ID A0A364L809_9EURO Unreviewed; 776 AA. AC A0A364L809; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 31-JUL-2019, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RAO71944.1}; 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 -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000256|RuleBase:RU000492}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. 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|RuleBase:RU000492}; KW Complete proteome {ECO:0000313|Proteomes:UP000249363}; KW Helicase {ECO:0000256|RuleBase:RU000492}; KW Hydrolase {ECO:0000256|RuleBase:RU000492}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000492}; KW Reference proteome {ECO:0000313|Proteomes:UP000249363}. FT DOMAIN 188 216 Q_MOTIF. {ECO:0000259|PROSITE:PS51195}. FT DOMAIN 219 437 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 489 640 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT REGION 1 33 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 64 184 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 253 272 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 380 407 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 687 718 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT MOTIF 188 216 Q motif. {ECO:0000256|PROSITE-ProRule: FT PRU00552}. FT COMPBIAS 1 28 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 84 101 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 110 165 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 254 271 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 383 397 Acidic. {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 //