ID A0A162IG93_9HYPO Unreviewed; 862 AA. AC A0A162IG93; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 14-DEC-2022, entry version 28. DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552}; DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552}; GN ORFNames=AAL_06015 {ECO:0000313|EMBL:KZZ92983.1}; OS Moelleriella libera RCEF 2490. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella. OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ92983.1, ECO:0000313|Proteomes:UP000078544}; RN [1] {ECO:0000313|EMBL:KZZ92983.1, ECO:0000313|Proteomes:UP000078544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ92983.1, RC ECO:0000313|Proteomes:UP000078544}; RX PubMed=27071652; DOI=10.1093/gbe/evw082; RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.; RT "Divergent and convergent evolution of fungal pathogenicity."; RL Genome Biol. Evol. 8:1374-1387(2016). 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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000256|ARBA:ARBA00004604}. 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:KZZ92983.1}. 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; AZGY01000014; KZZ92983.1; -; Genomic_DNA. DR AlphaFoldDB; A0A162IG93; -. DR STRING; 1081109.A0A162IG93; -. DR OrthoDB; 973872at2759; -. DR Proteomes; UP000078544; Unassembled WGS sequence. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR025313; DUF4217. 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; PF13959; DUF4217; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM01178; DUF4217; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KZZ92983.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000078544}; KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}. FT DOMAIN 74..102 FT /note="Q_MOTIF" FT /evidence="ECO:0000259|PROSITE:PS51195" FT DOMAIN 105..279 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 305..460 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT REGION 1..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 527..570 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 587..613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 715..845 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 74..102 FT /note="Q motif" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552" FT COMPBIAS 545..570 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 715..729 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 797..826 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 862 AA; 96071 MW; 25B015E6E8CB2241 CRC64; MPHPGGLSKD LSSVPKSHAL PPVAMAVRPD RRQQRLQKQS HPNHRQQKRK RDQDDLQTLE QAVADLDPKS TDITAFTDLP LSQPTAAGLK ASHFQTLTEV QQRAIPLALK NNDVLGAAKT GSGKTLAFLI PVLEKLYRSQ WTEYDGLGAL IISPTRELAV QIFEVLRKIG RNHVFSAGLV IGGKSLKEEA ERLARINILV CTPGRMLQHL DQTAGFDANN LQILVLDEAD RIMDMGFQSA VDALVDHLPK TRQTLMFSAT QSKKVSDLAR LSLHEPEYVS VHEAAASATP TNLQQNYVTM ALPDKLDTLW GFIKSNLKSK MIVFLSSGKQ VRFVYESFRH LQPGIPLLHL HGRQKQGARL KITSQFAAAK HSCLIATDVV ARGIDFPAVD WVIQADCPED VDTYIHRVGR TARYQSNGRA VLFLDPSEEE GMIKQLEQRK IPIKPIRVRE NRKKSIKDDL QNMCFQKPDL KYLGQKAFIS YTRAIHLRKH KDVFKLSELD LDAFAASLGL PGTPQIKFCK GSDIKKIKNA PRDGMSSGSE SEMDPDDAGE SKKKEKKNKK SDKVRTKYDK MFERQNQDVL SEHYSKLVAD DGGDGSGAQA DESDNDDDDN DILAVKRRLD DADIDAVIQG GQGHIRDAKV IGGLGGAEPF VIDSKRREKA LLSKKKMLKY KGQPTKLVFD EDGQAHELYE LQHEEDFKRQ GPAEDLRQQF VESEAARVRE ADVHDKQHAR EKRRLKKEKR KASERAGAAA MAGFASDDDD DGAQPTLVVG RGEDGDEDED PLALLRSLPV PGAAKDESDQ EPPRKKKKKD KKWFQDDDDV DEQRPSARST RAAAPKSKVF HVADEPETLE DLEALATGLL GD //