ID   TRAP_ABMVW              Reviewed;         129 AA.
AC   P21944;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 3.
DT   23-FEB-2022, entry version 87.
DE   RecName: Full=Transcriptional activator protein;
DE            Short=TrAP;
DE   AltName: Full=Protein AC2;
DE   AltName: Full=Protein AL2;
GN   ORFNames=AC2, AL2;
OS   Abutilon mosaic virus (isolate West India) (AbMV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=10816;
OH   NCBI_TaxID=3630; Abutilon.
OH   NCBI_TaxID=3635; Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OH   NCBI_TaxID=47605; Hibiscus.
OH   NCBI_TaxID=96479; Malva.
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH   NCBI_TaxID=108335; Sida.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2219703; DOI=10.1016/0042-6822(90)90343-p;
RA   Frischmuth T., Zimmat G., Jeske H.;
RT   "The nucleotide sequence of abutilon mosaic virus reveals prokaryotic as
RT   well as eukaryotic features.";
RL   Virology 178:461-468(1990).
RN   [2]
RP   SEQUENCE REVISION.
RA   Jeske H.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; X15983; CAA34112.2; -; Genomic_DNA.
DR   PIR; D36214; QQCVW4.
DR   RefSeq; NP_047217.2; NC_001928.2.
DR   GeneID; 956372; -.
DR   KEGG; vg:956372; -.
DR   Proteomes; UP000006885; 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..129
FT                   /note="Transcriptional activator protein"
FT                   /id="PRO_0000222222"
FT   ZN_FING         33..50
FT                   /evidence="ECO:0000250"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..114
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        84..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  14627 MW;  89CAE4DE0FC3BB9F CRC64;
     MRSSSPSQPP SIKKAHRQAK RRAIRRRRID LQCGCSIYFH IDCTGHGFTH RGIHHCTSGG
     EWRVYLGDSK SPVFQDIQSR GPAIHQNEDI PCTNTVQPQP EESVASPQSL PELPSLDDFD
     DSFWVNLFK