ID A9Y6A9_9HIV1 Unreviewed; 498 AA. AC A9Y6A9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 28-FEB-2018, entry version 76. 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; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. 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 RT from Nairobi, Kenya reveals a high proportion of intersubtype RT recombinants."; RL AIDS Res. Hum. Retroviruses 24:865-872(2008). CC -!- SUBCELLULAR LOCATION: Matrix protein p17: Virion CC {ECO:0000256|RuleBase:RU004487}. Host nucleus CC {ECO:0000256|RuleBase:RU004487}. Host cytoplasm CC {ECO:0000256|RuleBase:RU004487}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm CC {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS00558641}. CC Host nucleus {ECO:0000256|RuleBase:RU004487, CC ECO:0000256|SAAS:SAAS00558562}. Virion CC {ECO:0000256|RuleBase:RU004487}. CC -!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the CC viral protease yield mature proteins. CC {ECO:0000256|RuleBase:RU004487}. CC -!- SIMILARITY: Belongs to the primate lentivirus group gag CC polyprotein family. {ECO:0000256|SAAS:SAAS00558534}. 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 ProteinModelPortal; A9Y6A9; -. 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}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000128438}; KW Host cytoplasm {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS00053376}; KW Host nucleus {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS00053394}; KW Host-virus interaction {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS00997666}; KW Metal-binding {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS00916097}; KW Repeat {ECO:0000256|SAAS:SAAS00994306}; KW Ribosomal frameshifting {ECO:0000256|SAAS:SAAS00053419}; KW RNA-binding {ECO:0000256|RuleBase:RU004487, KW ECO:0000256|SAAS:SAAS00053246}; KW Viral budding {ECO:0000256|SAAS:SAAS00994480}; KW Viral budding via the host ESCRT complexes KW {ECO:0000256|SAAS:SAAS00994355}; KW Viral nucleoprotein {ECO:0000256|RuleBase:RU004487}; KW Viral release from host cell {ECO:0000256|SAAS:SAAS00053410}; KW Virion {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS00997935}; KW Zinc {ECO:0000256|RuleBase:RU004487, ECO:0000256|SAAS:SAAS00915002}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047, KW ECO:0000256|SAAS:SAAS00915647}. FT DOMAIN 389 404 CCHC-type. {ECO:0000259|PROSITE:PS50158}. FT DOMAIN 411 426 CCHC-type. {ECO:0000259|PROSITE:PS50158}. FT COILED 94 117 {ECO:0000256|SAM:Coils}. 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 //