ID   TRAP_TLCVA              Reviewed;         135 AA.
AC   P36280;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-FEB-2022, entry version 75.
DE   RecName: Full=Transcriptional activator protein;
DE            Short=TrAP;
DE   AltName: Full=Protein C2;
DE   AltName: Full=Protein L2;
GN   ORFNames=C2, L2;
OS   Tomato leaf curl virus (strain Australia) (ToLCV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=223353;
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=8423446; DOI=10.1099/0022-1317-74-1-147;
RA   Dry I.B., Rigden J.E., Krake L.R., Mullineaux P.M., Rezaian M.A.;
RT   "Nucleotide sequence and genome organization of tomato leaf curl
RT   geminivirus.";
RL   J. Gen. Virol. 74:147-151(1993).
CC   -!- FUNCTION: Strong activator of the late viral genes promoters. Acts as a
CC       suppressor of RNA-mediated gene silencing, also known as post-
CC       transcriptional gene silencing (PTGS), a mechanism of plant viral
CC       defense that limits the accumulation of viral RNAs. TrAP suppresses the
CC       host RNA silencing by inhibiting adenosine kinase 2 (ADK2), a kinase
CC       involved in a general methylation pathway. Also suppresses the host
CC       basal defense by interacting with and inhibiting SNF1 kinase, a key
CC       regulator of cell metabolism implicated in innate antiviral defense.
CC       Determines pathogenicity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction correlates
CC       with nuclear localization and efficient activation of transcription.
CC       Monomers suppress local silencing by interacting with and inactivating
CC       host adenosine kinase 2 (ADK2) in the cytoplasm. Interacts with and
CC       inhibits host SNF1 kinase. Binds to ssDNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=The phosphorylated form appears to accumulate
CC       almost exclusively in the nucleus, whereas the non-phosphorylated form
CC       is found in both nucleus and cytoplasm. {ECO:0000250}.
CC   -!- DOMAIN: The zinc finger and the transactivation region are involved in
CC       PTGS suppression. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
CC       protein family. {ECO:0000305}.
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DR   EMBL; S53251; AAM33780.1; -; Genomic_DNA.
DR   PIR; JQ1888; JQ1888.
DR   RefSeq; NP_632005.1; NC_003896.1.
DR   SMR; P36280; -.
DR   GeneID; 944503; -.
DR   KEGG; vg:944503; -.
DR   Proteomes; UP000008246; Genome.
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   InterPro; IPR000942; Gemini_AL2.
DR   Pfam; PF01440; Gemini_AL2; 1.
DR   PRINTS; PR00230; GEMCOATAL2.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Host cytoplasm; Host nucleus;
KW   Host-virus interaction; Metal-binding; Phosphoprotein;
KW   Suppressor of RNA silencing; Zinc; Zinc-finger.
FT   CHAIN           1..135
FT                   /note="Transcriptional activator protein"
FT                   /id="PRO_0000222233"
FT   ZN_FING         37..54
FT                   /evidence="ECO:0000250"
FT   REGION          77..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..135
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250"
FT   MOTIF           17..32
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        90..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  15304 MW;  486B1D56B99F1806 CRC64;
     MQNSSPSTSH YTQVPIKVQH KIAKKRSIRR KRIDLPCGCS YYLHINCHNH GFTHRGTHHC
     SSSDEWRVYL EGSKSPLFQD HKAPQAPVQL QPRHHSSPDT VQSQPEESIG DTQMLPGLHS
     FHSLTTSDLA FLEGI