ID A9Y6A9_9HIV1 Unreviewed; 498 AA. AC A9Y6A9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 26-FEB-2020, entry version 85. DE RecName: Full=Gag polyprotein {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS00998370}; GN Name=gag {ECO:0000313|EMBL:ABW86733.1}; OS Human immunodeficiency virus 1. OC Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABW86733.1, ECO:0000313|Proteomes:UP000128438}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ABW86733.1, ECO:0000313|Proteomes:UP000128438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ML1990 {ECO:0000313|EMBL:ABW86733.1}; RX PubMed=18544023; DOI=10.1089/aid.2007.0200; RA Land A.M., Ball T.B., Luo M., Rutherford J., Sarna C., Wachihi C., RA Kimani J., Plummer F.A.; RT "Full-length HIV type 1 proviral sequencing of 10 highly exposed women from RT Nairobi, Kenya reveals a high proportion of intersubtype recombinants."; RL AIDS Res. Hum. Retroviruses 24:865-872(2008). CC -!- FUNCTION: Capsid protein. {ECO:0000256|SAAS:SAAS01239565}. CC -!- FUNCTION: Matrix protein. {ECO:0000256|SAAS:SAAS01239606}. CC -!- FUNCTION: Nucleocapsid protein. {ECO:0000256|SAAS:SAAS01239538}. CC -!- FUNCTION: capsid protein. {ECO:0000256|SAAS:SAAS01239633}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|RuleBase:RU004487, CC ECO:0000256|SAAS:SAAS01052174}. Host nucleus CC {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS01052953}. Virion CC {ECO:0000256|RuleBase:RU004487}. CC -!- SUBCELLULAR LOCATION: [atrix protein p1]: Virion CC {ECO:0000256|RuleBase:RU004487}. Host nucleus CC {ECO:0000256|RuleBase:RU004487}. Host cytoplasm CC {ECO:0000256|RuleBase:RU004487}. CC -!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral CC protease yield mature proteins. {ECO:0000256|RuleBase:RU004487}. CC -!- SIMILARITY: Belongs to the primate lentivirus group gag polyprotein CC family. {ECO:0000256|SAAS:SAAS01052372}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU110092; ABW86733.1; -; Genomic_DNA. DR Proteomes; UP000128438; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW. DR Gene3D; 1.10.1200.30; -; 1. DR Gene3D; 1.10.150.90; -; 1. DR Gene3D; 1.10.375.10; -; 1. DR InterPro; IPR000721; Gag_p24. DR InterPro; IPR014817; Gag_p6. DR InterPro; IPR000071; Lentvrl_matrix_N. DR InterPro; IPR012344; Matrix_HIV/RSV_N. DR InterPro; IPR008916; Retrov_capsid_C. DR InterPro; IPR008919; Retrov_capsid_N. DR InterPro; IPR010999; Retrovr_matrix. DR InterPro; IPR001878; Znf_CCHC. DR InterPro; IPR036875; Znf_CCHC_sf. DR Pfam; PF00540; Gag_p17; 1. DR Pfam; PF00607; Gag_p24; 1. DR Pfam; PF08705; Gag_p6; 1. DR Pfam; PF00098; zf-CCHC; 2. DR PRINTS; PR00234; HIV1MATRIX. DR SMART; SM00343; ZnF_C2HC; 2. DR SUPFAM; SSF47836; SSF47836; 1. DR SUPFAM; SSF47943; SSF47943; 1. DR SUPFAM; SSF57756; SSF57756; 1. DR PROSITE; PS50158; ZF_CCHC; 2. PE 3: Inferred from homology; KW Capsid protein {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS00132057}; KW Host cytoplasm {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS01052578}; KW Host nucleus {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS01052847}; KW Host-virus interaction {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS00443752}; KW Metal-binding {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS01024529}; Repeat {ECO:0000256|SAAS:SAAS00994306}; KW Ribosomal frameshifting {ECO:0000256|SAAS:SAAS01052335}; KW RNA-binding {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS01052574}; KW Viral budding {ECO:0000256|SAAS:SAAS00994480}; KW Viral budding via the host ESCRT complexes {ECO:0000256|SAAS:SAAS00994355}; KW Viral nucleoprotein {ECO:0000256|RuleBase:RU004487}; KW Viral release from host cell {ECO:0000256|SAAS:SAAS00443592}; KW Virion {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS00954881}; KW Zinc {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS01024443}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047, KW ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS01024440}. FT DOMAIN 389..404 FT /note="CCHC-type" FT /evidence="ECO:0000259|PROSITE:PS50158" FT DOMAIN 411..426 FT /note="CCHC-type" FT /evidence="ECO:0000259|PROSITE:PS50158" FT REGION 107..128 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 218..243 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 435..498 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 111..128 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 474..498 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 498 AA; 55282 MW; 1B187BA7E8F53B83 CRC64; MGARASVLSG GKLDAWEKIR LRPGGKKKYR MKHLVWASRE LERFALNPSL LETTEGCQQI MEQLQSALRT GTEELRSLFN TVATLYCVHQ RIDVKDTKEA LDKVEEIKNK SNQKTQQAAA DTGSSSTVSQ NYPIVQNAQG QLTHQALSPR TLNAWVKVIE EKAFSPEVIP MFSALSEGAT PQDLNMMLNI VGGHQAAMQM LKDTINEEAA EWDRTHPVQA GPIAPGQIRE PRGSDIAGTT STPQEQIRWM TNNPPIPVGD IYKRWIILGL NKIVRMYSPV SILDIKQGPK EPFRDYVDRF FKTLRAEQAT QEVKNWMTDT LLVQNANPDC KSILRALGPG ATLEEMMTSC QGVGGPGHKA RVLAEAMSQL NSTNIMMQKG NFRGQKRIKC FNCGKEGHLA RNCRAPRKKG CWKCGKEGHQ MKDCTERQAN FLGKLWPSSK GRPGNFPQNK IEPTAPPAEL LGMGEEIASP PKQDQEGRGQ TPPSISLKSL FGNDPLSQ //