ID   CAPSD_CALCV             Reviewed;         251 AA.
AC   Q96701;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
GN   ORFNames=AR1, AV1;
OS   Cabbage leaf curl virus (isolate Jamaica) (CaLCuV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=345184;
OH   NCBI_TaxID=3712; Brassica oleracea (Wild cabbage).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Abouzid A.M., Hiebert E., Strandberg J.O.;
RT   "Cloning, identification and partial sequencing of a new geminivirus
RT   infecting Brassicaceae.";
RL   Phytopathology 82:1070-1070(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; U65529; AAB17960.1; -; Genomic_DNA.
DR   SMR; Q96701; -.
DR   Proteomes; UP000007622; 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_0000320107"
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;  29313 MW;  F7DBFF48D64AB3ED CRC64;
     MPKRDAPWRS MAGTSKVSRN ANYSPRAGMI HKFDKAAAWV NRPMYRKPRI YRTFRSPDVP
     RGCEGPCKVQ SYEQRHDISH VGKVMCISDI TRGNGITHRV GKRFCVKSVY ILGKIWMDEN
     IKLKNHTNSV MFWLVRDRRP YGTPMEFGQV FNMFDNEPST ATVKNDLRDR YQVMHKFYAK
     VTGGQYASNE QALVKRFWKV NNYVVYNHQE AGKYENHTEN ALLLYMACTH ASNPVYATLK
     IRIYFYDSIT N