GAG_EIAVC
ID GAG_EIAVC Reviewed; 486 AA.
AC P69731; P03351;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 79.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p26;
DE Short=CA;
DE Contains:
DE RecName: Full=p1;
DE Contains:
DE RecName: Full=Nucleocapsid protein p11;
DE Short=NC;
DE Contains:
DE RecName: Full=p9;
GN Name=gag;
OS Equine infectious anemia virus (isolate CL22) (EIAV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=31675;
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1318398; DOI=10.1128/jvi.66.7.4085-4097.1992;
RA Perry S.T., Flaherty M.T., Kelley M.J., Clabough D.L., Tronick S.R.,
RA Coggins L., Whetter L., Lengel C.R., Fuller F.;
RT "The surface envelope protein gene region of equine infectious anemia virus
RT is not an important determinant of tropism in vitro.";
RL J. Virol. 66:4085-4097(1992).
CC -!- FUNCTION: Matrix protein p15 forms the outer shell of the core of the
CC virus, lining the inner surface of the viral membrane. {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p26 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p11 encapsulates and protects viral
CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
CC fingers (By similarity). {ECO:0000250}.
CC -!- FUNCTION: p9 plays a role in budding of the assembled particle by
CC interacting with PDCD6IP/AIP1. {ECO:0000250}.
CC -!- SUBUNIT: [p9]: Interacts with human PDCD6IP/AIP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. p9 contains one L domain: a LYPX(n)L motif,
CC which interacts with PDCD6IP/AIP1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the equine lentivirus group gag polyprotein
CC family. {ECO:0000305}.
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; M87581; AAA43003.1; -; Genomic_RNA.
DR PIR; A03949; FOLJEV.
DR RefSeq; NP_056901.1; NC_001450.1.
DR BMRB; P69731; -.
DR SMR; P69731; -.
DR GeneID; 1489984; -.
DR KEGG; vg:1489984; -.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
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; IPR014834; Gag_p15.
DR InterPro; IPR045345; Gag_p24_C.
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; PF08723; Gag_p15; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 2.
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; Disulfide bond; Host-virus interaction; Metal-binding;
KW Repeat; Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW Virion; Zinc; Zinc-finger.
FT CHAIN 1..124
FT /note="Matrix protein p15"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038776"
FT CHAIN 125..359
FT /note="Capsid protein p26"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038777"
FT PEPTIDE 355..359
FT /note="p1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272314"
FT CHAIN 360..454
FT /note="Nucleocapsid protein p11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038778"
FT CHAIN 436..486
FT /note="p9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038779"
FT ZN_FING 381..398
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 400..417
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 414..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 457..461
FT /note="LYPX(n)L motif"
FT COMPBIAS 417..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 322..342
FT /evidence="ECO:0000250"
SQ SEQUENCE 486 AA; 54809 MW; 97137FA5933D1DDA CRC64;
MGDPLTWSKA LKKLEKVTVQ GSQKLTTGNC NWALSLVDLF HDTNFVKEKD WQLRDVIPLL
EDVTQTLSGQ EREAFERTWW AISAVKMGLQ INNVVDGKAS FQLLRAKYEK KTANKKQSEP
SEEYPIMIDG AGNRNFRPLT PRGYTTWVNT IQTNGLLNEA SQNLFGILSV DCTSEEMNAF
LDVVPGQAGQ KQILLDAIDK IADDWDNRHP LPNAPLVAPP QGPIPMTARF IRGLGVPRER
QMEPAFDQFR QTYRQWIIEA MSEGIKVMIG KPKAQNIRQG AKEPYPEFVD RLLSQIKSEG
HPQEISKFLT DTLTIQNANE ECRNAMRHLR PEDTLEEKMY ACRDIGTTKQ KMMLLAKALQ
TGLAGPFKGG ALKGGPLKAA QTCYNCGKPG HLSSQCRAPK VCFKCKQPGH FSKQCRSVPK
NGKQGAQGRP QKQTFPIQQK SQHNKSVVQE TPQTQNLYPD LSEIKKEYNV KEKDQVEDLN
LDSLWE
