ID Q6FU15_CANGA Unreviewed; 768 AA.
AC Q6FU15;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN OrderedLocusNames=CAGL0F07139g {ECO:0000313|CGD:CAL0130980,
GN ECO:0000313|EMBL:CAG59203.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59203.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59203.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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DR EMBL; CR380952; CAG59203.1; -; Genomic_DNA.
DR RefSeq; XP_446279.1; XM_446279.1.
DR AlphaFoldDB; Q6FU15; -.
DR STRING; 284593.Q6FU15; -.
DR EnsemblFungi; CAGL0F07139g-T; CAGL0F07139g-T-p1; CAGL0F07139g.
DR GeneID; 2887645; -.
DR KEGG; cgr:CAGL0F07139g; -.
DR CGD; CAL0130980; CAGL0F07139g.
DR VEuPathDB; FungiDB:CAGL0F07139g; -.
DR eggNOG; KOG0925; Eukaryota.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; Q6FU15; -.
DR OMA; MKVYPLY; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IEA:EnsemblFungi.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IEA:EnsemblFungi.
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:EnsemblFungi.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IEA:EnsemblFungi.
DR CDD; cd17973; DEXHc_DHX15; 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; IPR044756; DHX15_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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 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:UP000002428}.
FT DOMAIN 106..271
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 296..476
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 87367 MW; FBEA50E9F5B154C3 CRC64;
MGSKRRFSGS QHEHADPVAT SIPEHAAEIA EDLTKKHPIP PEEPLVHHDA GEFNGLVRHK
TTVEQANKLE TGKINPFTGN QFSEKYFGIL KVRKDLPVHA QRAEFLKIYQ ENQIMVFVGE
TGSGKTTQIP QFVLFDEMPH LENTQIACTQ PRRVAAMSVA QRVAEEMDVK LGEEVGYSIR
FENKTSNKTI LKYMTDGMLL REAMEDHDLK RYSCIILDEA HERTLATDIL MGLIKQVVLR
RPDLKIIVMS ATLDAEKFQN YFHNAPLLAV PGRTYPVELY YTPEFQRDYL DSAIRTVLQI
HATEEAGDIL LFLTGEDEIE DAVRKISLEG DQLVREEGCG PLSVYPLYGS LPPHQQQRIF
EPAPESHNGR PGRKVVVSTN IAETSLTIDG IVYVVDPGFS KQKVYNPRIR VESLLVSPIS
KASAQQRAGR AGRTRPGKCF RLYTEEAFQK ELIEQSYPEI LRSNLSSTVL ELKKLGIDDL
VHFDFMDPPA PETMMRALEE LNYLACLDDE GNLTALGRLA SQFPLDPMLA VMLIGAFEFK
CSQEILTIVA MLSVPNVFIR PSKDKKRADD AKNIFAHPDG DHITLLNVYH AFKSDEAYEY
GINKWCRDHY LNYRSLSAAD NIRSQLERLM IRHNLELNTT DYESPQYFDN IRKALAAGFF
MQVAKKRSGG KGYITVKDNQ DVLIHPSTVL GHDAEWVIYN EFVLTSKNYI RTVTSVRPEW
LIELAPAYYD LDNFQKGDVK LSLERIQEKV ERMKELKKGK DKKKSKKK
//
