ID A0A1E3QAZ6_LIPST Unreviewed; 1283 AA.
AC A0A1E3QAZ6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=LIPSTDRAFT_1498 {ECO:0000313|EMBL:ODQ74738.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ74738.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ74738.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ74738.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; KV454291; ODQ74738.1; -; Genomic_DNA.
DR STRING; 675824.A0A1E3QAZ6; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000094385; 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: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; 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 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:UP000094385}.
FT DOMAIN 484..663
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 754..929
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 143116 MW; C2D798D7E7D91FD3 CRC64;
MGKYRIRHNA KARSGSITKQ RKLRSSRQPR ASRLPEAVEN GAVKDKAGSQ TSTTINTEHE
EQDPNAQVLV PMTAEEKATK RAELEQLLKP PESKWSRAKS KRLDKYIERQ LKREEKKVLL
QKLADSKFDT SLLHSLKRLG TNNMSRREQL QEALSKEKLG ILDEEASKLL YEERTIISEL
PISWNEPESP PASTQATAPA SLPLKRELEE SPSTTSQVID SISAVNNGNG STMSLFGSSH
GFGFGNLRKR PKTTATLINS NKQVPYTWRA RLEQEKLRKA KIPMMNSDDD YSSGSNSDDN
DDDEEKEEEE EDEWNGFDDD PTVAEGATIT DLFEDGKLAD NVSKDDAENC QGDGDEEDSD
GSDESVVHDD DDKEDEEEEE DEVEEEEETP GSRISRGESF KKWAEIQVRG GEAEELSNIN
TLPKTIGQYK PIDRPEDRAT PPPEIVTVDD AQNRKAYYVQ LDRHPDIQAV RILLPVVQDE
QRIMEAINNN LCVIICGETG SGKTTQVPQF LFEAGYGDPG SDNPGMIGIT QPRRVAAVSM
ARRVSDEIGS KHTGRVAYQI RFEQNTREGT AMKFMTDGVL LRELSTDFTL SKYSAIIIDE
AHERNVNTDI LIGVLSRVLK LRHEMSKESG SSTKPLKLII MSATLRVSDF SENSTLFEIA
PPVLNVEARQ FPVSNHFSRR TAVKYLDEAF TKIGKIHQRL PPGGILVFLT GQNEITHLCR
RLRQAFSKKG RHQKNVIDDA SVDVSLKLSA KEAGLEVEDI DLGDDIIEDV FDDNVSDSEL
PGEIEEGFEE QTDEINSAPL HVLPLYSLLP TAQQLKIFEP PPDGARLCVI ATNVAETSLT
IPGIRYIVDC GRVKERHYDE ETGVQRFDVS WISKASADQR AGRAGRTGPG HCYRLYSSAV
FESEFKQFSK AEILRMPIEG VVLQMKSMGI DTIANFPFPT APDRNTLVMA ENLLHYLGAI
NRAGRLTDLG MTMSVFPLAP RFAKMLVIGQ QFDCLQYVIA IVAGLSVGDP FLSEHELGIE
SEMLDNVDGD DSGEEGQMTH GEIELNKRRR KEYYIVRRKF SGLDASSDVL QMLSAICAYE
FENAKAEFCF KNFVRQKSME EIHKLRQQLT HIVAINTPNL ANLQFNTRLD APSTVQVKAL
KQIVASGFID QVVVRADLVA GFDLSSSASG PSKKKVKVTD IPYLRLNQYT FIRDTVFLSG
KGGVDKSCIR EPESPVYIHP SSVLLSSDES RNINEMAPFL IYNIIQQSSS GNTVKGGQQQ
PRIRVKPLTS ITGKQLANLA KTM
//
