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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
 
 
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