CAPSD_TLCVA
ID CAPSD_TLCVA Reviewed; 256 AA.
AC P36278;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 88.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=V1;
OS Tomato leaf curl virus (strain Australia) (ToLCV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=223353;
OH NCBI_TaxID=185024; Cynanchum acutum.
OH NCBI_TaxID=145753; Malva parviflora (Little mallow) (Cheeseweed mallow).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8423446; DOI=10.1099/0022-1317-74-1-147;
RA Dry I.B., Rigden J.E., Krake L.R., Mullineaux P.M., Rezaian M.A.;
RT "Nucleotide sequence and genome organization of tomato leaf curl
RT geminivirus.";
RL J. Gen. Virol. 74:147-151(1993).
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; S53251; AAM33778.1; -; Genomic_DNA.
DR PIR; JQ1886; JQ1886.
DR RefSeq; NP_632003.1; NC_003896.1.
DR SMR; P36278; -.
DR GeneID; 944501; -.
DR KEGG; vg:944501; -.
DR Proteomes; UP000008246; 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 T=1 icosahedral capsid protein; Viral penetration into host nucleus;
KW Virion; Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..256
FT /note="Capsid protein"
FT /id="PRO_0000222196"
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; 29713 MW; 3F4AAA7230F4DE66 CRC64;
MSKRPADIVI STPASKVRRK LNFNSPFKSA AAVPTVRVTR RRTWVNRPMY RKPMMYRLFR
SPDVPRGCEG PCKVQSYEQR HDVAHVGKVL CVSDVTRGTG ITHRTGKRFC IKSIYVLGKI
WMDDNIKTRN HTNTVMFFLV RDRRPYGTPK DFGQVFNMYD NEPSTATVKN DMRDGFQVIK
KWSATVTGGQ YASKEQAIIN RFYKIYNHCT YNHQEAAKYE NHTENALLLY MACTHASNPV
YATLKIRIYF YDSIQN