ID A0A0D2BWG1_9EURO Unreviewed; 958 AA.
AC A0A0D2BWG1;
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=PV08_05647 {ECO:0000313|EMBL:KIW15599.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW15599.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW15599.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW15599.1,
RC ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
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};
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DR EMBL; KN847495; KIW15599.1; -; Genomic_DNA.
DR RefSeq; XP_016235815.1; XM_016379988.1.
DR AlphaFoldDB; A0A0D2BWG1; -.
DR STRING; 91928.A0A0D2BWG1; -.
DR GeneID; 27332730; -.
DR VEuPathDB; FungiDB:PV08_05647; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000053328; 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 CDD; cd17917; DEXHc_RHA-like; 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; 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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT DOMAIN 106..292
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 337..528
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..817
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 102914 MW; AB63C68B6D9810BF CRC64;
MSRPGTAASS HGKPKPAKGK KRSAAEAFAP KSTSVQDSLQ AHRKNPSVGK TVTFTDGPER
KRSENVATTQ PASPKSTKRP NLRERAHALL SVRQKLPIYE HADAIRQALR DSDVLLLVGE
TGSGKSTQIP QFLVNEEWCK KKTTKGGAKV GGCIAITQPR RVAAISLARR VAEEMGTPLG
NSSPASQVGY SVRFENSTGP ATKVKFLTEG MLLQEMLRDP WLKEYSAVVV DEVHERGVNV
DLVLGFLRRL HEQRNADDGR GGVSMKVVVM SATADMEKIQ RFFAFDPPDV PSKGGDDDKA
ALAKEAISTA AKTRTNATTL FIKGRQYPVT VNYTPAPVPD VIDAAFERIK HIHTHSPLPG
DILVFLTGQE TVESLMSLVT AWSTSIAKDA ALSKTHLPKL LVLPLYAALP SAAQQRVFQH
TPKFTRKIIL STNIAETSIT VPGIRHVIDT GKAKQRLFRP SLNLDTLLTV PISRSSANQR
SGRAGRDAPG TAYRLYTQSD FATLAQDTEP EVLRCDLSQL VLTLKAHGID DLASFPFLTT
PPRRALERAL VHLLQLSALD PRSGTITPLG REMSVLPLPA SLGRVLLASA EPDYACTDEI
IDIVSALSVE NIFLNVHTNR AAGGDSGPRS PWSSATRNPS DDSLTRLLSK SNSHTSRTDD
DADSDDDDGN SMSRSAIVSQ NRGALYRREG DHLTLLATMQ AYAAETTDRR RWCDDRAISH
RAMSGAMDVR KQLANVMERR RRRRRRSSSD RRKSKSSGAS TSTSTSASPS ASTRTGTTGP
GVTGAGTVQG ADVVDGTSDT DPPSPSPPPP PPHDPTTLPT RILKTLLTGF HTNVARLSSD
GSYRTLITNQ PVAIHPSSVL FSAAGGGGGG GSVMDDDDDD HRDSSATNAT TTMTRNPNRN
RPDTVGGGGG GGGGGGGGGN RRKYEGIMYN EFVFTGTKAY ARGVSAVEMR WIGEVLRS
//
