CAPSD_PYMVV
ID CAPSD_PYMVV Reviewed; 251 AA.
AC P27255;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=AR1, AV1;
OS Potato yellow mosaic virus (isolate Venezuela) (PYMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=223310;
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1856690; DOI=10.1099/0022-1317-72-7-1515;
RA Coutts R.H.A., Coffin R.S., Roberts E.J.F., Hamilton W.D.O.;
RT "The nucleotide sequence of the infectious cloned DNA components of potato
RT yellow mosaic virus.";
RL J. Gen. Virol. 72:1515-1520(1991).
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; D00940; BAA00779.1; -; Genomic_DNA.
DR PIR; JU0367; QQCVP2.
DR RefSeq; NP_047238.1; NC_001934.1.
DR SMR; P27255; -.
DR GeneID; 956388; -.
DR KEGG; vg:956388; -.
DR Proteomes; UP000006828; 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; 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_0000222190"
FT ZN_FING 63..80
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..20
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
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 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 29267 MW; 98939DD842AE3A55 CRC64;
MPKRDAPWRS MAGTSKVSRN ANYSPRSGIG PRINKAAEWV NRPMYRKPRI YRTLRTPDVP
RGCEGPCKVQ SFEQRHDILH TGKVMCISDV TRGNGITHRV GKRFCVKSVY ILGKIWMDEN
IKLKNHTNSV MFWLVRDRRP YGTPMDFGQV FNMFDNEPST ATVKNDLRDR YQVMHRFYGK
VTGGQYASNE HAIVRRFWKV NNHVVYNHQE AGKYENHTEN ALLLYMACTH ASNPVYATLK
IRIYFYDSIL N