ID   TRAP_SLCV               Reviewed;         131 AA.
AC   P27445;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Transcriptional activator protein;
DE            Short=TrAP;
DE   AltName: Full=Protein AC2;
DE   AltName: Full=Protein AL2;
GN   ORFNames=AC2, AL2;
OS   Squash leaf curl virus (SLCV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=10829;
OH   NCBI_TaxID=3662; Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var. moschata).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1984668; DOI=10.1016/0042-6822(91)90009-z;
RA   Lazarowitz S.G., Lazdins I.B.;
RT   "Infectivity and complete nucleotide sequence of the cloned genomic
RT   components of a bipartite squash leaf curl geminivirus with a broad host
RT   range phenotype.";
RL   Virology 180:58-69(1991).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC32413.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M38183; AAC32413.1; ALT_INIT; Genomic_DNA.
DR   PIR; F36785; QQCVS4.
DR   RefSeq; NP_047246.1; NC_001936.1.
DR   GeneID; 956397; -.
DR   KEGG; vg:956397; -.
DR   Proteomes; UP000009151; 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..131
FT                   /note="Transcriptional activator protein"
FT                   /id="PRO_0000222229"
FT   ZN_FING         33..52
FT                   /evidence="ECO:0000250"
FT   REGION          78..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..131
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250"
FT   MOTIF           13..28
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        98..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   131 AA;  14584 MW;  3A6DA7B590D2C22A CRC64;
     MPNSSSSKVP SIKAQHRIAK KRAVRRRRID LDCGCSIYIH INCAKDGNGF THMGRHHCAS
     GREFRFYLGG SKSPLFQDVQ XGGSTLHAHK DIPHTNPVQP QPEESTKSSQ SVPELPSLDG
     IDSSFWDDIF E