DBP4_ASPOR
ID DBP4_ASPOR Reviewed; 796 AA.
AC Q2UHB7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP-dependent RNA helicase dbp4;
DE EC=3.6.4.13;
GN Name=dbp4; ORFNames=AO090023000510;
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-dependent RNA helicase required for ribosome biogenesis.
CC Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC Required for pre-rRNA cleavage at site A2 (By similarity).
CC {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 -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC ribosomal complexes (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC subfamily. {ECO:0000305}.
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DR EMBL; AP007157; BAE59048.1; -; Genomic_DNA.
DR RefSeq; XP_001821050.1; XM_001820998.1.
DR AlphaFoldDB; Q2UHB7; -.
DR SMR; Q2UHB7; -.
DR STRING; 510516.Q2UHB7; -.
DR EnsemblFungi; BAE59048; BAE59048; AO090023000510.
DR GeneID; 5993052; -.
DR KEGG; aor:AO090023000510; -.
DR VEuPathDB; FungiDB:AO090023000510; -.
DR HOGENOM; CLU_003041_26_1_1; -.
DR OMA; YDKMFER; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0034512; F:box C/D RNA binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..796
FT /note="ATP-dependent RNA helicase dbp4"
FT /id="PRO_0000232195"
FT DOMAIN 76..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 272..435
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..73
FT /note="Q motif"
FT MOTIF 198..201
FT /note="DEAD box"
FT COMPBIAS 509..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 796 AA; 90157 MW; 98D22FF3A3C8EB89 CRC64;
MAPSNGPRSG KNAKSSHTLK RKRAQDDLST LTQRVEDLDI KETYKSFSDL PLSEPTASGL
ASSHFKTLTD IQSRAIGHAL KGRDILGAAK TGSGKTLAFL IPVLENLYRK QWSEHDGLGA
LILSPTRELA IQIFEVLRKI GRYHTFSAGL IIGGKSLKEE QERLGRMNIL VCTPGRMLQH
LDQTAMFDVF NLQMLVLDEA DRILDMGFQK TVDAIVGHLP KERQTLLFSA TQTKKVSDLA
RLSLQDPEYV AVHETASSAT PSTLQQHYVV TPLSQKLDVL WSFIRSNLKA KTIVFLSSGK
QVRFVYESFR HLQPGIPLMH LHGRQKQGGR LDITAKFSQA KHAVLFSTDI TARGLDFPAV
DWVIQMDCPE DADTYIHRVG RTARYERDGR AVLFLDPSEE SGMLKRLEQK KVPIERINIK
ANKQQSIRDQ LQNMCFKDPE LKYLGQKAFI SYVKSVYVQK DKEVFKLKEL KLEDFASSLG
LPGAPRIKFI KGDDTKERKN ASRATAYLSS DDDSDEGGEK KSKKDEKQVR TKYDRMFERR
NQDVLADHYS KLINDDGTLV DPSKTASAAD DADEDDDFLS VKRRFDAGDE DLGGNSEEEL
EQKGVKVVQL DGKDTLVIDS KRREKLLKSK KKLLKFKGKG TKLIYDDEGN AHELYEMEDE
EDFKARGDAK EQQARFLAEE TERTRTADME DKEVAKQKRR EKKEKRKARE RELLAEEEAE
EAVAQLAPYK EDDEFSASDR EDDAPRPSKK QKVRIAEPEE SKEEPWYKKS KKPAAKAPEQ
IQTLEDLESL ATGLLG
