GAG_CAEVC
ID GAG_CAEVC Reviewed; 441 AA.
AC P33458;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Caprine arthritis encephalitis virus (strain Cork) (CAEV-Co).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11661;
OH NCBI_TaxID=9925; Capra hircus (Goat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2171210; DOI=10.1016/0042-6822(90)90303-9;
RA Saltarelli M., Querat G., Konings D.A.M., Vigne R., Clements J.E.;
RT "Nucleotide sequence and transcriptional analysis of molecular clones of
RT CAEV which generate infectious virus.";
RL Virology 179:347-364(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 -!- SEQUENCE CAUTION:
CC Sequence=AAA91825.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M33677; AAA91825.1; ALT_INIT; Genomic_RNA.
DR PIR; A45345; A45345.
DR RefSeq; NP_040938.1; NC_001463.1.
DR SMR; P33458; -.
DR GeneID; 1489975; -.
DR KEGG; vg:1489975; -.
DR Proteomes; UP000203242; Genome.
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; 1.10.375.10; -; 1.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_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; Reference proteome;
KW Repeat; Viral budding; Viral budding via the host ESCRT complexes;
KW Viral release from host cell; Virion; Zinc; Zinc-finger.
FT CHAIN 1..146
FT /note="Matrix protein p16"
FT /id="PRO_0000038769"
FT CHAIN 147..358
FT /note="Capsid protein p25"
FT /id="PRO_0000038770"
FT CHAIN 359..441
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000038771"
FT ZN_FING 379..396
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 398..415
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 419..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 435..438
FT /note="PTAP/PSAP motif"
SQ SEQUENCE 441 AA; 49909 MW; 3DBD26CFA214D8A9 CRC64;
MARQVSGGKR DYPELEKCIK HACKIKVRLR GEHLTEGNCL WCLKTLDYMF EDHKEEPWTK
VKFRTIWQKV KNLTPEESNK KDFMSLQATL AGLMCCQMGM RPETLQDAMA TVIMKDGLLE
QEEKKEDKRE KEESVFPIVV QAAGGRSWKA VDSVMFQQLQ TVAMQHGLVS EDFERQLAYY
ATTWTSKDIL EVLAMMPGNR AQKELIQGKL NEEAERWRRN NPPPPAGGGL TVDQIMGVGQ
TNQAAAQANM DQARQICLQW VINALRAVRH MAHRPGNPML VKQKTNEPYE DFAARLLEAI
DAEPVTQPIK DYLKLTLSYT NASADCQKQM DRTLGQRVQQ ASVEEKMQAC RDVGSEGFKM
QLLAQALRPG KGKGNGQPQR CYNCGKPGHQ ARQCRQGIIC HNCGKRGHMQ KECRGKRDIR
GKQQGNGRRG IRVVPSAPPM E