CAPSD_BGYMJ
ID CAPSD_BGYMJ Reviewed; 251 AA.
AC P0CK34; P05152; Q67579;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 02-JUN-2021, entry version 32.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=AR1, AV1;
OS Bean golden yellow mosaic virus (isolate Puerto Rico-Japan) (BGYMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=222449;
OH NCBI_TaxID=260885; Macroptilium lathyroides.
OH NCBI_TaxID=108453; Malvastrum coromandelianum.
OH NCBI_TaxID=3884; Phaseolus lunatus (Lima bean) (Phaseolus limensis).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3037283; DOI=10.1111/j.1348-0421.1987.tb03078.x;
RA Morinaga T., Ikegami M., Shimotohno K., Miura K.;
RT "Total nucleotide sequences of the infectious cloned DNAs of bean golden
RT mosaic virus.";
RL Microbiol. Immunol. 31:147-154(1987).
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 {ECO:0000250}.
CC Note=It is actively transported into the host cell nucleus. It may be
CC exported out of the nucleus through a nuclear export signal for cell-
CC to-cell movement and spread (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geminiviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; D00201; BAA00136.1; -; Genomic_DNA.
DR RefSeq; NP_040772.1; NC_001439.1.
DR SMR; P0CK34; -.
DR GeneID; 988088; -.
DR KEGG; vg:988088; -.
DR Proteomes; UP000008769; 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 3: Inferred from homology;
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..251
FT /note="Capsid protein"
FT /id="PRO_0000415529"
FT ZN_FING 54..71
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..20
FT /note="Bipartite nuclear localization signal"
FT MOTIF 35..49
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 96..117
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 195..242
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 29042 MW; DF36B014E5E2B4BE CRC64;
MPKRDAPWRH MAGTSKVSRS GNYSPSGGMG SKSNKANAWV NRPMYRKPRI YRMYKSPDVP
KGCEGPCKVQ SYEQRHDISH VGKVMCISDI TRGNGITHRV GKRFCVKSVY ILGKIWMDEN
IMLKNHTNSV IFWLVRDRRP YGTPMDFGQV FNMFDNEPST ATVKNDLRDR YQVMHRFNAK
VSGGQYASNE QALVRRFWKV NNHVVYNHQE AGKYENHTEN ALLLYMACTH ASNPVYATLK
IRIYFYDSIT N