ID   A0A0D1ZGV2_EXOME        Unreviewed;       800 AA.
AC   A0A0D1ZGV2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=PV10_05086 {ECO:0000313|EMBL:KIV93912.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV93912.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV93912.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV93912.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847522; KIV93912.1; -; Genomic_DNA.
DR   RefSeq; XP_016225486.1; XM_016369698.1.
DR   AlphaFoldDB; A0A0D1ZGV2; -.
DR   STRING; 212818.A0A0D1ZGV2; -.
DR   GeneID; 27322931; -.
DR   VEuPathDB; FungiDB:PV10_05086; -.
DR   HOGENOM; CLU_001832_7_2_1; -.
DR   OMA; MKVYPLY; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000054302; 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; IPR048333; HA2_WH.
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; PF04408; HA2_N; 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:KIV93912.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054302}.
FT   DOMAIN          145..310
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          335..517
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          41..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   800 AA;  90056 MW;  E4FCF1907DA4A14A CRC64;
     MTIWNNRLPL EINHLIANRS ALLPHRLCLL HPSISNFGPT MAGKHSDAVD GTPSKRQKTS
     NDVDPKNNPY LSHWYDNTTN GTSNGNVAGG PLSLLKRHQT TATLARQVED SKINPFTGRP
     ASDRYFSILK TRRDLPVHAQ RDEFLQLYQK SQILVFVGET GSGKTTQIPQ FVLYDDLPQQ
     ERKLVACTQP RRVAAMSVAE RVAQELDVKL GDEVGYSIRF EDMTSQKTVL KYMTDGMLLR
     EAMNDHDLSR YSTIILDEAH ERTLATDILM GLLKDVVGRR PDLKLIIMSA TLDAQKFQRY
     FLDAPLLAVP GRTHPVEIFY TPEPERDYVE AAIRTVLQIH ATEAEGDILL FLTGEEEIED
     ACRKISLEAD EMAREADAGP VKVYPLYGSL PPAQQQRIFE PAPPPRRPGG RPGRKCIVAT
     NIAETSLTID GIVYVVDPGF SKQKVYNPRI RVESLLVSPI SKASAQQRAG RAGRTRPGKC
     FRLYTEGAFK KELIEQTYPE ILRSNLSSTV LELKKLGVDD LVHFDLMDPP APETLMRALE
     ELNYLACLDD DGNLTTMGRL ASEFPLDPAL AVMLISSPEF YCSNEILSLT ALLSVPQVFV
     RPASARKRAD EMKNLFAHTD GDHLTLLNVY HAFKGEAAQA NPKQWCHDHF LSLRALQSAD
     NVRLQLKRIM ERSELELIST PFEDKKYYEN IRRALVSGFF MQVAKKEANG KTYTTVKDNQ
     TVLLHPSTVL GQESDWVIYN EFVLTSKNYI RTVTGVRGEW LLDLAPGYYD IDSFPKGEVK
     TALQRLSERV ARRQKMKAGR
//