ID   TRAP_TYLCI              Reviewed;         135 AA.
AC   P27262;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   29-SEP-2021, entry version 59.
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 virus (strain Israel) (TYLCV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=66366;
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=1926771; DOI=10.1016/0042-6822(91)90763-2;
RA   Navot N., Pichersky E., Zeidan M., Zamir D., Czosnek H.;
RT   "Tomato yellow leaf curl virus: a whitefly-transmitted geminivirus with a
RT   single genomic component.";
RL   Virology 185:151-161(1991).
RN   [2]
RP   DNA-BINDING.
RX   PubMed=8610454; DOI=10.1006/viro.1996.0157;
RA   Noris E., Jupin I., Accotto G.P., Gronenborn B.;
RT   "DNA-binding activity of the C2 protein of tomato yellow leaf curl
RT   geminivirus.";
RL   Virology 217:607-612(1996).
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 (By similarity). Binds to ssDNA.
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; X15656; CAA33689.1; -; Genomic_DNA.
DR   PIR; C40779; QQCVC4.
DR   PRIDE; P27262; -.
DR   Proteomes; UP000007547; 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   1: Evidence at protein level;
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_0000222232"
FT   ZN_FING         37..54
FT                   /evidence="ECO:0000250"
FT   REGION          77..117
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        87..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  15611 MW;  F111C8C2F7E9DD32 CRC64;
     MQPSSPSTSH CSQVSIKVQH KIAKKKPIRR KRVDLDCGCS YYLHLNCNNH GFTHRGTHHC
     SSGREWRFYL GDKQSPLFQD NRTQPEAISN EPRHHFHSDK IQPQHQEGNG DSQMFSRLPN
     LDDITASDWS FLKSI