ID K1VXK7_TRIAC Unreviewed; 1202 AA.
AC K1VXK7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=A1Q2_01446 {ECO:0000313|EMBL:EKD04227.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD04227.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD04227.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04227.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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 -!- 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:EKD04227.1}.
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DR EMBL; AMBO01000229; EKD04227.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VXK7; -.
DR STRING; 1220162.K1VXK7; -.
DR eggNOG; KOG0922; Eukaryota.
DR HOGENOM; CLU_001832_2_3_1; -.
DR InParanoid; K1VXK7; -.
DR OMA; DPMVAPE; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd21691; GH2-like_DHX8; 1.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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 Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 240..310
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 547..710
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 735..908
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 84..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 134206 MW; 654ECA6A0933CC0C CRC64;
MGADKELYKL ELLSLVSRVA QELFNHTKLQ DKSLAEFVIA SKNVDEFTKK LKEIGADFPE
SFIKNLDRLI ATMHPKYKRK AAKAKAKAAA GKGKSDVGES NDEKAIKARK FPGLSMPDQE
MKPEDTYLGG REGKDARDVD HDFSLDNTMA ELEKAASRRN RPAADDFMDG EPSGKRMRYD
DRDSGYDRQG RDRYDDRRRD RDDDAGYGIR DNGWAGRGGR PAPPEERRGR SGLDDAPVLY
KIYNGTVTGV RDFGAFVRLD GVAGNQEGLV HVSNITGARL ETASEGVRRN QRVKVKVISV
AGNKFGLSMK DVNQETGEDN TPHLRVKSRE EMEAEQRRMA ARVGTGANAA PLHSSSMPMD
QKRSAKRLTS PERFEIKQLI ASGAVSAADY PDLDDDFNAS NNNPEIDEDV DIEVAEKEPA
FLAGQTKITL DISPVKIVKA PDGSLNRAAL AGGQLAKERA EMRRMEANEQ ADKEAKNLAT
PWLDPMAQAS DRQFAADLRT NQQGQRQQQV PAWKKANKST TFGKITTMSI AEQRRSLPVY
KLRDQLVKAV RENQILVVVG DTGSGKTTQI AQYLAEDGLL EHGKLGCTQP RRVAAVSVAK
RVSEEVGCRL GSEVGYTVRF EDVTSPETKI KFMTDGMLLR ELLIDPDMSR YSVIMLDEAH
ERTIATDVLF GLMKKACKRR PDLKLICTSA TLDAEKFATY FWGCPIFTIP GRTFPVEILY
TKDPEPDYLE ASLITILQIH LMEPPGDILL FLTGQEEIDT ACEVLYERVK ALGPQVPELI
ILPVYAALPS EMQSKIFDPP PPGARKCVIA TNIAETSITI DGIYYVIDPG FSKQNAYDPK
LGMDSLIVTP ISQAQARQRS GRAGRTGPGK CYRLYTEIAY RNEMLPNPIP EIQRTNLAST
ILTLKAMGIN DLINFDFMDP PPAATMLTAL EQLYALGALD DEGLLTRVGR KMADFPLDPS
LCKVLIKSVD YGCSEEVLTI VSMLQAGGQI FYRPKDKQQQ ADAKKAKFHQ PEGDLLTLLA
VYNGWKASKF SNPWCFENFV HTRALKTAQN VRKQLVGIMD RYKHDLVSCG TNYNRVRMAI
CSGFFRNAAK KDPVEGYKTL VEGTPVSIHP SSALFQRPPE WCIYYELILT SKEYMSQVTV
IEPKWLSEVA PTFFKVADQN RISKRKQKEK IEPLFDRFAE SKDSWRLSKQ KRPIKNSQTF
GS
//
