ID   TRAP_TMOV               Reviewed;         129 AA.
AC   Q06658;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-FEB-2022, entry version 69.
DE   RecName: Full=Transcriptional activator protein;
DE            Short=TrAP;
DE   AltName: Full=Protein AC2;
DE   AltName: Full=Protein AL2;
GN   ORFNames=AC2, AL2;
OS   Tomato mottle virus (isolate Florida) (ToMoV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=223359;
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1469361; DOI=10.1099/0022-1317-73-12-3225;
RA   Abouzid A.M., Polston J.E., Hiebert E.;
RT   "The nucleotide sequence of tomato mottle virus, a new geminivirus isolated
RT   from tomatoes in Florida.";
RL   J. Gen. Virol. 73:3225-3229(1992).
RN   [2]
RP   PHOSPHORYLATION AT SER-109, AND MUTAGENESIS OF SER-109.
RX   PubMed=24990996; DOI=10.1128/jvi.00761-14;
RA   Shen W., Dallas M.B., Goshe M.B., Hanley-Bowdoin L.;
RT   "SnRK1 phosphorylation of AL2 delays Cabbage leaf curl virus infection in
RT   Arabidopsis.";
RL   J. Virol. 88:10598-10612(2014).
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 (By similarity). {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 at Ser-109 by A.thaliana KIN10.
CC       {ECO:0000269|PubMed:24990996}.
CC   -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
CC       protein family. {ECO:0000305}.
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DR   EMBL; L14460; AAC32417.1; -; Genomic_DNA.
DR   PIR; JQ1871; JQ1871.
DR   RefSeq; NP_047252.1; NC_001938.1.
DR   iPTMnet; Q06658; -.
DR   GeneID; 956412; -.
DR   KEGG; vg:956412; -.
DR   Proteomes; UP000008249; 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..129
FT                   /note="Transcriptional activator protein"
FT                   /id="PRO_0000222231"
FT   ZN_FING         33..50
FT                   /evidence="ECO:0000250"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..129
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250"
FT   MOTIF           13..28
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        73..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         109
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000269|PubMed:24990996"
FT   MUTAGEN         109
FT                   /note="S->A: Strongly reduces phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:24990996"
SQ   SEQUENCE   129 AA;  14503 MW;  A51FA1223739C9D9 CRC64;
     MRSSSPSQPP SIKRAHRQAK KRAIRRRRVD LQCGCSIYFH LGCAGHGFTH RGTHHCTSGG
     EWRVYLGARK SPLFQDTQSR GPTVYQNEGI PRTDTVQPQP EESVASPQSL PELPSLDDVD
     DSFWINLFS