CAPSD_BGYMV
ID CAPSD_BGYMV Reviewed; 250 AA.
AC P0CK33; P05152; Q67579;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 02-JUN-2021, entry version 31.
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) (BGYMV) (Bean golden
OS mosaic virus (isolate Puerto Rico)).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=222448;
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=16593562; DOI=10.1073/pnas.82.11.3572;
RA Howarth A.J., Caton J., Bossert M., Goodman R.M.;
RT "Nucleotide sequence of bean golden mosaic virus and a model for gene
RT regulation in geminiviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3572-3576(1985).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46319.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M10070; AAA46319.1; ALT_FRAME; Genomic_DNA.
DR SMR; P0CK33; -.
DR Proteomes; UP000006572; 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..250
FT /note="Capsid protein"
FT /id="PRO_0000222179"
FT ZN_FING 53..70
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..19
FT /note="Bipartite nuclear localization signal"
FT MOTIF 34..48
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 95..116
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 194..241
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 28834 MW; A48E34583F24EE33 CRC64;
MPKRDAPWLM AGTSKVSRSG NYSPSGGMGS KSNKANAWVN RPMYRKPRIY RMYKSPDVPK
GCEGPCKVQS YEQRHDISHV GKVMCISDIT RGNGITHRVG KRFCVKSVYI LGKIWMDENI
MLKNHTNSVI FWLVRDRRPY GTPMDFGQVF NMFDNEPSTA TVKNDFRDRY QVMHRFNAKV
SGGQYASNDQ ALVRRFWKVN NHVVYNHQEA GKYENHTENA LLLYMACTHA SNPVYATLKI
RIYVYDSITN