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 02-JUN-2021, entry version 85. 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}. 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; NC_001928.2. DR SMR; P21944; -. 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 GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. 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 //