ID   GAG_EIAVY               Reviewed;         486 AA.
AC   P69732; P03351;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-NOV-2023, entry version 95.
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 (strain Wyoming) (EIAV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Equine infectious anemia virus.
OX   NCBI_TaxID=11672;
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=3003905; DOI=10.1126/science.3003905;
RA   Stephens R.M., Casey J.W., Rice N.R.;
RT   "Equine infectious anemia virus gag and pol genes: relatedness to visna and
RT   AIDS virus.";
RL   Science 231:589-594(1986).
RN   [2]
RP   CHARACTERIZATION OF P26.
RX   PubMed=9165100; DOI=10.1016/s0167-4838(96)00215-4;
RA   Birkett A.J., Yelamos B., Rodriguez-Crespo I., Gavilanes F., Peterson D.L.;
RT   "Cloning, expression, purification, and characterization of the major core
RT   protein (p26) from equine infectious anemia virus.";
RL   Biochim. Biophys. Acta 1339:62-72(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF P26.
RX   PubMed=9931251; DOI=10.1006/jmbi.1998.2443;
RA   Jin Z., Jin L., Peterson D.L., Lawson C.L.;
RT   "Model for lentivirus capsid core assembly based on crystal dimers of EIAV
RT   p26.";
RL   J. Mol. Biol. 286:83-93(1999).
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   -!- CAUTION: The original EMBL accession numbers (M11337 and M14855)
CC       assigned to this isolate (isolate Wyoming) have been made secondary to
CC       M16575 which is from a different isolate (clone 1365). {ECO:0000305}.
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DR   PIR; A03949; FOLJEV.
DR   PDB; 1EIA; X-ray; 2.70 A; A=140-346.
DR   PDB; 1HEK; X-ray; 2.80 A; A/B=1-124.
DR   PDB; 2BL6; NMR; -; A=381-417.
DR   PDB; 2EIA; X-ray; 2.70 A; A/B=141-346.
DR   PDB; 2K84; NMR; -; A=457-486.
DR   PDB; 2R03; X-ray; 2.59 A; B=456-463.
DR   PDB; 4ZUT; X-ray; 2.60 A; C=21-32.
DR   PDB; 4ZUU; X-ray; 2.20 A; C=172-180.
DR   PDB; 4ZUW; X-ray; 2.60 A; C=21-32.
DR   PDBsum; 1EIA; -.
DR   PDBsum; 1HEK; -.
DR   PDBsum; 2BL6; -.
DR   PDBsum; 2EIA; -.
DR   PDBsum; 2K84; -.
DR   PDBsum; 2R03; -.
DR   PDBsum; 4ZUT; -.
DR   PDBsum; 4ZUU; -.
DR   PDBsum; 4ZUW; -.
DR   BMRB; P69732; -.
DR   SMR; P69732; -.
DR   ELM; P69732; -.
DR   EvolutionaryTrace; P69732; -.
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; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 1.10.150.90; Immunodeficiency lentiviruses, gag gene matrix protein p17; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 2.
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   PANTHER; PTHR40389; ENDOGENOUS RETROVIRUS GROUP K MEMBER 24 GAG POLYPROTEIN-RELATED; 1.
DR   PANTHER; PTHR40389:SF3; IGE-BINDING PROTEIN; 1.
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; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Disulfide bond; Host-virus interaction;
KW   Metal-binding; Repeat; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral matrix protein;
KW   Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..124
FT                   /note="Matrix protein p15"
FT                   /id="PRO_0000038780"
FT   CHAIN           125..354
FT                   /note="Capsid protein p26"
FT                   /id="PRO_0000038781"
FT   PEPTIDE         355..359
FT                   /note="p1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000272315"
FT   CHAIN           360..435
FT                   /note="Nucleocapsid protein p11"
FT                   /id="PRO_0000038782"
FT   CHAIN           436..486
FT                   /note="p9"
FT                   /id="PRO_0000038783"
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   HELIX           7..16
FT                   /evidence="ECO:0007829|PDB:1HEK"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1HEK"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:4ZUW"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:1HEK"
FT   HELIX           53..64
FT                   /evidence="ECO:0007829|PDB:1HEK"
FT   HELIX           71..86
FT                   /evidence="ECO:0007829|PDB:1HEK"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:1HEK"
FT   HELIX           98..108
FT                   /evidence="ECO:0007829|PDB:1HEK"
FT   HELIX           146..152
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   TURN            153..157
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           159..168
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           174..183
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           188..208
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   TURN            232..235
FT                   /evidence="ECO:0007829|PDB:2EIA"
FT   HELIX           238..242
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           247..269
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           285..297
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           305..316
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           320..325
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   TURN            326..328
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   HELIX           335..341
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   TURN            342..344
FT                   /evidence="ECO:0007829|PDB:1EIA"
FT   STRAND          383..386
FT                   /evidence="ECO:0007829|PDB:2BL6"
FT   TURN            393..395
FT                   /evidence="ECO:0007829|PDB:2BL6"
FT   HELIX           410..413
FT                   /evidence="ECO:0007829|PDB:2BL6"
FT   STRAND          463..465
FT                   /evidence="ECO:0007829|PDB:2K84"
FT   HELIX           466..470
FT                   /evidence="ECO:0007829|PDB:2K84"
FT   TURN            471..476
FT                   /evidence="ECO:0007829|PDB:2K84"
FT   HELIX           477..479
FT                   /evidence="ECO:0007829|PDB:2K84"
FT   TURN            480..482
FT                   /evidence="ECO:0007829|PDB:2K84"
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
//