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Transcriptional activator protein (TrAP)

 G4XFU6_9GEMI            Unreviewed;       129 AA.
G4XFU6;
14-DEC-2011, integrated into UniProtKB/TrEMBL.
14-DEC-2011, sequence version 1.
08-JUN-2016, entry version 11.
RecName: Full=Transcriptional activator protein {ECO:0000256|RuleBase:RU363028};
Short=TrAP {ECO:0000256|RuleBase:RU363028};
Tomato golden vein virus.
Viruses; ssDNA viruses; Geminiviridae; Begomovirus;
unclassified Begomovirus.
NCBI_TaxID=296190 {ECO:0000313|EMBL:AEP82993.1};
[1] {ECO:0000313|EMBL:AEP82993.1}
NUCLEOTIDE SEQUENCE.
STRAIN=DF[BR:Pip1670:03] {ECO:0000313|EMBL:AEP82993.1},
DF[BR:Pip1719:03] {ECO:0000313|EMBL:AEP82998.1},
DF[BR:Pip1799:03] {ECO:0000313|EMBL:AEP83003.1}, and
DF[BR:Taq1613:03] {ECO:0000313|EMBL:AEP82988.1};
PubMed=22218964; DOI=10.1007/s00705-011-1213-7;
Albuquerque L.C., Varsani A., Fernandes F.R., Pinheiro B.,
Martin D.P., de Tarso Oliveira Ferreira P., Lemos T.O.,
Inoue-Nagata A.K.;
"Further characterization of tomato-infecting begomoviruses in
Brazil.";
Arch. Virol. 157:747-752(2012).
-!- FUNCTION: Strong activator of the late viral genes promoters. Acts
as a suppressor of RNA-mediated gene silencing, also known as
post-transcriptional gene silencing (PTGS), a mechanism of plant
viral defense that limits the accumulation of viral RNAs. Also
suppresses the host basal defense by interacting with and
inhibiting SNF1 kinase, a key regulator of cell metabolism
implicated in innate antiviral defense. Determines pathogenicity.
{ECO:0000256|RuleBase:RU363028}.
-!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction
correlates with nuclear localization and efficient activation of
transcription. {ECO:0000256|RuleBase:RU363028}.
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000256|RuleBase:RU363028}.
-!- SUBCELLULAR LOCATION: Host nucleus
{ECO:0000256|RuleBase:RU363028}.
-!- DOMAIN: The zinc finger and the transactivation region are
involved in PTGS suppression. {ECO:0000256|RuleBase:RU363028}.
-!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
protein family. {ECO:0000256|RuleBase:RU363028}.
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EMBL; JF803255; AEP82988.1; -; Genomic_DNA.
EMBL; JF803256; AEP82993.1; -; Genomic_DNA.
EMBL; JF803257; AEP82998.1; -; Genomic_DNA.
EMBL; JF803258; AEP83003.1; -; Genomic_DNA.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR000942; Gemini_AL2.
Pfam; PF01440; Gemini_AL2; 1.
PRINTS; PR00230; GEMCOATAL2.
ProDom; PD001117; Gemini_AL2; 1.
3: Inferred from homology;
Activator {ECO:0000256|RuleBase:RU363028};
DNA-binding {ECO:0000256|RuleBase:RU363028};
Host cytoplasm {ECO:0000256|RuleBase:RU363028};
Host nucleus {ECO:0000256|RuleBase:RU363028};
Host-virus interaction {ECO:0000256|RuleBase:RU363028};
Metal-binding {ECO:0000256|RuleBase:RU363028};
Suppressor of RNA silencing {ECO:0000256|RuleBase:RU363028};
Zinc {ECO:0000256|RuleBase:RU363028};
Zinc-finger {ECO:0000256|RuleBase:RU363028}.
SEQUENCE 129 AA; 14739 MW; C9DC709E11764560 CRC64;
MLNSSSSTPP SIKPRHRAAK QKTTRRKRID LNCGCSIYIH INCRNNGFTH RGTHHCASSR
EWRLYLGDYK SPLFQDNQRR GPLLHNDQDI PCADTFQPQP AESVGSPQGI SKFPSLDDIP
ESFWDDIFN


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