ID   A0A0K0P9K1_9GEMI        Unreviewed;       135 AA.
AC   A0A0K0P9K1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-JUN-2016, entry version 7.
DE   RecName: Full=Transcriptional activator protein {ECO:0000256|RuleBase:RU363028};
DE            Short=TrAP {ECO:0000256|RuleBase:RU363028};
GN   Name=AC2 {ECO:0000313|EMBL:AKQ21214.1};
OS   Clerodendron yellow mosaic virus.
OC   Viruses; ssDNA viruses; Geminiviridae; Begomovirus;
OC   unclassified Begomovirus.
OX   NCBI_TaxID=326811 {ECO:0000313|EMBL:AKQ21214.1};
RN   [1] {ECO:0000313|EMBL:AKQ21214.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MJGD1 {ECO:0000313|EMBL:AKQ21214.1};
RA   Jaidi M., Srivastava A., Kumar S., Raj S.K.;
RT   "Molecular characterization of Clerodendron yellow mosaic virus
RT   causing yellow mosaic disease in Duranta erecta in India.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Strong activator of the late viral genes promoters. Acts
CC       as a suppressor of RNA-mediated gene silencing, also known as
CC       post-transcriptional gene silencing (PTGS), a mechanism of plant
CC       viral defense that limits the accumulation of viral RNAs. Also
CC       suppresses the host basal defense by interacting with and
CC       inhibiting SNF1 kinase, a key regulator of cell metabolism
CC       implicated in innate antiviral defense. Determines pathogenicity.
CC       {ECO:0000256|RuleBase:RU363028}.
CC   -!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction
CC       correlates with nuclear localization and efficient activation of
CC       transcription. {ECO:0000256|RuleBase:RU363028}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm
CC       {ECO:0000256|RuleBase:RU363028}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus
CC       {ECO:0000256|RuleBase:RU363028}.
CC   -!- DOMAIN: The zinc finger and the transactivation region are
CC       involved in PTGS suppression. {ECO:0000256|RuleBase:RU363028}.
CC   -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
CC       protein family. {ECO:0000256|RuleBase:RU363028}.
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DR   EMBL; KR869857; AKQ21214.1; -; Genomic_DNA.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
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:0016032; P:viral process; IEA:UniProtKB-KW.
DR   InterPro; IPR000942; Gemini_AL2.
DR   Pfam; PF01440; Gemini_AL2; 1.
DR   PRINTS; PR00230; GEMCOATAL2.
DR   ProDom; PD001117; Gemini_AL2; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|RuleBase:RU363028};
KW   DNA-binding {ECO:0000256|RuleBase:RU363028};
KW   Host cytoplasm {ECO:0000256|RuleBase:RU363028};
KW   Host nucleus {ECO:0000256|RuleBase:RU363028};
KW   Host-virus interaction {ECO:0000256|RuleBase:RU363028};
KW   Metal-binding {ECO:0000256|RuleBase:RU363028};
KW   Suppressor of RNA silencing {ECO:0000256|RuleBase:RU363028};
KW   Zinc {ECO:0000256|RuleBase:RU363028};
KW   Zinc-finger {ECO:0000256|RuleBase:RU363028}.
SQ   SEQUENCE   135 AA;  15435 MW;  5B9FD4E5331B95C7 CRC64;
     MRPSSPSTSR STQVPIKVQH RIAKRRAIRR KRIDLKCGCS YYLHINCHNH GFTHRGTHHC
     SSSDEWRVYL GGSKSPLFQD PKPPGQTILP EPRHNNNPDP VQPQPEESTG TTQMLHRLPD
     LDEFTSSDWS FLNGL
//