom Coprinus comatusAnti-TMV DRAVPR0162PGSHMGDAQDKLKYLVKQLERALRELKKSLDELERSLEELEKNPSEDALVENNRLNVENNKIIVEVLRIILELAKASAKLA ABP-D25YACE2[Ref:33002032]SARS-Cov-2:The inhibitor consists of two  helical peptides homologues to protease domain (PD) of ACE2. Docking studies and molecular dynamic simulation revealed that the inhibitor binds exclusively at the ACE2 binding site of S protein. The computed binding affinity of the inhibitor is higher than the ACE2 and thus will likely out compete ACE2 for binding to S protein. Hence, the proposed inhibitor ABP-D25Y could be a potential blocker of S protein and receptor binding domain (RBD) attachment.33002032Jaiswal G, Kumar V.AIn-silicodesign of a potential inhibitor of SARS-CoV-2 S protein DRAVPR0163xSLTHRKFGGSGGSPFSGLSSIAVRSGSYLDAIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQYGRFTGriffithsiasp.3[Ref:20032190]SARS-Cov-252, >10 and 10 g/mL (IC50)O'Keefe, B. R., Giomarelli, B., Barnard, D. L., Shenoy, S. R., Chan, P. K., McMahon, J. B., Palmer, K. E., Barnett, B. W., Meyerholz, D. K., Wohlford-Lenane, C. L., & McCray, P. B., Jr (2010). DRAVPR0164rMASYKVNIPAGPLWSNAEAQQVGPKIAAAHQGNFTGQWTTVVESAMSVVEVELQVENTGIHEFKTDVLAGPLWSNDEAQKLGPQIAASYGAEFTGQWRTIVEGVMSVIQIKYTFMicrocystis viridis lectin%blue-green algae,Microcystis viridisQ9RHG4mvl 1ZHQ, 1ZHS>[Ref:9210678]HIV-1:The antiviral activity of CV-N is due, at least in part, to unique, high-affinity interactions of CV-N with the viral surface envelope glycoprotein gp120. The biological activity of CV-N is highly resistant to physicochemical denaturation, further enhancing its potential as an anti-HIV microbicide.9210678Boyd, M. R., Gustafson, K. R., McMahon, J. B., Shoemaker, R. H., O'Keefe, B. R., Mori, T., Gulakowski, R. J., Wu, L., Rivera, M. I., Laurencot, C. M., Currens, M. J., Cardellina, J. H., 2nd, Buckheit, R. W., Jr, Nara, P. L., Pannell, L. K., Sowder, R. C., 2nd, & Henderson, L. E. (1997).Isolation and characterization of a mannan-binding lectin from the freshwater cyanobacterium (blue-green algae) Microcystis vir< idis DRAVPR0165Etears, saliva, airway, gastrointestines, genital tracts,Homo sapiensELANE 2Z7F, 4DOQ>[Ref:15731023]HIV-1:SLPI was found to be the most potent anti-HIV-1 factor among several innate inhibitory molecules, namely, virus-specific antibodies, mucins, and thrombospondins, identified and purified from saliva.Moderate activity is also exerted against HIV-2 strains, but only when the concentration of SLPI exceeds the norm.The mechanism by which SLPI inhibits HIV-1 infection is still elusive, but it appears to involve the host cell target rather than binding to the virus.Evidence suggests that SLPI blocks HIV-1 internalization in a dose-dependent manner rather than binding to CD4.McNeely et al. found that SLPI most likely inhibits a step of viral infection that occurs after virus binding but before reverse transcription. They also succeeded in preventing HIV infection of macrophages after pretreatment with SLPI.QN-terminal transglutaminase domain substrate and a C-terminal four-disulfide core15731023:Doumas, S., Kolokotronis, A., & Stefanopoulos, P. (2005).SAnti-inflammatory and antimicrobial roles of secretory leukocyte protease inhibitor DRAVPR0166]VGSEVSDKRTCVSLTTQRLPVSRIKTYTITEGSLRAVIFITKRGLKVCADPQATWVRDVVRSMDRKSNTRNNMIQTKPTGTQQSTNTAVTLTGXCL1 CD8+ T cells,Homo sapiensQ9HWT82JPI`[Ref:26085164]HIV:This CD8+ T cells derived chemokine inhibits a broad spectrum of HIV isolates.Interestingly, introducing a disulfide bond between A36C and A49C mutants locks the chemokine conformation to the all-beta dimeric form (dubbed CC5), which is indeed a potent HIV inhibitor with high affinity to heparin26085164EGuzzo, C., Fox, J. C., Miao, H., Volkman, B. F., & Lusso, P. (2015). hStructural Determinants for the Selective Anti-HIV-1 Activity of the All- Alternative Conformer of XCL1 DRAVPR0167DKPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNKCXCL12 Homo