ID A9Y6A9_9HIV1 Unreviewed; 498 AA. AC A9Y6A9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-FEB-2014, entry version 48. DE SubName: Full=Gag protein; GN Name=gag; OS Human immunodeficiency virus 1. OC Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. OX NCBI_TaxID=11676; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ML1990; 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 -!- FUNCTION: Capsid protein p24 forms the conical core of the virus CC that encapsulates the genomic RNA-nucleocapsid complex (By CC similarity). CC -!- FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc CC fingers (By similarity). CC -!- SUBCELLULAR LOCATION: Matrix protein p17: Virion (By similarity). CC -!- SUBCELLULAR LOCATION: Virion (By similarity). CC -!- PTM: Specific enzymatic cleavages by the viral protease yield CC mature proteins (By similarity). CC -!- SIMILARITY: Contains 2 CCHC-type zinc fingers. CC -!- SIMILARITY: Contains CCHC-type zinc fingers. 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 SMR; A9Y6A9; 2-430. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-KW. 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 GO; GO:0019076; P:viral release from host cell; 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 Gene3D; 4.10.60.10; -; 1. DR InterPro; IPR000721; Gag_p24. DR InterPro; IPR014817; Gag_p6. DR InterPro; IPR000071; Lentvrl_matrix_N. DR InterPro; IPR012344; Matrix_N_HIV/RSV. DR InterPro; IPR008916; Retrov_capsid_C. DR InterPro; IPR008919; Retrov_capsid_N. DR InterPro; IPR010999; Retrovr_matrix_N. DR InterPro; IPR001878; Znf_CCHC. 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; SSF47353; SSF47353; 1. 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 AIDS; Capsid protein; Host cytoplasm; Host nucleus; KW Host-virus interaction; Metal-binding; Repeat; KW Ribosomal frameshifting; RNA-binding; Viral budding; KW Viral budding via the host ESCRT complexes; Viral nucleoprotein; KW Virion; Virus exit from host cell; Zinc; Zinc-finger. 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 //