ID   A0A0M8MYC0_9HYPO        Unreviewed;       826 AA.
AC   A0A0M8MYC0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=ESCO_002199 {ECO:0000313|EMBL:KOS21766.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21766.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS21766.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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. DEAH subfamily.
CC       DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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:KOS21766.1}.
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DR   EMBL; LGSR01000006; KOS21766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8MYC0; -.
DR   STRING; 150374.A0A0M8MYC0; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000053831; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd17973; DEXHc_DHX15; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044756; DHX15_DEXHc.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KOS21766.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT   DOMAIN          169..334
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          356..541
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   826 AA;  93553 MW;  B892D394EED8DB93 CRC64;
     MERSIAKRRR AVVVTQPLAI AEAARHVSAS DFDFDFDFDF DFDFDFDFDL SFLRGSRSVQ
     APAVIMGDSK AAKRSSAESD DFASKKIKTD DRRNPYLAHM YENGEDGEDG SDSSPLADFK
     RRETTAKQAA QAEDSTHNPF TGVAHSQKYF QILKTRRDLP VFKQRQEFLD KYHSTQILVF
     VGETGSGKTT QIPQYVVYDE LPNLTGKLIA CTQPRRVAAM SVAQRVADEM DVRLGEEVGY
     SIRFEDKTGP STMLKYMTDG MLLREAMHDH EMSRYSCIIL DEAHERTLAT DILMALLKQI
     AQRRADLKII IMSATLDAQK FQRYFNNAPL LAVPGRTHPV EIFYTPEPER DYVEAAIRTV
     LQIHASEPDG DVLLFLTGED EIEDACRKIR LEADELTREV GAGPLVVHPL YGTLPPHQQQ
     RIFDKAPEPL RKGGRPGRKV IVSTNIAETS LTIDGIVYVV DPGFSKQKIY NARIRVDSLL
     VSPISKASAQ QRAGRAGRTK PGKCFRLYTE KAFKKELIEQ THPEILRSNL ANTVLELKKL
     GVEDLVHFDL MDPPAPETMM RALEELNYLA CLDDEGELTT LGGLASEFPL DPALAVMLIS
     SPEFYCSNEV LSITSLLSVP QIFLRPANNR KRADEMKAHF SHPDGDHLTL LNAYHAFKGQ
     ETSNPDGLKN WCHEHFLSFR HLSSADSVRA QLKRIMETHA LELVSTPFED KNYYTNIRRA
     LLAGFFMQVA MKESSGKLYR TIKDEQAVLI HPSTVLRTEY DFVVYNEFVL TSKQYVRTVT
     GIRPEWLLDI APVYYDLDTF EKGDIKRALQ RAVEKKRRKE AMKAGR
//