DBP7_ASPOR
ID DBP7_ASPOR Reviewed; 760 AA.
AC Q2UE66;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP-dependent RNA helicase dbp7;
DE EC=3.6.4.13;
GN Name=dbp7; ORFNames=AO090026000744;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; AP007159; BAE60149.1; -; Genomic_DNA.
DR RefSeq; XP_001822151.1; XM_001822099.1.
DR AlphaFoldDB; Q2UE66; -.
DR SMR; Q2UE66; -.
DR STRING; 510516.Q2UE66; -.
DR EnsemblFungi; BAE60149; BAE60149; AO090026000744.
DR GeneID; 5994179; -.
DR KEGG; aor:AO090026000744; -.
DR VEuPathDB; FungiDB:AO090026000744; -.
DR HOGENOM; CLU_003041_26_2_1; -.
DR OMA; AVHIKAD; -.
DR Proteomes; UP000006564; Chromosome 3.
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:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..760
FT /note="ATP-dependent RNA helicase dbp7"
FT /id="PRO_0000232251"
FT DOMAIN 170..372
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 396..609
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 23..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..166
FT /note="Q motif"
FT MOTIF 308..311
FT /note="DEAD box"
FT COMPBIAS 24..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 760 AA; 84640 MW; 7627B40971F24709 CRC64;
MADDGLLLNF SIGDTNIIKP ETKLKGGTWR DRLSAKKIAQ HRTKNPRKPG EERPSSGKGP
QNPNRIQVSS SRPSKRQKTD ADGDNEKSRH DNKQHPRQFV SSLFSKNPTP RNAEEEPEQE
PVEDAKPTNA PLIDGLDTFT NLGLSPSLAA HLLTKLELKA PTGIQKASMS QLLKEDSDAF
IQAETGSGKT LAYLLPLVQR IMTVSNPKNM STNSKGEPIV HRDSGLFAIV LAPTRELCKQ
ISVVLESLLR CAHWIVAGTV IGGEKKKSEK ARLRKGLNIL VATPGRLADH LENTQALDVS
NVRWLVLDEG DRLMELGFEK ELQGIIQKLD ARQRPSRIPG IPTKRTTILC SATLKMNVQK
LGEISLKDAV HIKADPADED GETKRKDDDG FRVPAQLKQS YAIVAAKLRL VTLTAYLKRT
FMRKGSVMKA IVFVSCADSV DFHFEVFSRR KQYRDESEDE DEEKEDDDED NSKTKSEASP
HGTIAPAVAF SNPSNPVKLH KLHGSLPQHV RTATLNAFSR EREPSVLVCT DVASRGLDLP
NVDLVIEYDP AFSADDHTHR IGRTARLGRD GRALIFLMPG CEENYVEILK QGYRDGGKAL
TRTTAEDILK RGFGGNITSE TKNWEEKATD WQMDLERWAV DNPQYLEMAR RAYQSHIRAY
ATHIASERSM FNIKELHLGH LAKSFALRDR PSKINVPGLR PGDKEAKKDY KAERNTVGKK
RKAGGRDDDF QPSNDATSAA QKMRAKLKEH MAGASEFNLA
