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 25-NOV-2008, entry version 44. 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; ssDNA viruses; 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 MEDLINE=91020984; 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 RT as 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. CC Enhances the expression of the capsid protein and nuclear shuttle CC protein. Acts as a suppressor of RNA-mediated gene silencing, also CC known as post-transcriptional gene silencing (PTGS), a mechanism CC of plant viral defense that limits the accumulation of viral RNAs. CC Suppresses the host RNA silencing by inhibiting adenosine kinase 2 CC (ADK2), a kinase involved in a general methylation pathway. Also CC suppresses the host basal defense by interacting with and CC inhibiting SNF1 kinase, a key regulator of cell metabolism CC implicated in innate antiviral defense. Determines pathogenicity CC (By similarity). CC -!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction CC correlates with nuclear localization and efficient activation of CC transcription. Monomers suppress local silencing by interacting CC with and inactivating host adenosine kinase 2 (ADK2) in the CC cytoplasm. Interacts with and inhibits host SNF1 kinase. Binds to CC ssDNA (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By CC similarity). Note=The phosphorylated form apears to accumulate CC almost exclusively in the nucleus, whereas the nonphosphorylated CC form is found in both nucleus and cytoplasm (By similarity). CC -!- DOMAIN: The zinc finger and the transactivation region are CC involved in PTGS suppression (By similarity). CC -!- PTM: Phosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator CC protein family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X15983; CAA34112.2; -; Genomic_DNA. DR PIR; D36214; QQCVW4. DR RefSeq; NP_047217.2; -. DR GeneID; 956372; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR InterPro; IPR000942; Gemini_AL2. DR Pfam; PF01440; Gemini_AL2; 1. DR PRINTS; PR00230; GEMCOATAL2. DR ProDom; PD001117; Gemini_AL2; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; Cytoplasm; DNA-binding; KW Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; KW Suppressor of RNA silencing; Zinc; Zinc-finger. FT CHAIN 1 129 Transcriptional activator protein. FT /FTId=PRO_0000222222. FT ZN_FING 33 50 By similarity. FT REGION 115 129 Transactivation (By similarity). FT MOTIF 13 28 Nuclear localization signal (By FT similarity). FT COMPBIAS 25 28 Poly-Arg. SQ SEQUENCE 129 AA; 14627 MW; 89CAE4DE0FC3BB9F CRC64; MRSSSPSQPP SIKKAHRQAK RRAIRRRRID LQCGCSIYFH IDCTGHGFTH RGIHHCTSGG EWRVYLGDSK SPVFQDIQSR GPAIHQNEDI PCTNTVQPQP EESVASPQSL PELPSLDDFD DSFWVNLFK //