ID A0A2S5BGV5_9BASI Unreviewed; 1187 AA.
AC A0A2S5BGV5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE Flags: Fragment;
GN ORFNames=BMF94_1088 {ECO:0000313|EMBL:POY76002.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY76002.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY76002.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY76002.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:POY76002.1}.
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DR EMBL; PJQD01000009; POY76002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5BGV5; -.
DR STRING; 741276.A0A2S5BGV5; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd17971; DEXHc_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; IPR044762; DHX8/Prp22_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; 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:UP000237144}.
FT DOMAIN 257..327
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 574..737
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 755..935
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 178..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1187
FT /evidence="ECO:0000313|EMBL:POY76002.1"
SQ SEQUENCE 1187 AA; 131083 MW; BE3D2FEEAC15BF88 CRC64;
MAGDELEKLE LLSLVNSITQ ELVNHTGLSD STLAEFLIHI HGESKDYASF KQKCAEVGAD
FPESFLQAVD RLVLSMHPKY KVKSKAVLPA KKLDGNLQGT PAAEPVDENK QKQMRLFPGL
AVPDSDWIPS YTPDDPATVK ERQMRLGQPV DVKGVVDRDD ATDMGVDDMM AQLEGVRKRT
AAGHADDDQG GKRQRHRSPD YERRDNGYGD RGGGGGGGRD NGYGDRGRNL GVPYGGGRDI
RTGGAGSSRA DEKPVLYKIY RGKVSNLKDF GAFVTLEGVM GRVEGMVHIG SISAGRVSHP
SDLLARNQSV FVKVMSVAGN RLSLSMRDAD QRTGADLSPH LRIKTEEELF EETRRAAERT
ASGANGVAAR KSFADDNRTA SVRRMTSPER WEIKQLIASG AASAADYPGL DEDYMNSGFD
TANGKSLADE ADEELDIEIN EAEAPFLHGQ SKRALELSPV KIVKAPDGGL NRAAMAGAAL
AKERREMKAQ EAADEADSEV RDVNTPWLDP MTAPHEKTFA ADARGATAAA KAKDMPAWKK
EAFNAATTFG KITSMTIADQ RKSLPIYKFR EQLIEAFANN QVLVVVGDTG SGKTTQMTQY
LAEAGYADRL KIGCTQPRRV AAMSVAKRVA EEVGCRLGQE VGYTIRFEDC TSPETKIKYM
TDGMLQRECL VDPDMSNYSV LMLDEAHERT IATDVLFGLL KKSLKRRPDL KLIVTSATLD
AEKFSEYFFG CPIFTIPGRT FPVEILYTKE PEPDYLDAAL ITIMQIHLSE PPGDILLFLT
GQEEIDTSCE ILYERMKALG PNVPDLIILP IYSALPSEMQ SRIFDPAPPG ARKVILATNI
AETSLTIDGI YYVVDPGFVK QNAYDPRLGM DSLIVTPISQ AQARQRSGRA GRTGPGKCYR
LYTEAAYRNE MLPNSIPDIQ RQNLAHTILM LKAMGINDLL NFDFMDPPPH QTMITALENL
YALSALDDEG LLTRLGRKMA DLPIEPPLAK MLIASVDLEC SEEILTIVAM LSVGGSVFYR
PKEKQAQADA KKAKFHQPEG DHLTLLTVYN GWAASKFSNP WCSENFIQGR AMRRAQDVRK
QLLGIMDRYK HDILSCGKNY NRVRRAITSG YFRHAAKKDP QEGYKTLVEG TPVFLHPSSA
LFNRAPEWCV YHELVLTTRE YMREVTAIEP KWLTEVAPSF FKVADQN
//