sapiensP48061CXCL12,SDF1,SDF1A,SDF1B2KOL[Ref:33872329]HIV:a CXCL12 variant that binds CXCR4 with comparable affinity compared to CXCL12 but does not internalize the receptor.resistance to CXCL12 originates from its reduced capacity to competitively inhibit virus binding to CXCR4.33872329Armani-Tourret M, Zhou Z, Gasser R, Staropoli I, Cantaloube-Ferrieu V, Benureau Y, Garcia-Perez J, Prez-Olmeda M, Lorin V, Puissant-Lubrano B, Assoumou L, Delaugerre C, Lelivre JD, Lvy Y, Mouquet H, Martin-Blondel G, Alcami J, Arenzana-Seisdedos F, Izopet J, Colin P, Lagane B.tMechanisms of HIV-1 evasion to the antiviral activity of chemokine CXCL12 indicate potential links with pathogenesis DRAVPR01689AQEPVKGPVSTKPGSCPIILIRCAMLNPPNRCLKDTDCPGIKKCCEGSCGMACFVPQElafinskin,Homo sapiensP19957PI32REL HIV-1, HSV-2x[Ref:23637403]HIV-1Serine protease inhibitor elafin (E) and its precursor, trappin-2 (Tr), have been associated with mucosal resistance to HIV-1 infection. We recently showed that Tr/E are among principal anti-HIV-1 molecules in cervicovaginal lavage (CVL) fluid, that E is <"130 times more potent than Tr against HIV-1, and that Tr/E inhibited HIV-1 attachment and transcytosis across human genital epithelial cells (ECs). [Ref:22345469]HSV-2:Since herpes simplex virus 2 (HSV-2) is a major sexually transmitted infection and risk factor for HIV-1 infection and transmission, we assessed Tr/E contribution to defense against HSV-2.23637403##22345469Drannik, A. G., Nag, K., Sallenave, J. M., & Rosenthal, K. L. (2013)##Drannik, A. G., Nag, K., Yao, X. D., Henrick, B. M., Jain, S., Ball, T. B., Plummer, F. A., Wachihi, C., Kimani, J., & Rosenthal, K. L. (2012). Antiviral activity of trappin-2 and elafin in vitro and in vivo against genital herpes;##Anti-HIV-1 activity of elafin is more potent than its precursor's, trappin-2, in genital epithelial cellsAnti-HIV,Anti-HSV DRAVPR01699KRRPAKAWSGRRTRLCCHRVPSPNSTNLKGHHVRLCKPCKLEPEPRLWVVPGALPQVAP-57 Qantibody detection mainly in stomach, colon, and epityphlon tissues,Homo sapiensQ6UWK7GPR15LG8ZQELVS[Ref:25585381]LV:Lentivirus (MEC 16.50 ug/ml) and Adenovirus Ad5 (MEC >200 ug/ml)./predicte< d two disulfide bonds: C1-C4 and C2-C3.25585381VYang M, Tang M, Ma X, Yang L, He J, Peng X, Guo G, Zhou L, Luo N, Yuan Z, Tong A. 2015FAP-57/C10orf99 is a new type of multifunctional antimicrobial peptide.Anti-LV DRAVPR0170SVN cyanobacterium,Scytonema varium Not available 2QSK##2JMV[Ref:2614152]HIV:Has strong anti-HIV activity against T-tropic strains of HIV-1 and weaker activity against M-tropic strains of HIV-1. Inhibits HIV-1 fusion and infection of CD4 LTR beta-gal cells in vitro. Inhibits fusion of HIV infected CEM-SS cells with uninfected CEM-SS cells, and fusion of HIV-1 Env expressing HL2/3 cells with CD4 LTR beta-gal cells. Binds to HIV gp120, HIV gp160 and to a lesser extent HIV gp41. Binding to HIV gp120 is glycosylation dependent. Binds with high specificity to the tetrasaccharide Man-alpha-1,2-Man-alpha-1,6-Man-alpha-1,6-Man and also binds the higher-order oligosaccharides oligomannose 8 and oligomannose 9. Does not bind to monosaccharides, complex or hybrid N-linked oligosaccharides or chitin.kThe five disulfide bonds are proposed as Cys7-Cys55, Cys20-Cys32, Cys26-Cys38, Cys68-Cys80, and Cys74-Cys862614152Bokesch, H. R., O'Keefe, B. R., McKee, T. C., Pannell, L. K., Patterson, G. M., Gardella, R. S., Sowder, R. C., 2nd, Turpin, J., Watson, K., Buckheit, R. W., Jr, & Boyd, M. R. (2003).QA potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium DRAVPR0171MAACARFIDDFCDTLTPNIYRPRDNGQRCYAVNGHRCDFTVFNTNNGGNPIRASTPNCKTVLRTAANRCPTGGRGKINAntiviral protein Y3s[Ref:32711757]TMV:Compared with the control (TMV mixed with PBS buffer), the TMV concentrations of the tobacco plants treated with the different proteins were significantly lower. Y3 shown to be able to activate the expression of a number of defence-related genes.Some of the mechanisms of its protection can