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Transcriptional activator protein (TrAP) (Protein AC2) (Protein AL2)

 TRAP_TGMVY              Reviewed;         129 AA.
P03562;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 61.
RecName: Full=Transcriptional activator protein;
Short=TrAP;
AltName: Full=Protein AC2;
AltName: Full=Protein AL2;
ORFNames=AC2, AL2;
Tomato golden mosaic virus (strain Yellow vein) (TGMV).
Viruses; ssDNA viruses; Geminiviridae; Begomovirus.
NCBI_TaxID=223341;
NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16453557;
Hamilton W.D.O., Stein V.E., Coutts R.H.A., Buck K.W.;
"Complete nucleotide sequence of the infectious cloned DNA components
of tomato golden mosaic virus: potential coding regions and regulatory
sequences.";
EMBO J. 3:2197-2205(1984).
[2]
FUNCTION.
PubMed=9191840; DOI=10.1006/viro.1997.8549;
Sunter G., Bisaro D.M.;
"Regulation of a geminivirus coat protein promoter by AL2 protein
(TrAP): evidence for activation and derepression mechanisms.";
Virology 232:269-280(1997).
[3]
DNA-BINDING, TRANSACTIVATION REGION, AND PHOSPHORYLATION.
PubMed=10544077; DOI=10.1006/viro.1999.9925;
Hartitz M.D., Sunter G., Bisaro D.M.;
"The tomato golden mosaic virus transactivator (TrAP) is a single-
stranded DNA and zinc-binding phosphoprotein with an acidic activation
domain.";
Virology 263:1-14(1999).
[4]
FUNCTION, AND INTERACTION WITH ARABIDOPSIS THALIANA SNF1.
PubMed=12671096; DOI=10.1105/tpc.009530;
Hao L., Wang H., Sunter G., Bisaro D.M.;
"Geminivirus AL2 and L2 proteins interact with and inactivate SNF1
kinase.";
Plant Cell 15:1034-1048(2003).
[5]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
ARABIDOPSIS THALIANA ADK1 AND ADK2.
PubMed=14615595; DOI=10.1105/tpc.015180;
Wang H., Hao L., Shung C.-Y., Sunter G., Bisaro D.M.;
"Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins.";
Plant Cell 15:3020-3032(2003).
[6]
FUNCTION.
PubMed=15919897; DOI=10.1128/JVI.79.12.7410-7418.2005;
Wang H., Buckley K.J., Yang X., Buchmann R.C., Bisaro D.M.;
"Adenosine kinase inhibition and suppression of RNA silencing by
geminivirus AL2 and L2 proteins.";
J. Virol. 79:7410-7418(2005).
[7]
SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH ARABIDOPSIS THALIANA
ADK2, AND MUTAGENESIS OF CYS-33; CYS-35; HIS-40 AND CYS-43.
PubMed=17715241; DOI=10.1128/JVI.00617-07;
Yang X., Baliji S., Buchmann R.C., Wang H., Lindbo J.A., Sunter G.,
Bisaro D.M.;
"Functional modulation of the geminivirus AL2 transcription factor and
silencing suppressor by self-interaction.";
J. Virol. 81:11972-11981(2007).
-!- FUNCTION: Strong activator of the late viral genes promoters.
Enhances the expression of the capsid protein and nuclear shuttle
protein. 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.
Suppresses the host RNA silencing by inhibiting adenosine kinase
(ADK), a kinase involved in a general methylation pathway. 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:0000269|PubMed:12671096, ECO:0000269|PubMed:14615595,
ECO:0000269|PubMed:15919897, ECO:0000269|PubMed:9191840}.
-!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction
correlates with nuclear localization and efficient activation of
transcription. Monomers suppress local silencing by interacting
with and inactivating host adenosine kinase (ADK) in the
cytoplasm. Interacts with and inhibits host SNF1 kinase. Binds to
ssDNA. {ECO:0000269|PubMed:12671096, ECO:0000269|PubMed:14615595,
ECO:0000269|PubMed:17715241}.
-!- INTERACTION:
Q96703:AL2 (xeno); NbExp=2; IntAct=EBI-16175508, EBI-16175606;
Q8GZB6:SUVH4 (xeno); NbExp=4; IntAct=EBI-16175508, EBI-16175525;
-!- SUBCELLULAR LOCATION: Host nucleus. Host cytoplasm. Note=The
phosphorylated form appears to accumulate almost exclusively in
the nucleus, whereas the non-phosphorylated form is found in both
nucleus and cytoplasm.
-!- DOMAIN: The zinc finger and the transactivation region are
involved in PTGS suppression. {ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000305|PubMed:10544077,
ECO:0000305|PubMed:14615595}.
-!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
protein family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; K02029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A04165; QQCVL2.
ProteinModelPortal; P03562; -.
DIP; DIP-62056N; -.
IntAct; P03562; 6.
OrthoDB; VOG0900018A; -.
Proteomes; UP000007405; Genome.
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.
1: Evidence at protein level;
Activator; Complete proteome; DNA-binding; Host cytoplasm;
Host nucleus; Host-virus interaction; Metal-binding; Phosphoprotein;
Suppressor of RNA silencing; Zinc; Zinc-finger.
CHAIN 1 129 Transcriptional activator protein.
/FTId=PRO_0000222230.
ZN_FING 33 50 {ECO:0000250}.
REGION 115 129 Transactivation.
MOTIF 13 28 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 4 7 Poly-Ser.
COMPBIAS 25 28 Poly-Arg.
MUTAGEN 33 33 C->A: 66% loss of transactivation.
{ECO:0000269|PubMed:17715241}.
MUTAGEN 35 35 C->A: 95% loss of transactivation.
{ECO:0000269|PubMed:17715241}.
MUTAGEN 40 40 H->A: Enhances transactivation.
{ECO:0000269|PubMed:17715241}.
MUTAGEN 43 43 C->A: 72% loss of transactivation.
{ECO:0000269|PubMed:17715241}.
SEQUENCE 129 AA; 14888 MW; 001759FB17963B9E CRC64;
MRNSSSSTPP SIKAQHRAAK RRAIRRRRID LNCGCSIYIH IDCRNNGFTH RGTYHCASSR
EWRLYLGDNK SPLFQDNQRR GSPLHQHQDI PLTNQVQPQP EESIGSPQGI SQLPSMDDID
DSFWENLFK


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