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CAPSD_MYMVV
ID   CAPSD_MYMVV             Reviewed;         257 AA.
AC   Q9YPS5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   29-SEP-2021, entry version 64.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
GN   ORFNames=AR1, AV1;
OS   Mungbean yellow mosaic virus (strain Vigna) (MYMV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=223295;
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3915; Vigna mungo (Black gram) (Phaseolus mungo).
OH   NCBI_TaxID=157791; Vigna radiata (Mung bean).
OH   NCBI_TaxID=3916; Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OH   NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15290387; DOI=10.1007/s00705-004-0313-z;
RA   Karthikeyan A.S., Vanitharani R., Balaji V., Anuradha S.,
RA   Thillaichidambaram P., Shivaprasad P.V., Parameswari C., Balamani V.,
RA   Saminathan M., Veluthambi K.;
RT   "Analysis of an isolate of Mungbean yellow mosaic virus (MYMV) with a
RT   highly variable DNA B component.";
RL   Arch. Virol. 149:1643-1652(2004).
RN   [2]
RP   SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION WITH
RP   ORYZA SATIVA IMPORTIN ALPHA-1A.
RX   PubMed=15914861; DOI=10.1099/vir.0.80920-0;
RA   Guerra-Peraza O., Kirk D., Seltzer V., Veluthambi K., Schmit A.C., Hohn T.,
RA   Herzog E.;
RT   "Coat proteins of Rice tungro bacilliform virus and Mungbean yellow mosaic
RT   virus contain multiple nuclear-localization signals and interact with
RT   importin alpha.";
RL   J. Gen. Virol. 86:1815-1826(2005).
CC   -!- FUNCTION: Encapsidates the viral DNA into characteristic twinned
CC       ('geminate') particles. Binds the genomic viral ssDNA and shuttles it
CC       into and out of the cell nucleus. The CP of bipartite geminiviruses is
CC       not required for cell-to-cell or systemic movement.
CC   -!- SUBUNIT: Homomultimer. Binds to single-stranded and double-stranded
CC       viral DNA. Interacts (via nuclear localization signals) with host
CC       importin alpha-1a (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus
CC       {ECO:0000269|PubMed:15914861}. Note=It is actively transported into the
CC       host cell nucleus. It may be exported out of the nucleus through a
CC       nuclear export signal for cell-to-cell movement and spread (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the geminiviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ132575; CAA10704.1; -; Genomic_DNA.
DR   SMR; Q9YPS5; -.
DR   PRIDE; Q9YPS5; -.
DR   Proteomes; UP000007784; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR000650; Gem_coat_AR1.
DR   InterPro; IPR000263; GV_A/BR1_coat.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00844; Gemini_coat; 1.
DR   PRINTS; PR00224; GEMCOATAR1.
DR   PRINTS; PR00223; GEMCOATARBR1.
PE   1: Evidence at protein level;
KW   Capsid protein; DNA-binding; Host nucleus; Host-virus interaction;
KW   Metal-binding; Reference proteome; T=1 icosahedral capsid protein;
KW   Viral penetration into host nucleus; Virion; Virus entry into host cell;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..257
FT                   /note="Capsid protein"
FT                   /id="PRO_0000320108"
FT   ZN_FING         69..86
FT                   /evidence="ECO:0000255"
FT   MOTIF           3..20
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           41..55
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           102..123
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           201..248
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   257 AA;  29829 MW;  F8ABA0B0C5F1C723 CRC64;
     MPKRNYDTAF STPMSNVRRR LTFDTPLSLP ATAGSVPASA KRRRWTNRPM WRKPRYYRLY
     RSPDVPRGCE GPCKVQSFEA KHDISHVGKV ICVTDVTRGM GITHRVGKRF CVKSIWVTGK
     IWMDENIKTK NHTNTVMFKL VRDRRPFGTP QDFGQVFNMY DNEPSTATVK NDLRDRYQVV
     RKFQATVTGG QYASKEQAIV SKFYRVNNYV VYNHQEAAKY ENHTENALLL YMACTHASNP
     VYATLKIRIY FYDSISN
 
 
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