be attributed to a direct interaction between Y3 and TMV-CP. When Phe at the 43rd amino acid of Y3 was replaced by Cys, the predicted disulfide bonds were changed, and the interaction of Y3-CP and Y3T1 (mutated Y3) could not be detected by BiFCdisulfide bonds32711757-Xiao H, Bian Y, Huang H, Zhang Z, Wu L, Wu L.MInhibitory effect of protein Y3 from Coprinus comatus on tobacco mosaic virus DRAVPR01722FFLLFLQGAAGNSVLCRIRGGRCHVGSCHFPERHIGRCSGFQACCIRTWG Apl-AvBD16Peking duck,Anas platyrhynchosI1W762DHV[ref:23112840]DHV:The level of expression of AvBD16 in both the bursa of Fabricius and the spleen was increased significantly at 24 h after infection (P<0.05 or P<0.01), and significant induction was observed in the liver (at 24 h and 96 h) in response to infection. the mRNA of the Apl_AvBD16 was upregulated in various immune tissues and in the livers of ducks following DHV infection. These findings provide evidence that the defensins activate the immune response to combat microbial infection.23112840;Ma D, Zhang K, Zhang M, Xin S, Liu X, Han Z, Shao Y, Liu S.RIdentification, expression and activity analyses of five novel duck beta-defensinsAnti-DHV DRAVPR01733EEESEVAHLRVRRGFGCPLNQGACHRHCRSIRRRGGYCSGIIKQTCTCYRN Hedefensin$Hemolymph,Haemaphysalis longicornis A0A2D1CLH7 HEdefensinLGTVk[Ref:27871830]LGTV:HEdefensin at 37 C for 2 h reduced the number of fluorescence-positive viral foci as compared to the medium-treated virus. Such a reduction is equivalent to a 99.2% foci reduction.Similarly, cells infected with LGTV treated with HEdefensin produced almost a five-fold lower virus yield as compared to cells infected with a medium-treated virus27871830pTalactac MR, Yada Y, Yoshii K, Hernandez EP, Kusakisako K, Maeda H, Galay RL, Fujisaki K, Mochizuki M, Tanaka T.Characterization and antiviral activity of a newly identified defensin-like peptide, HEdefensin, in the hard tick Haemaphysalis longicornis Anti-LGTV DRAVPR0174LGQTPSQWFAIQHINNNANLQCNVEMQRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSDNISRNCHNSSSRVRITVCNITSRRRTPYTQCRYQPRRSLEYYTVACNPRTPQDSPMYPVVPVHLDGTFmEar2 M. musculusP97425Ear2PVM[Ref:26184157]PVM:mEar 2 has antiviral activity against pneumonia virus of mice (PVM), a rodent virus related to hRSV; expression<  of mEars is diminished in mouse lung tissue in response to PVM infection in vivo26184157Rosenberg H. F. (2015).Eosinophil-Derived Neurotoxin (EDN/RNase 2) and the Mouse Eosinophil-Associated RNases (mEars): Expanding Roles in Promoting Host DefenseAnti-PVM DRAVPR0175Microcystis viridis lectin(MVL)%Blue-green algae,Microcystis viridis 1ZHQ##1ZhS HIV-1,HCVz[Ref:37012452]HCV,HIV-1:The lectin blocks fusion of cells with the HCV and HIV-1 with an IC50value of approximately 30nM37012452cSingh, U., Gandhi, H. A., Nikita, Bhattacharya, J., Tandon, R., Tiwari, G. L., & Tandon, R. (2023).<Cyanometabolites: molecules with immense antiviral potentialAnti-HIV,Anti-HSCV DRAVPR0176RSSFSPAAPLPPGTKHPCLPLSCPPCPDEECPTCEILPPCELCPEIHIGCDCPFHHSCLCDQPACPPCDFPFGSLINKGGYRGMj-sty(Mainly gills and hemocytes;Marsupenaeus[Ref:26439413]WSSV:The transcription profiles demonstrated that in both of gills and hepatopancreas Mj-sty mRNA was down-regulated at the first several hours after infection of WSSV following with up-regulated to the highest level at 24h 48h, then considerably down-regulated at 48h 72h, and at the end of the experimental hours it returned to the half levels of the controls. Some penaeidins showed a similar expression profiles with Mj-sty against WSSV infection.26439413lLiu, H. T., Wang, J., Mao, Y., Liu, M., Niu, S. F., Qiao, Y., Su, Y. Q., Wang, C. Z., & Zheng, Z. P. (2015).|Identification and expression analysis of a novel stylicin antimicrobial peptide from Kuruma shrimp (Marsupenaeus japonicus)     dMbP?_*+%"d??U      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~                   ~ s@                    ! 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