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CAPSD_TYLCI
ID   CAPSD_TYLCI             Reviewed;         260 AA.
AC   P27256;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   29-SEP-2021, entry version 78.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
GN   ORFNames=V1;
OS   Tomato yellow leaf curl virus (strain Israel) (TYLCV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=66366;
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=1926771; DOI=10.1016/0042-6822(91)90763-2;
RA   Navot N., Pichersky E., Zeidan M., Zamir D., Czosnek H.;
RT   "Tomato yellow leaf curl virus: a whitefly-transmitted geminivirus with a
RT   single genomic component.";
RL   Virology 185:151-161(1991).
RN   [2]
RP   SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNALS.
RX   PubMed=9680988; DOI=10.1046/j.1365-313x.1998.00037.x;
RA   Kunik T., Palanichelvam K., Czosnek H., Citovsky V., Gafni Y.;
RT   "Nuclear import of the capsid protein of tomato yellow leaf curl virus
RT   (TYLCV) in plant and insect cells.";
RL   Plant J. 13:393-399(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=9820160; DOI=10.1099/0022-1317-79-11-2829;
RA   Palanichelvam K., Kunik T., Citovsky V., Gafni Y.;
RT   "The capsid protein of tomato yellow leaf curl virus binds cooperatively to
RT   single-stranded DNA.";
RL   J. Gen. Virol. 79:2829-2833(1998).
RN   [4]
RP   NUCLEAR EXPORT SIGNAL.
RX   PubMed=10748526; DOI=10.1038/74500;
RA   Rhee Y., Gurel F., Gafni Y., Dingwall C., Citovsky V.;
RT   "A genetic system for detection of protein nuclear import and export.";
RL   Nat. Biotechnol. 18:433-437(2000).
RN   [5]
RP   SUBUNIT, AND MUTAGENESIS OF GLN-135 AND ASP-153.
RX   PubMed=11699961; DOI=10.1007/s007050170062;
RA   Hallan V., Gafni Y.;
RT   "Tomato yellow leaf curl virus (TYLCV) capsid protein (CP) subunit
RT   interactions: implications for viral assembly.";
RL   Arch. Virol. 146:1765-1773(2001).
RN   [6]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=Isolate Dominican Republic;
RX   PubMed=11878881; DOI=10.1006/viro.2001.1194;
RA   Rojas M.R., Jiang H., Salati R., Xoconostle-Cazares B., Sudarshana M.R.,
RA   Lucas W.J., Gilbertson R.L.;
RT   "Functional analysis of proteins involved in movement of the monopartite
RT   begomovirus, Tomato yellow leaf curl virus.";
RL   Virology 291:110-125(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.
CC       {ECO:0000269|PubMed:11878881, ECO:0000269|PubMed:9820160}.
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
CC       {ECO:0000269|PubMed:11878881, ECO:0000269|PubMed:9680988}. Note=It is
CC       actively transported into the host cell nucleus. It may be exported out
CC       of the nucleus through a nuclear export signal for cell-to-cell
CC       movement and spread.
CC   -!- SIMILARITY: Belongs to the geminiviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; X15656; CAA33686.1; -; Genomic_DNA.
DR   PIR; A40779; QQCVCL.
DR   SMR; P27256; -.
DR   PRIDE; P27256; -.
DR   Proteomes; UP000007547; 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   1: Evidence at protein level;
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..260
FT                   /note="Capsid protein"
FT                   /id="PRO_0000222195"
FT   ZN_FING         69..86
FT                   /evidence="ECO:0000255"
FT   MOTIF           3..20
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           41..55
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           102..123
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           202..251
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         135
FT                   /note="Q->H: 90% loss of homomultimerization."
FT                   /evidence="ECO:0000269|PubMed:11699961"
FT   MUTAGEN         153
FT                   /note="D->E: 90% loss of homomultimerization."
FT                   /evidence="ECO:0000269|PubMed:11699961"
SQ   SEQUENCE   260 AA;  30320 MW;  95DE37CC1DAED73D CRC64;
     MSKRPGDIII STPVSKVRRR LNFDSPYSSR AAVPIVQGTN KRRSWTYRPM YRKPRIYRMY
     RSPDVPRGCE GPCKVQSYEQ RDDIKHTGIV RCVSDVTRGS GITHRVGKRF CVKSIYFLGK
     VWMDENIKKQ NHTNQVMFFL VRDRRPYGNS PMDFGQVFNM FDNEPSTATV KNDLRDRFQV
     MRKFHATVIG GPSGMKEQAL VKRFFKINSH VTLFIFIQEA AKYENHTENA LLLYMACTHA
     SNPVYATMKI RIYFYDSISN
 
 
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