ID   TRAP_PHUV               Reviewed;         138 AA.
AC   Q06924;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Transcriptional activator protein;
DE            Short=TrAP;
DE   AltName: Full=Protein AC2;
DE   AltName: Full=Protein AL2;
GN   ORFNames=AC2, AL2;
OS   Pepper huasteco yellow vein virus (PHYVV) (Pepper huasteco virus).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=223303;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8409944; DOI=10.1099/0022-1317-74-10-2225;
RA   Torres-Pacheco I., Garzon-Tiznado J.A., Herrera-Estrella L.,
RA   Rivera-Bustamante R.F.;
RT   "Complete nucleotide sequence of pepper huasteco virus: analysis and
RT   comparison with bipartite geminiviruses.";
RL   J. Gen. Virol. 74:2225-2231(1993).
CC   -!- FUNCTION: Strong activator of the late viral genes promoters. Enhances
CC       the expression of the capsid protein and nuclear shuttle protein. Acts
CC       as a 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. Suppresses the host
CC       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; X70418; CAA49857.1; -; Genomic_DNA.
DR   PIR; JQ2301; JQ2301.
DR   PIR; S31876; S31876.
DR   RefSeq; NP_040323.1; NC_001359.1.
DR   GeneID; 988145; -.
DR   KEGG; vg:988145; -.
DR   Proteomes; UP000002321; 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..138
FT                   /note="Transcriptional activator protein"
FT                   /id="PRO_0000222227"
FT   ZN_FING         42..59
FT                   /evidence="ECO:0000250"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..138
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250"
FT   MOTIF           23..37
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  15343 MW;  632C240358E4ACCC CRC64;
     MTGSKKTPST SPSKKLSSPP EVKLRHRFAK RQIRRRRIDL ACGCSIYIHI NCVNNGFTHR
     GTHHCSSSSE WRFYLGASKS PIFQNTASGD ANVHTQPGIS HSSQSKPQHE DSVGSPQSLL
     QLPSLDDVDD DFWADLLK