ID   GAG_OMVVS               Reviewed;         446 AA.
AC   P16900;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Gag polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p16;
DE   Contains:
DE     RecName: Full=Capsid protein p25;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p14;
GN   Name=gag;
OS   Ovine maedi visna related virus (strain South Africa) (SA-OMVV) (Ovine
OS   lentivirus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11664;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2158181; DOI=10.1016/0042-6822(90)90428-t;
RA   Querat G., Audoly G., Sonigo P., Vigne R.;
RT   "Nucleotide sequence analysis of SA-OMVV, a visna-related ovine lentivirus:
RT   phylogenetic history of lentiviruses.";
RL   Virology 175:434-447(1990).
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: 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. Nucleocapsid protein p14 contains one L
CC       domain: a PTAP/PSAP motif, which interacts with the UEV domain of
CC       TSG101 (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC   -!- SIMILARITY: Belongs to the Ovine/caprine lentivirus group gag
CC       polyprotein family. {ECO:0000305}.
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DR   EMBL; M34193; AAA46779.1; -; Genomic_DNA.
DR   EMBL; M31646; AAA66811.1; -; Genomic_RNA.
DR   SMR; P16900; -.
DR   PRIDE; P16900; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; 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; IPR045345; Gag_p24_C.
DR   InterPro; IPR000721; Gag_p24_N.
DR   InterPro; IPR012344; Matrix_HIV/RSV_N.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF19317; Gag_p24_C; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF47943; SSF47943; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   3: Inferred from homology;
KW   Capsid protein; Host-virus interaction; Metal-binding; Repeat;
KW   Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral release from host cell; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..143
FT                   /note="Matrix protein p16"
FT                   /id="PRO_0000038796"
FT   CHAIN           144..363
FT                   /note="Capsid protein p25"
FT                   /id="PRO_0000038797"
FT   CHAIN           364..446
FT                   /note="Nucleocapsid protein p14"
FT                   /id="PRO_0000038798"
FT   ZN_FING         384..401
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         403..420
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          415..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           440..443
FT                   /note="PTAP/PSAP motif"
FT   COMPBIAS        421..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  50550 MW;  3B7BFFA00FAC5C71 CRC64;
     MATQGSKEKK GYPELKEVIK TTCKIKVGPG KETLTEGNCL WALKTLDFIF EDIKTEPWTL
     TKMYTVWEKL KQVTPEETSK REFASLQATL ACIMCSQMGM RPETVQAARG IISMKEGLHE
     KQEDKEKKVE QLYPNLEKHR EVYPIVNLQA GGRSWKAVES VTFQQLQTVA MQHGLVSEDF
     ERQLAYYATT WTSKDILEVL AMMPGNRAQK ELIQGKLNEE AERWVRQNPP GPNVLTVDQI
     MGVGQTNQQA SQANMDQARQ LCLQWVITAL RSVRHMSHRP GNPMLIKQKN SESYEDFIAR
     LLEAIDTEPV TDPIKTYLKV TLSFTNASTD CQKQMDRVLG TRVQQASVEE KMQACRDVGS
     EGFKMQLLAQ ALRPPRKEGK QGVQKCYYCG KPGHLARQCR QGIICHHCGK RGHMQKDCRQ
     KKGNPTSQQG NSRRGPRVVP SAPPML