ID A0A364L809_9EURO Unreviewed; 776 AA. AC A0A364L809; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 07-OCT-2020, entry version 10. DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552}; DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552}; GN ORFNames=BHQ10_007956 {ECO:0000313|EMBL:RAO71944.1}; OS Talaromyces amestolkiae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces. OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO71944.1, ECO:0000313|Proteomes:UP000249363}; RN [1] {ECO:0000313|EMBL:RAO71944.1, ECO:0000313|Proteomes:UP000249363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIB {ECO:0000313|EMBL:RAO71944.1, RC ECO:0000313|Proteomes:UP000249363}; RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7; RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L., RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.; RT "Differential ?-glucosidase expression as a function of carbon source RT availability in Talaromyces amestolkiae: a genomic and proteomic RT approach."; RL Biotechnol. Biofuels 10:161-161(2017). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000256|ARBA:ARBA00001556}; CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000256|RuleBase:RU000492}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RAO71944.1}. 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; MIKG01000017; RAO71944.1; -; Genomic_DNA. DR Proteomes; UP000249363; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000492}; KW Reference proteome {ECO:0000313|Proteomes:UP000249363}. FT DOMAIN 188..216 FT /note="Q_MOTIF" FT /evidence="ECO:0000259|PROSITE:PS51195" FT DOMAIN 219..437 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 489..640 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 64..184 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 253..272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 380..407 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 687..718 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 188..216 FT /note="Q motif" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552" FT COMPBIAS 1..28 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 84..101 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 110..165 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 254..271 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 383..397 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 776 AA; 85753 MW; 1D072E425619EA5B CRC64; MGMKRGRESR NLAKKAAKKQ RVEENTGQDG EDIVGLDDLD WQTVQLPDRL GDVGGFFGLE EIDGVDIVRP ESTGQIKFKV SSDKPSKSIL KKAKPADETP SENNEEWSGF SEGEEQKGKP QKKQKQKKSE QQNSEEPKEK SATDDKKPVT KKQQQQQKAK AEKPNEKIQS LPFTALEDEE EEDEVDVSAW ESLGLSPALQ TGISKLKFST PSTIQQAVIP EVLAGHDVVG KASTGSGKTL AFGIPILEHY LNTRAQHDTP KENKKKEKKQ SQPIALILSP TRELAHQLAK HIGALNTHTP AANARIALLT GGLAIQKQQR LLKDADIVIG TPGRVWEILS SGTGLIQRMS RVKYLVLDEA DRLLSDGHYK ELEEILDALD RKEDNDEAEE NSEISEEDEE GQKEKATAAR QTLVFSATFH KGLQQKLAGK GKFMTSDLLN KSESMEYLLQ KLKFREEKPK FIDVNPISQM AQGLKEGILE CGAMEKDLYL YTLLLYHPGH RCLLFANSIS SVRRLSQLLQ NLGIPALALH STMEQKARLR SVERFSSPDA DPSSVLVATD VAARGLDIKG IDMVIHYHVP RTADMYVHRS GRTARAGASG KSVLICAPDE VVGVARLVAK VHAQAEAGAS ARRNPLESLE LDRRVVSRVK PRMTLAKKIT ESNLAKEKIS SEDNWLRNAA EELGVNYDSE EFEKQGGKSK GRGRGGGRSQ KEKEASSITK GELAGLRAEL KQHLSKRINI GISERYITAG RXDVESLLRG EGNNKAFIGL VDKLEF //