ID   CAPSD_SLCV              Reviewed;         251 AA.
AC   P27444;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
GN   ORFNames=AR1, AV1;
OS   Squash leaf curl virus (SLCV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=10829;
OH   NCBI_TaxID=3662; Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var. moschata).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1984668; DOI=10.1016/0042-6822(91)90009-z;
RA   Lazarowitz S.G., Lazdins I.B.;
RT   "Infectivity and complete nucleotide sequence of the cloned genomic
RT   components of a bipartite squash leaf curl geminivirus with a broad host
RT   range phenotype.";
RL   Virology 180:58-69(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; M38183; AAC32411.1; -; Genomic_DNA.
DR   PIR; D36785; QQCVS2.
DR   RefSeq; NP_047244.1; NC_001936.1.
DR   SMR; P27444; -.
DR   GeneID; 956395; -.
DR   KEGG; vg:956395; -.
DR   Proteomes; UP000009151; 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_0000222191"
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;  29229 MW;  C807EA0C6F3C6C43 CRC64;
     MVKRDAPWRL MAGTSKVSRS ANFSPREGMG PKFNKAAAWV NRPMYRKPRI YRTMRGPDIP
     KGCEGPCKVQ SYEQRHDISH LGKVMCISDV TRGNGITHRV GKRFCVKSVY ILGKIWMDEN
     IKLKNHTNSV MFWLVRDRRP YGTPMDFGQV FNMFDNEPST ATIKNDLRDR YQVMHRFYAK
     VTGGQYASNE QALVRRFWKV NNHVVYNHQE AGKYENHTEN ALLLYMACTH ASNPVYATLK
     IRIYFYDSIT N