ID A2QPZ8_ASPNC Unreviewed; 671 AA.
AC A2QPZ8;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=An08g00760 {ECO:0000313|EMBL:CAK45228.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK45228.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK45228.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270157; CAK45228.1; -; Genomic_DNA.
DR RefSeq; XP_001392194.1; XM_001392157.1.
DR AlphaFoldDB; A2QPZ8; -.
DR EnsemblFungi; CAK45228; CAK45228; An08g00760.
DR GeneID; 4982390; -.
DR KEGG; ang:An08g00760; -.
DR VEuPathDB; FungiDB:An08g00760; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000006706; Chromosome 8R.
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 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF136; ATP-DEPENDENT RNA HELICASE DHX35-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAK45228.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 32..196
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 238..409
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 671 AA; 75042 MW; 04B2440C440EE39D CRC64;
MASELDLSTS FIPALYKPAA LLPIARHKQS LLYLVETYPV TIVVGQTGSG KTTQLPQYLD
QAGWCADGKA IAVTQPRRVA ATTVAARVAE EMRCKLGEDV GYSIRFEDLT SASTRIKFLT
DGMLLREALV DPLLSRYSVI MVDEAHERSL STDILLGILK KIMKRRPELR IVVSSATLQA
EDFLRFFAGE EFDSSPESGE IGGKVGRIIS LEGRMYPVDM LFLENPAEDY VERAVRTVFD
IHLQEAEGDI LVFLTGREEI DTTVQMIAER AATLHPKAQS ILPLPLYSGL TTDQQMYVFE
PTPENTRKVI VSTNIAEASV TINGIVYVID CGFAKLRAYN PQTGIETLTA VPISKAAAVQ
RAGRAGRTKP GKCFRLYTQQ AYEQLPEATV PEIQRSNLAP VIMQLKALGI DNIVRFDFLT
SPPTELVIRA FELLYSLGAV DDYAKLTKPH GMRMAELAVD PMMAKVLLSA PSFNCLSEIL
SIAAMVSLQG TVWVQHEGDR KSSESHRRKF AVEEGDHLTY LNVYQAFITK GKKDSKWCRD
NLLNFRSLQR AVSIRAQLKR YLERFGIQVD ETLSARSRQE DPSKLAEQIR RCLTTGYFAH
AAKMQPDGTF KTVSGGLTLH AHPSSLMFNR KADWVIFHEI LQTGEKTFIR DVTKIEKNYL
LEYAPNCYQV Y
//
