ID   CAPSD_ABMVW             Reviewed;         251 AA.
AC   P21942;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   29-SEP-2021, entry version 102.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
GN   ORFNames=AR1, AV1;
OS   Abutilon mosaic virus (isolate West India) (AbMV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=10816;
OH   NCBI_TaxID=3630; Abutilon.
OH   NCBI_TaxID=3635; Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OH   NCBI_TaxID=47605; Hibiscus.
OH   NCBI_TaxID=96479; Malva.
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH   NCBI_TaxID=108335; Sida.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-251.
RX   PubMed=2219703; DOI=10.1016/0042-6822(90)90343-p;
RA   Frischmuth T., Zimmat G., Jeske H.;
RT   "The nucleotide sequence of abutilon mosaic virus reveals prokaryotic as
RT   well as eukaryotic features.";
RL   Virology 178:461-468(1990).
RN   [2]
RP   SEQUENCE REVISION.
RA   Jeske H.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   DNA-BINDING.
RX   PubMed=15220444; DOI=10.1128/jvi.78.14.7698-7706.2004;
RA   Hehnle S., Wege C., Jeske H.;
RT   "Interaction of DNA with the movement proteins of geminiviruses
RT   revisited.";
RL   J. Virol. 78:7698-7706(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X15983; CAA34110.2; -; Genomic_DNA.
DR   PIR; B36214; QQCVW2.
DR   RefSeq; NP_047215.2; NC_001928.2.
DR   SMR; P21942; -.
DR   GeneID; 956370; -.
DR   KEGG; vg:956370; -.
DR   Proteomes; UP000006885; 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   1: Evidence at protein level;
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_0000222177"
FT   ZN_FING         63..80
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
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"
SQ   SEQUENCE   251 AA;  29352 MW;  0EAC8A52E53854A3 CRC64;
     MPKRDLPWRS MPGTSKTSRN ANYSPRARIG PRVDKASEWV HRPMYRKPRI YRTLRTADVP
     RGCEGPCKVQ SYEQRHDISH VGKVMCISDV TRGNGITHRV GKRFCVKSVY ILGKIWMDEN
     IKLQNHTNSV MFWLVRDRRP YGTPMDFGHV FNMFDNEPST ATVKNDLRDR YQVLHKFYGK
     VTGGQYASNE QAIVKRFWKV NNHVVYNHQE AGKYENHTEN ALLLYMACTH ASNPVYATLK
     IRIYFYDSLM N