ID A9Y6A9_9HIV1 Unreviewed; 498 AA. AC A9Y6A9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 09-JAN-2013, entry version 41. 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; 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-1 Proviral Sequencing of Ten Highly Exposed Women RT from Nairobi, Kenya Reveals a High Proportion of Intersubtype RT Recombinants."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. 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: Capsid protein p24: Virion (By similarity). CC -!- SUBCELLULAR LOCATION: Matrix protein p17: Virion (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleocapsid protein p7: Virion (By CC 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 --------------------------------------------------------------------------- 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:0019028; C:viral capsid; 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:0019076; P:viral release from host cell; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.90; Matrix_HIV/RSV_N; 1. DR Gene3D; 1.10.1200.30; Retrov_capsid_C; 1. DR Gene3D; 1.10.375.10; Retrov_capsid_N; 1. DR Gene3D; 4.10.60.10; Znf_CCH_retrovir; 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; Retrov_capsid_C; 1. DR SUPFAM; SSF47943; Retrov_capsid_N; 1. DR SUPFAM; SSF47836; Retrovir_matrix; 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; Metal-binding; KW Repeat; 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 //