CAPSD_TYCS2
ID CAPSD_TYCS2 Reviewed; 257 AA.
AC Q67617;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=V1;
OS Tomato yellow leaf curl Sardinia virus (isolate Spain-2) (TYLCSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=221538;
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Reina J., Cuadrado-Gomez I.M., Jimenez J., Bejarano E.R.;
RT "Characterization of a tomato yellow leaf curl virus isolated from
RT southeast Spain (almeria).";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
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; L27708; AAA47952.1; -; Genomic_DNA.
DR SMR; Q67617; -.
DR Proteomes; UP000008266; 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..257
FT /note="Capsid protein"
FT /id="PRO_0000320109"
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 201..248
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 30056 MW; 209E9B421883A4FE CRC64;
MPKRTGDILM SSPLSKFRRK LNFDSPYTSR AAAPTVQGIK RRSWTYRPMY RKPRMYRMYR
SPDVPFGCEG PCKVQSYEQR DDVKHTGVVR CVSDVTRGSG ITHRVGKRFC IKSIYILGKI
WMDENIKKQN HTNQVMFFLV RDRRPYGTSP MDFGQVFNMF DNEPSTATVK NDLRDRYQVM
RKFHATVVGG PSGMKEQCLL KRFFKVNTHV VYNHQEQAKY ENHTENALLL YMACTHASNP
VYATLKIRIY FYDAVTN