ID   DBP10_ASPTN             Reviewed;         928 AA.
AC   Q0CMM8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=ATP-dependent RNA helicase dbp10;
DE            EC=3.6.4.13;
GN   Name=dbp10; ORFNames=ATEG_05056;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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: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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476600; EAU34125.1; -; Genomic_DNA.
DR   RefSeq; XP_001214234.1; XM_001214234.1.
DR   AlphaFoldDB; Q0CMM8; -.
DR   SMR; Q0CMM8; -.
DR   STRING; 341663.Q0CMM8; -.
DR   PRIDE; Q0CMM8; -.
DR   EnsemblFungi; EAU34125; EAU34125; ATEG_05056.
DR   GeneID; 4321138; -.
DR   VEuPathDB; FungiDB:ATEG_05056; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000007963; 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:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10.
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; PTHR24031:SF292; PTHR24031:SF292; 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; 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..928
FT                   /note="ATP-dependent RNA helicase dbp10"
FT                   /id="PRO_0000281715"
FT   DOMAIN          120..292
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          361..515
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           89..117
FT                   /note="Q motif"
FT   MOTIF           240..243
FT                   /note="DEAD box"
FT   COMPBIAS        12..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..802
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..928
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   928 AA;  102988 MW;  2EB567DC5BE4CF58 CRC64;
     MPHRAASPAM SENEFDITNA LFQNDGDSDN EVPVTKSKPQ RKAAPQELDF LGGNVDDDDE
     DDEAFIAEQQ TSANRKAANL KGRTVKKGGG FQAMGLNANL LKAITRKGFS VPTPIQRKTI
     PVIMDDRDVV GMARTGSGKT AAFVIPMIEK LKSHSSKFGA RGLILSPSRE LALQTLKVVK
     ELGKGTDLKS VLLVGGDSLE EQFGMMAGNP DIVIATPGRF LHLKVEMNLD LSSIRYVVFD
     EADRLFEMGF AAQLTEILHG LPTTRQTLLF SATLPKSLVE FARAGLQEPT LIRLDTESKI
     SPDLQNAFFS VKSADKEGAL LYILHEVIKM PTGPTEVAQR LQEEKANSKD SKNSKKRKRS
     EMDKAVNMKE SPTKHSTIVF AATKHHVDYL YSLLREAGFA VSYAYGSLDQ TARKIQVNNF
     RTGLSNILVV TDVAARGIDI PILANVINYD FPSQPKIFVH RVGRTARAGR KGWSYSLVRD
     ADAPYLLDLQ LFLGRRLVLG REHGDQVDYA EDVVVGGFPR DSLAQNCEWV TRVLDDNRDI
     FSQRTVATKG EKLYMRTRNA ASLESAKRSK SVVGSDHWTT IHPLFSDAET EMEIQREKML
     ARIGGYRPQE TIFEVNNRRS GKPENEEALH TIKRVRSTLD SKKKRAQAEE QSELLEDASG
     GNEGEANGNP DAMSDDDIPD GVPDNMSMAS ESDLEVTFSS YSQSKSDKAK KDSTAAFQNP
     EYFMSYTPSS TNLAEDRAYG VHTGTNANFT QASRSVTMDL QLDEGARGFA EPRTMKRWDK
     RHKKYVSRQN DEDGSKGEHL VRGESGAKIA ASFRSGKFDA WKKSKRLGRL PRVGEAEDTS
     LSAGLNSAMG GKRFRHHKDQ APKRADPLRD DFYKKKKKNE AAKERQMSRA GGAAAGGKSE
     IKNTDDIRLA RKLKQKRREK NARPSRKK