ID A0A0K0P9K1_9GEMI Unreviewed; 135 AA. AC A0A0K0P9K1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-JUN-2019, entry version 11. DE RecName: Full=Transcriptional activator protein {ECO:0000256|RuleBase:RU363028}; DE Short=TrAP {ECO:0000256|RuleBase:RU363028}; GN Name=AC2 {ECO:0000313|EMBL:AKQ21214.1}; OS Clerodendron yellow mosaic virus. OC Viruses; Geminiviridae; Begomovirus. OX NCBI_TaxID=326811 {ECO:0000313|EMBL:AKQ21214.1}; RN [1] {ECO:0000313|EMBL:AKQ21214.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MJGD1 {ECO:0000313|EMBL:AKQ21214.1}; RA Jaidi M., Srivastava A., Kumar S., Raj S.K.; RT "Molecular characterization of Clerodendron yellow mosaic virus RT causing yellow mosaic disease in Duranta erecta in India."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Strong activator of the late viral genes promoters. Acts CC as a suppressor of RNA-mediated gene silencing, also known as CC post-transcriptional gene silencing (PTGS), a mechanism of plant CC viral defense that limits the accumulation of viral RNAs. 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 {ECO:0000256|RuleBase:RU363028}. CC -!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction CC correlates with nuclear localization and efficient activation of CC transcription. {ECO:0000256|RuleBase:RU363028}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm CC {ECO:0000256|RuleBase:RU363028}. Host nucleus CC {ECO:0000256|RuleBase:RU363028}. CC -!- DOMAIN: The zinc finger and the transactivation region are CC involved in PTGS suppression. {ECO:0000256|RuleBase:RU363028}. CC -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator CC protein family. {ECO:0000256|RuleBase:RU363028}. 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; KR869857; AKQ21214.1; -; Genomic_DNA. 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 {ECO:0000256|RuleBase:RU363028}; KW DNA-binding {ECO:0000256|RuleBase:RU363028}; KW Host cytoplasm {ECO:0000256|RuleBase:RU363028}; KW Host nucleus {ECO:0000256|RuleBase:RU363028}; KW Host-virus interaction {ECO:0000256|RuleBase:RU363028}; KW Metal-binding {ECO:0000256|RuleBase:RU363028}; KW Suppressor of RNA silencing {ECO:0000256|RuleBase:RU363028}; KW Zinc {ECO:0000256|RuleBase:RU363028}; KW Zinc-finger {ECO:0000256|RuleBase:RU363028}. FT REGION 72 112 Disordered. {ECO:0000256|MobiDB-lite: FT A0A0K0P9K1}. SQ SEQUENCE 135 AA; 15435 MW; 5B9FD4E5331B95C7 CRC64; MRPSSPSTSR STQVPIKVQH RIAKRRAIRR KRIDLKCGCS YYLHINCHNH GFTHRGTHHC SSSDEWRVYL GGSKSPLFQD PKPPGQTILP EPRHNNNPDP VQPQPEESTG TTQMLHRLPD LDEFTSSDWS FLNGL //