ID A0A1E4T235_9ASCO Unreviewed; 1228 AA.
AC A0A1E4T235;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=CANARDRAFT_232743 {ECO:0000313|EMBL:ODV85815.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV85815.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) 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 {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; KV453851; ODV85815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4T235; -.
DR STRING; 983967.A0A1E4T235; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000094801; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:UniProt.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR GO; GO:0006396; P:RNA processing; IEA:UniProt.
DR CDD; cd17982; DEXHc_DHX37; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000094801}.
FT DOMAIN 403..581
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 676..852
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 138986 MW; 023A1D179A4ED216 CRC64;
MGKRSFYGKA EQGPTDNIID ESNTQDDVSS TNKSSDGLTT AMTDQEKNKR KRKMKETLLK
NHQEKASRQK RKRMDKYIEH QLKREEKEIL FKKLEETRID SSMLKSAKLL GTGSTKTKRE
QFLEALELEK QGKGTDETKE ILYEERTIKK WDDSDNEDFP SGQAENEEEF KSTDDVGSGF
IDYRPAQPFT GIGTGFGFGN IAKVEKKVKR VTKNYSWRAK IEAEEKKKSK TEDDQDFDSS
SDEEVFDEDD SEDVSQNVEK KTSNDKTKIE SEEDDDNESD EDKSSEEEDS SEQESESEEE
EEDEEESVVA SKHSERAQGF KEWAEQQTRI MEQRTEFVAP TAPQADYTPI VREEDLNDGL
EQEYIPINED LKRKVFTVEV ERDDSIQQSR MQLPVYAEEH RIMEAIHHND CVIICGETGS
GKTTQVPQFL FESGYGNPQS ETPGMIGVTQ PRRVAAVAMS ERVGNELGNH SSKVGYQIRF
DATVKSTTAL KFMTDGVLLR EMMTDFLLTK YSALIIDEAH ERNINTDILI GMLSRVLKLR
REYHEKNPTK YTPLKLVIMS ATLRVSDFSE NKVLFDTPPP ILKVDARQYP VSIHFNKRTA
FNYTEEAFNK TCKIHKRLPP GGILVFLTGK AEITAMVKRL RARFPTPTTT KNKGSQKYIE
EDIPELKVSA KNADVEAEEI DFEVNEMIDD FNDEVGESGD DEEEEEEGFE ETLEEGQTDN
DPLYILPLYS LLPTKEQMKV FEEPPAGARL CVIATNVAET SLTIPGIRYV VDCGRSKERH
FNEDTGVQSF EVGWISKASS DQRAGRAGRT GPGHCYRLFS SAVYMNDFPQ FSKPEILRMP
VESVVLSMKS MGIDTISNFP FPTPPDRLML HKAEMLLQYL GALNDKKTIT DLGRTMSLFP
LSPRFSKMLI IGNQLECLPY VIALVSGLSV GDPFLSEFEL EDEEENPKDI EFKRQTLSKY
NKSSALFTKL DKSSDAMKLL SVICALDHIP INKREAFFEN NFLRAKVMEE TSKLRKQLTY
IVKVNTTKES IASTSNVEDK DLKLGKPSKQ QIQAIKQMIT SGFVDQIAVR ADTIDREVKI
TNNSNIINVP YLTLFPSSAS KQDNLDKFVY IHPSSILTKS GELPPQFLIY QSLNLGANQV
ANRVSKLRFK PLTDITGKAL ANVAKNSSLI TYSKPLGHPY SPKDISPTER ECYVIPRIGA
AIGSGGVGWD LPVVKVKQKK VMGSWVIQ
//
