ID   TRAP_MYMVV              Reviewed;         135 AA.
AC   Q9YPS3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   23-FEB-2022, entry version 55.
DE   RecName: Full=Transcriptional activator protein;
DE            Short=TrAP;
DE   AltName: Full=Protein AC2;
DE   AltName: Full=Protein AL2;
GN   ORFNames=AC2, AL2;
OS   Mungbean yellow mosaic virus (strain Vigna) (MYMV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=223295;
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3915; Vigna mungo (Black gram) (Phaseolus mungo).
OH   NCBI_TaxID=157791; Vigna radiata (Mung bean).
OH   NCBI_TaxID=3916; Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OH   NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15290387; DOI=10.1007/s00705-004-0313-z;
RA   Karthikeyan A.S., Vanitharani R., Balaji V., Anuradha S.,
RA   Thillaichidambaram P., Shivaprasad P.V., Parameswari C., Balamani V.,
RA   Saminathan M., Veluthambi K.;
RT   "Analysis of an isolate of Mungbean yellow mosaic virus (MYMV) with a
RT   highly variable DNA B component.";
RL   Arch. Virol. 149:1643-1652(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=15956560; DOI=10.1128/jvi.79.13.8149-8163.2005;
RA   Shivaprasad P.V., Akbergenov R., Trinks D., Rajeswaran R., Veluthambi K.,
RA   Hohn T., Pooggin M.M.;
RT   "Promoters, transcripts, and regulatory proteins of Mungbean yellow mosaic
RT   geminivirus.";
RL   J. Virol. 79:8149-8163(2005).
RN   [3]
RP   FUNCTION, NUCLEAR LOCALIZATION SIGNAL, TRANSACTIVATION REGION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15681452; DOI=10.1128/jvi.79.4.2517-2527.2005;
RA   Trinks D., Rajeswaran R., Shivaprasad P.V., Akbergenov R., Oakeley E.J.,
RA   Veluthambi K., Hohn T., Pooggin M.M.;
RT   "Suppression of RNA silencing by a geminivirus nuclear protein, AC2,
RT   correlates with transactivation of host genes.";
RL   J. Virol. 79:2517-2527(2005).
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       ECO:0000269|PubMed:15681452, ECO:0000269|PubMed:15956560}.
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:0000269|PubMed:15681452}. Host
CC       cytoplasm {ECO:0000250}. Note=The phosphorylated form appears to
CC       accumulate almost exclusively in the nucleus, whereas the non-
CC       phosphorylated form is found in both nucleus and cytoplasm.
CC       {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; AJ132575; CAA10706.1; -; Genomic_DNA.
DR   Proteomes; UP000007784; 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_0000324753"
FT   ZN_FING         37..54
FT                   /evidence="ECO:0000250"
FT   REGION          82..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..135
FT                   /note="Transactivation"
FT   MOTIF           17..32
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15219 MW;  30D7E7A0493E1C1E CRC64;
     MRNSTPSKNH FSPPSIKAQH KVAKKRAIRR SRIDLSCGCS YYIHINCRNY GFSHRGQHHC
     SSTQEWRLYL GGAKSPLFQD HAAPSNSSRV PDVCDPNTDN VQPRVEESTA DAQMLPGSDA
     LPLFDGDFWD DIIDF