CAPSD_ICMV
ID CAPSD_ICMV Reviewed; 256 AA.
AC Q08583;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=AR1, AV1;
OS Indian cassava mosaic virus (ICMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=31600;
OH NCBI_TaxID=3983; Manihot esculenta (Cassava) (Jatropha manihot).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8245859; DOI=10.1099/0022-1317-74-11-2437;
RA Hong Y.G., Robinson D.J., Harrison B.D.;
RT "Nucleotide sequence evidence for the occurrence of three distinct
RT whitefly-transmitted geminiviruses in cassava.";
RL J. Gen. Virol. 74:2437-2443(1993).
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; Z24758; CAA80885.1; -; Genomic_DNA.
DR PIR; JQ2326; JQ2326.
DR RefSeq; NP_047230.1; NC_001932.1.
DR SMR; Q08583; -.
DR PRIDE; Q08583; -.
DR GeneID; 991056; -.
DR KEGG; vg:991056; -.
DR Proteomes; UP000007210; 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..256
FT /note="Capsid protein"
FT /id="PRO_0000222183"
FT ZN_FING 68..85
FT /evidence="ECO:0000255"
FT MOTIF 3..20
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 40..54
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 101..122
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 200..247
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 256 AA; 29910 MW; 0FA4FD4AE48A702A CRC64;
MSKRPADIII STPGSKVRRR LNFDSPYSSR AAVPTVRVTK RQSWTNRPIN RKPRWYRMYR
SPDVPKGCEG PCKVQSFESR HDVVHIGKVM CISDVTRGIG LTHRVGKRFC VKSIYILGKI
WMDENIKTKN HTNSVMFFLV RDRRPVDKPQ DFGEVFNMFD NEPSTATVKN MHRDRYQVLR
KWHATVTGGQ YASKEQALVR RFFRVNNYVV YNQQEAGKYE NHTENALMLY MACTHASNPV
YATLKIRIYF YDSVSN
