ID   TRAP_TYCSV              Reviewed;         135 AA.
AC   P27263;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 76.
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 yellow leaf curl Sardinia virus (TYLCSV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=123735;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=185024; Cynanchum acutum.
OH   NCBI_TaxID=145753; Malva parviflora (Little mallow) (Cheeseweed mallow).
OH   NCBI_TaxID=29728; Sinapis arvensis (Charlock mustard) (Brassica kaber).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840676; DOI=10.1093/nar/19.24.6763;
RA   Kheyr-Pour A., Bendahmane M., Matzeit V., Accotto G.P., Crespi S.,
RA   Gronenborn B.;
RT   "Tomato yellow leaf curl virus from Sardinia is a whitefly-transmitted
RT   monopartite geminivirus.";
RL   Nucleic Acids Res. 19:6763-6769(1991).
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; X61153; CAA43464.1; -; Genomic_DNA.
DR   PIR; S22591; S22591.
DR   RefSeq; NP_620740.1; NC_003828.1.
DR   SMR; P27263; -.
DR   GeneID; 944424; -.
DR   KEGG; vg:944424; -.
DR   Proteomes; UP000002323; 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; Reference proteome;
KW   Suppressor of RNA silencing; Zinc; Zinc-finger.
FT   CHAIN           1..135
FT                   /note="Transcriptional activator protein"
FT                   /id="PRO_0000222234"
FT   ZN_FING         37..54
FT                   /evidence="ECO:0000250"
FT   REGION          120..135
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250"
FT   MOTIF           17..32
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15719 MW;  3DE9A8DC8918A485 CRC64;
     MQSSSPSTSH CSQIPIKIQH HIAKKRQVRR RRVDLDCGCS YYIHLDCINH GFTHRGVHHC
     ASSNEWRLYL RDNKSPIFHD NQTQSEPIQQ QIQHTNIPNQ IQPQLEEGTG DSQMFSQLPH
     LDDLTVSDWS FFKSL