CAPSD_TMOV
ID CAPSD_TMOV Reviewed; 251 AA.
AC P36277;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 29-SEP-2021, entry version 86.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=AR1, AV1;
OS Tomato mottle virus (isolate Florida) (ToMoV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=223359;
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1469361; DOI=10.1099/0022-1317-73-12-3225;
RA Abouzid A.M., Polston J.E., Hiebert E.;
RT "The nucleotide sequence of tomato mottle virus, a new geminivirus isolated
RT from tomatoes in Florida.";
RL J. Gen. Virol. 73:3225-3229(1992).
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; L14460; AAC32415.1; -; Genomic_DNA.
DR PIR; JQ1869; JQ1869.
DR RefSeq; NP_047250.1; NC_001938.1.
DR SMR; P36277; -.
DR PRIDE; P36277; -.
DR GeneID; 956410; -.
DR KEGG; vg:956410; -.
DR Proteomes; UP000008249; 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_0000222193"
FT ZN_FING 63..80
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 251 AA; 29266 MW; E15BB954E28826BA CRC64;
MPKRDLPWRS MAGTSKVSRN ANYSPRAGIG PRINKAAEWV NRPMYRKPRM YRTLRTTDVA
RGCEGPCKVQ SFEQRHDISH IGKVMCISDV TRGNGITHRV GKRFCVKSVY ILGKIWMDEN
IKLKNHTNSV MFWLVRDRRP YGTPMDIWTV FNMFDNEPST ATVKNDLRDR YQVMHKFYGK
VTGGQYASNE QAIVKRFWKV NNHVVYNHQE AGKYENHTEN ALLLYMACTH ASNPVYATLK
IRIYFYDSIT N