ID A0A1S9DYF9_ASPOZ Unreviewed; 929 AA.
AC A0A1S9DYF9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=OAory_01026840 {ECO:0000313|EMBL:OOO14089.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO14089.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO14089.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO14089.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000256|ARBA:ARBA00003706}.
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, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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:OOO14089.1}.
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DR EMBL; MKZY01000001; OOO14089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DYF9; -.
DR SMR; A0A1S9DYF9; -.
DR VEuPathDB; FungiDB:AO090023000504; -.
DR eggNOG; KOG0337; Eukaryota.
DR OMA; EDQFGMM; -.
DR Proteomes; UP000190312; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OOO14089.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 89..117
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 120..292
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 358..513
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 89..117
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 12..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..685
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 103096 MW; CF433DC2F9F7EB0A CRC64;
MPHRAASPAA SENEFDITNA LFQNDSDSDN DTSLKQTKRP QKAAPPQALD FLGGDIDDDE
DDEAFIAGQQ ASANRKASNL KGRTVKKGGG FQAMGLNAHL LKAITRKGFS VPTPIQRKTI
PVIMDGQDVV GMARTGSGKT AAFVIPMIEK LKSHSTKVGA RGLILSPSRE LALQTLKVVK
ELGKGTDLKS VLLVGGDSLE EQFSLMAGNP DIVIATPGRF LHLKVEMNLD LSSIRYVVFD
EADRLFEMGF ADQLTEILYG LPANRQTLLF SATLPKSLVE FARAGLQEPT LIRLDTESKI
SPDLENVFFS VKSSEKEGAL LHILHEVIKM PTGPTEAAQR QKEQGDGKNF KNFKKRKRGD
DKAINFQESP TKYSTIVFAA TKHHVDYLYS LLREAGFAVS YAYGSLDQTA RKIQVQNFRA
GLSNILVVTD VAARGIDIPI LANVINYDFP SQPKIFVHRV GRTARAGRKG WSYSLVRDAD
APYMLDLQLF LGRRLVIGRE HGDQVNFAED VVVGSLPRDG LSTSCEWVTK VLENEADIYS
QRTIAGKGEK LYMRTRNSAS LESAKRAKQV VSSDNWTAVH PLFNDQGSQM ELEREKMLAR
IGGYRPQETI FEVHNRRNGK HEGDEAIDTI KRIRTTVDYK KKKREMAEKQ SDFVEDASSG
NKGEANETEE TGAQPDEDEE DIGEGVPDNM SMASESDLEV TFSSYNGGKA KKDSAASFQN
PEYFMSYTPS STNLAEDRAY GVHTGTNANF TQASRSATMD LLGDEGARGF AEPRTMMRWD
KRHKKYVSRQ NDEDGSKGTH LVKGESGAKI ASTFRSGRFD AWRKGKRLGR MPRVGEEETP
ALVHDLNTAM RRRRFQHRKE QAPKAADRLR GDYEKMKKKG EAAKQRQLSK AGGAAAGGKS
ELKSTDDIRL ARKLKQQRRE KNARPSRKK
//
