ID   DBP7_NEOFI              Reviewed;         758 AA.
AC   A1DE84;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-dependent RNA helicase dbp7;
DE            EC=3.6.4.13;
GN   Name=dbp7; ORFNames=NFIA_076210;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW17691.1; -; Genomic_DNA.
DR   RefSeq; XP_001259588.1; XM_001259587.1.
DR   AlphaFoldDB; A1DE84; -.
DR   SMR; A1DE84; -.
DR   STRING; 36630.CADNFIAP00007501; -.
DR   EnsemblFungi; EAW17691; EAW17691; NFIA_076210.
DR   GeneID; 4586305; -.
DR   KEGG; nfi:NFIA_076210; -.
DR   VEuPathDB; FungiDB:NFIA_076210; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   HOGENOM; CLU_003041_26_2_1; -.
DR   OMA; AVHIKAD; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000006702; 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: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..758
FT                   /note="ATP-dependent RNA helicase dbp7"
FT                   /id="PRO_0000281709"
FT   DOMAIN          171..372
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          398..603
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          26..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           138..167
FT                   /note="Q motif"
FT   MOTIF           308..311
FT                   /note="DEAD box"
FT   COMPBIAS        44..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..723
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         184..191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   758 AA;  83538 MW;  696DE784DFAB1694 CRC64;
     MADDGLLLNF SLGDNNIIQP ETKLKGGTWR DRLSAKKIAK HHAKGPRTAG DEDSTPRAPR
     NPNRIEVPSS RPTKRQRTDG GDSGKQQSHT HPHSNQPRQF ISSLFTKNPE PQKVEEVKEE
     GHVEDAKPTN APLIDGLDTF TNLGLSPSLA AHLLTKLELK APTAIQKASI SQLLKEEGDA
     FIQAETGSGK TLAYLLPLVQ RIMALSKPGA QTDAKGQPIV HRDSGLFAIV LAPTRELCKQ
     ISVVLENLLR CAHWIVAGTV IGGEKKKSEK ARLRKGLNIL VATPGRLADH LDNTQALDVS
     NVRWLVLDEG DRLMELGFEE EIQGIVKKLD ARQRPSRIPG VPTRRTTILC SATLKMSVQK
     LGEISLKDAV HIKADPEDED EKARRSKEEE SAYRVPAQLK QSYAVVAAKL RLVTLTAFFK
     RTFMRKGSVM KAIIFVSCAD SVDFHFEVFT RKQAKEDGDE SSDTDKSEDK PPSSPHGTIA
     PATAFSNPSN PVTLFRLHGS LPQNVRTSTL GAFAKNKEAS VLICTDVASR GLDLPNVDLV
     VEYDPAFSAE DHLHRIGRTA RVGRDGRALI FLQPGCEENY VEVLKRGYRD GGKALTRADA
     NDILKRGFGG NVESGNKDWE TKATDWQCEI ERWALENPEY LEMARRAFQS HIRAYATHIA
     AERSMFNIKE LHLGHLAKAF ALRDRPSKIN VPGLRQGKEE TKKDFKAERN SAAGKKRKAG
     GTDLADDIPS ANNTATAAQK MRAKMKEHIS GANEFNLA