ID   DBP10_ASPFU             Reviewed;         869 AA.
AC   Q8NJM2; Q4WM56;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=ATP-dependent RNA helicase dbp10;
DE            EC=3.6.4.13;
GN   Name=dbp10; ORFNames=AfA12H2.09c, AFUA_6G11120;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RA   Harris D.E., O'Neil S., Knowles D.G., Hall N., Quail M.A., Woodward J.R.,
RA   Denning D.W., Anderson M.J., Barrell B.G.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL807577; CAD37147.1; -; Genomic_DNA.
DR   EMBL; AAHF01000006; EAL88958.1; -; Genomic_DNA.
DR   RefSeq; XP_750996.1; XM_745903.1.
DR   AlphaFoldDB; Q8NJM2; -.
DR   SMR; Q8NJM2; -.
DR   STRING; 746128.CADAFUBP00007518; -.
DR   EnsemblFungi; EAL88958; EAL88958; AFUA_6G11120.
DR   GeneID; 3508301; -.
DR   KEGG; afm:AFUA_6G11120; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   InParanoid; Q8NJM2; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; IBA:GO_Central.
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..869
FT                   /note="ATP-dependent RNA helicase dbp10"
FT                   /id="PRO_0000232309"
FT   DOMAIN          101..273
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          341..495
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           70..98
FT                   /note="Q motif"
FT   MOTIF           221..224
FT                   /note="DEAD box"
FT   COMPBIAS        319..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..869
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         114..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   869 AA;  96324 MW;  7D8BCD712316391F CRC64;
     MPHRAASPAV SENEFDITGA LFQNDSDSDN EQPSAKSKRQ PPKKAFIAEQ QTSANRKASN
     LKGRTVKKGG GFQAMGLSAN LLKAIARKGF SVPTPIQRKT IPVIMDDQDV VGMARTGSGK
     TAAFVIPMIE KLKSHSTKVG ARGLVLSPSR ELALQTLKVV KELGRGTDLK SVLLVGGDSL
     EEQFAMIAGN PDIIIATPGR FLHLKVEMNL DLSSIRYVVF DEADRLFEMG FAAQLTEILH
     GLPANRQTLL FSATLPKSLV EFARAGLQEP TLVRLDTESK ISPDLQNAFF SVKSSEKEGA
     LLYILHEVIK MPTGPTEVSQ QRKEEDASAK NLKNKKRKRA EMEKAVNTRE SPTKHSTIVF
     AATKHHVDYL YSLLCEAGFA VSYVYGSLDQ TARKIQVQNF RTGMTNILVV TDVAARGIDI
     PILANVINYD FPSQPKIFVH RVGRTARAGR KGWSYSLVRD ADAPYLLDLQ LFLGRRLVVG
     REFGDQVNFA EDVVTGSLPR DGLSQSCEWV TKVLDDNADL AAQRTVAAKG EKLYMRTRNA
     ASLESAKRSK QVVSSDNWTS VHPLFQDETS NLEAEREKML ARIGGYRPPE TIFEVNNRRM
     GKHENVDALD TIKRVRSTLE SKKKPFSDED DDVPTGVADN MSMASDSELE VTFSSYSKSK
     DNKAKKASAA SFQNPEYFMS YTPNNTSLAE DRAYGVHSGT NSNFAQASRS ATMDLAGDDG
     GRGFGEARTL MRWDKRHKKY VARQNDEDGS KGTRLVRGES GAKIAASFRS GRFDAWKREN
     RLGRLPRVAI SGKRFRHRKE QAPKKADPLR GDYEKMKKKA ELAKERAMSK AGGAAPRGKS
     ELKSTDDIRI ARKLKQKRRE KNARPSRKK