DBP4_EMENI
ID DBP4_EMENI Reviewed; 812 AA.
AC Q5BFU1; C8VSB7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP-dependent RNA helicase dbp4;
DE EC=3.6.4.13;
GN Name=dbp4; ORFNames=AN0589;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000007; EAA66688.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89171.1; -; Genomic_DNA.
DR RefSeq; XP_658193.1; XM_653101.1.
DR AlphaFoldDB; Q5BFU1; -.
DR SMR; Q5BFU1; -.
DR STRING; 162425.CADANIAP00002085; -.
DR EnsemblFungi; CBF89171; CBF89171; ANIA_00589.
DR EnsemblFungi; EAA66688; EAA66688; AN0589.2.
DR GeneID; 2876356; -.
DR KEGG; ani:AN0589.2; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q5BFU1; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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..812
FT /note="ATP-dependent RNA helicase dbp4"
FT /id="PRO_0000232199"
FT DOMAIN 79..253
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 279..438
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 503..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..76
FT /note="Q motif"
FT MOTIF 201..204
FT /note="DEAD box"
FT COMPBIAS 517..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 812 AA; 92025 MW; 0B796C65721958A3 CRC64;
MAPSNGHRNG KHAKSSNKSG NLKRKRVQED LSSLIKRVED LDLKAKYESF SDLPISEPTL
SGLTSSHFKT LTDIQSRAIS HALKGRDVLG AAKTGSGKTL AFLVPILENL YRKQWSDHDG
LGALIISPTR ELAIQIFEVL RKIGRYHTFS AGLVIGGKSL KEEQERLGRM NILVCTPGRM
LQHLDQTAFF ETYNLQMLVL DEADRIMDMG FQKTVDAIIG HLPPERQTLL FSATQTKKVS
DLARLSLQDP EYVAVHEAAS SATPSKLQQH YVVTPLPQKL DTLWSFIRSN LKSKTIVFMS
SGKQVRFVYE SFRHMQPGIP LLHLHGRQKQ GGRLDITTRF SQAQHAVLFS TDVAARGLDF
PAVDWVIQLD CPEDADTYIH RVGRTARYER DGRAVLFLDP SEEKGMLRRL EQKRVTVERI
NVRANKQQSI KNQLQNMCFK DPELKYLGQK AFISYVKSVY IQKDKETFNL KELKLDDFAA
SLGLPGAPRI KFIKGDDTKE RKNASRATAY LTSGDEESDE EGGKKKQPKE KEVRTKYDRM
FERRNQDVLA EHYSKLINDD GTIADSKNTE EADEDEDFLS VKRRFDAGDD ALHAEDSSAS
DSDASDSEAE DHTEKKDPKV VKISDKDTLV IDSKRREKLL KSKKKLLKFK GKGTKLVYDD
EGNAHELYEM EDEEAFKARG DAKEQQARFL AEEAARTQRA DMEDKEIAKQ KRREKKEKRK
ARERELLAEE EREERVAQLV PFDEDEDMGD AGGYSQSSDG EEEAPRPSKR AKVEEPKAVP
WYKKEAGKKN DAGEKQIQTL EDLESLATGL LG
