ID A0A1V1STD7_9FUNG Unreviewed; 788 AA. AC A0A1V1STD7; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 02-JUN-2021, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAW11866.1}; GN ORFNames=ANO14919_012190 {ECO:0000313|EMBL:GAW11866.1}; OS fungal sp. No.14919. OC Eukaryota; Fungi. OX NCBI_TaxID=1813822 {ECO:0000313|EMBL:GAW11866.1, ECO:0000313|Proteomes:UP000189293}; RN [1] {ECO:0000313|EMBL:GAW11866.1, ECO:0000313|Proteomes:UP000189293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=No.14919 {ECO:0000313|EMBL:GAW11866.1, RC ECO:0000313|Proteomes:UP000189293}; RG Technology Reseach Association of Highly Efficient Gene Design; RA Itoh H., Matsui M., Shibata T.; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAW11866.1, ECO:0000313|Proteomes:UP000189293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=No.14919 {ECO:0000313|EMBL:GAW11866.1, RC ECO:0000313|Proteomes:UP000189293}; RA Itoh H., Matsui M., Kumagai T., Arita M., Machida M., Shibata T.; RT "Genome Sequence of Fungus Strain No.14919 Producing HMG-CoA Reductase RT Inhibitor FR901512."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. 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:GAW11866.1}. 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; BDMC01000002; GAW11866.1; -; Genomic_DNA. DR OrthoDB; 268859at2759; -. DR Proteomes; UP000189293; 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:0016787; F:hydrolase 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492}; KW Coiled coil {ECO:0000256|SAM:Coils}; 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:UP000189293}. FT DOMAIN 244..272 FT /note="Q_MOTIF" FT /evidence="ECO:0000259|PROSITE:PS51195" FT DOMAIN 275..449 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 479..626 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 1..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 94..246 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 701..788 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 632..665 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 244..272 FT /note="Q motif" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552" FT COMPBIAS 1..33 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..76 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 104..134 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 135..155 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 170..195 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..239 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 701..736 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 788 AA; 86607 MW; A21AF4780F77D911 CRC64; MASKRKADDF IYTLSDNDDI PDHEEVTEPN PPKKKSKKSK KGAPVDDDIE DGVWGKKEDD DGAMDSEFEF AEDKTTDFRT EDFEGWGFEG AHKAMNGAAQ KKVVDVDEIV RRRRGGQGNA EVESERKHSQ DSDPELEEGD EDIDLDDDDD EVLAEDGFGM GAASDDESGD EGAGINEEEE DEDAGENDDA ASDDDSVATP IDHPDDMGQS DATDDEEDPE EAAKREAFFA PEDKKTSGKQ TGKSSFQTMS LSRPILRGLN SVGFNTPTPI QAKTIPLALE GRDLVGGAVT GSGKTAAFVV PILERLLYRP NRIPTSRVVI LAPTRELAIQ CHAVATKLSS HTDIKFCLAV GGLSLKVQEA ELRLRPDVII ATPGRFIDHM RNSASFATDT IEILVLDEAD RMLEDGFADE LNEILTTLPK SRQTMLFSAT MTSSVDRLIR VGLNKPVRVM VDSQKKTVDK LEQKFVRLRP GREEKRMGYL IHICKTMHTE RVIIFFRQKK DAHRARIIFA LFNLSCAELH GSMNQSQRIA SVEAFRDGKV NFLLATDLAS RGLDIKGVDT VINYESPQTL EIYVHRVGRT ARAGRSGVAI TLAAEPDRKV VKAAVKAGKS QGAKISSLVI EPADADGWHT RIEESEDEIA AIAREEKEER QLAQAEMQIR KGENMVTHED EIKARPKRTW FETQADKKAA KEAGRAELNG FRDALKKKGG GKLSNKDKKK LDARSTRKED AEGAGGRMWK KGAAERAGKG AVLNFAKDKS KTKKKVSGPG VKASAKVSGK GRTGGKRR //