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CAPSD_TYLCC
ID   CAPSD_TYLCC             Reviewed;         256 AA.
AC   Q9DXE8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   12-AUG-2020, entry version 63.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
GN   ORFNames=V1;
OS   Tomato yellow leaf curl China virus (TYLCCNV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=185793;
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH   NCBI_TaxID=185191; Sigesbeckia orientalis.
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate CHI;
RX   PubMed=11682126; DOI=10.1016/s0168-1702(01)00363-x;
RA   Yin Q., Yang H., Gong Q., Wang H., Liu Y., Hong Y., Tien P.;
RT   "Tomato yellow leaf curl China virus: monopartite genome organization and
RT   agroinfection of plants.";
RL   Virus Res. 81:69-76(2001).
CC   -!- FUNCTION: Encapsidates the viral genome into characteristic twinned
CC       ('geminate') particles. Binds the genomic viral ssDNA and shuttles it
CC       into and out of the cell nucleus. Plays a role in protection of the
CC       genome from degradation, virus acquisition and transmission by insect
CC       vectors, infectivity, and systemic movement. The CP of monopartite
CC       geminiviruses is absolutely essential for virus movement (By
CC       similarity). {ECO:0000250}.
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; AF311734; AAG27472.1; -; Genomic_DNA.
DR   RefSeq; NP_660165.1; NC_004044.1.
DR   SMR; Q9DXE8; -.
DR   GeneID; 949226; -.
DR   KEGG; vg:949226; -.
DR   Proteomes; UP000008267; 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; Metal-binding;
KW   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_0000312151"
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;  29886 MW;  7C1AFC11EF50F13A CRC64;
     MAKRPADIVI STPASKVRRR LNFDSPYTGR VAAPTVRVTR RQMWSNRPMY RKPMMYRMYR
     SPDVPRGCEG PCKVQSCEAR HDVSHTGKVI CVSDVTRGNG ITHRVGKRFC VKSIYVIGKI
     WMDENIKFKN HTNTVMFFLV RDRRPSGTPM DFQQVFNCYD NEPSTATVKN DLRDRFQVRR
     KFYSTVTGGQ YACKEQALVK RFIRLNTHVV YNHQEQAKYE NHTENALLLY MACTHASNPV
     YATLKVRIYF YDSQMN
 
 
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