ID W0TC88_KLUMD Unreviewed; 768 AA.
AC W0TC88;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=PRP43 {ECO:0000313|EMBL:BAO40643.1};
GN ORFNames=KLMA_40619 {ECO:0000313|EMBL:BAO40643.1};
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO40643.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO40643.1, ECO:0000313|Proteomes:UP000065495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC {ECO:0000313|Proteomes:UP000065495};
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
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; AP012216; BAO40643.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TC88; -.
DR VEuPathDB; FungiDB:KLMA_40619; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000065495; Chromosome 4.
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:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR GO; GO:0006396; P:RNA processing; IEA:UniProt.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:BAO40643.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 102..267
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 292..472
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 735..762
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 768 AA; 87345 MW; ABEFF060EC7AF689 CRC64;
MGKRKLSNEH VSAVETSIPE HAAEIAEQRS KEHPLVFEEP LVHHDAGEFS GMVRHQTTAE
EAEKLENASV NPFTGNPYSE KYYGILKVRR DLPVHAQRAE FLKIYQENQI MVFVGETGSG
KTTQIPQFVL FDEMPHLRNT QVACTQPRRV AAMSVAQRVA EEMDVKLGEE VGYSIRFENK
TSNKTILKYM TDGMLLREAM EDHDLKRYSC IILDEAHERT LATDILMGLL KQVVQRRPDL
KIIIMSATLD AEKFQKYFNK APLLAVPGRT HPVEIYYTPE FQRDYLDSAI RTVLQIHATE
EKGDVLLFLT GEDEIEDAVR KISLEGDQLI REQGCGPLSV YPLYGSLPPH QQQRIFEPAP
ESHNGRPGRK VIVSTNIAET SLTIDGIVYV VDPGFSKQKV YNPRIRVESL LVSPISKASA
QQRAGRAGRT RPGKCFRLYT EEAFKKELIE QSYPEILRSN LSSTVLELKK LGIDDLVHFD
FMDPPAPETM MRALEELNFL ACLDDDGNLT PLGRLASQFP LDPMLAVMLI GSPEFSCSEE
ILTIVAMLSV PSVFIRPSKD KKRADDIKSA FAHPDGDHLT LLNVYHAFKS DEAYEYGINK
WCRDNFLNYR SLSAADNIRN QLERLMTRYN LELNTSDYNS PKYFDNIRKA LAAGFFMQVA
KKRSGGKGYI TVKDNQDVLI HPSTVLGHDA EWVVYNEFVL TSKNYIRTVT SVRPEWLLEV
APAYYNLDHF QKGDIKLSLE RIKQKVDKME ELNKERKSKS GKSKKSKK
//
