ID DBP10_NEUCR Reviewed; 934 AA.
AC Q7S9J4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 126.
DE RecName: Full=ATP-dependent RNA helicase dbp-10;
DE EC=3.6.4.13;
GN Name=dbp-10; ORFNames=NCU07712;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002239; EAA33062.1; -; Genomic_DNA.
DR RefSeq; XP_962298.1; XM_957205.2.
DR AlphaFoldDB; Q7S9J4; -.
DR SMR; Q7S9J4; -.
DR STRING; 367110.Q7S9J4; -.
DR PaxDb; 5141-EFNCRP00000008050; -.
DR EnsemblFungi; EAA33062; EAA33062; NCU07712.
DR GeneID; 3878446; -.
DR KEGG; ncr:NCU07712; -.
DR VEuPathDB; FungiDB:NCU07712; -.
DR HOGENOM; CLU_003041_5_2_1; -.
DR InParanoid; Q7S9J4; -.
DR OMA; EDQFGMM; -.
DR OrthoDB; 5475716at2759; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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 CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 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; P-loop containing nucleoside triphosphate hydrolases; 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..934
FT /note="ATP-dependent RNA helicase dbp-10"
FT /id="PRO_0000232318"
FT DOMAIN 130..302
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 359..513
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 21..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..127
FT /note="Q motif"
FT MOTIF 250..253
FT /note="DEAD box"
FT COMPBIAS 346..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..697
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 934 AA; 103653 MW; E010C55016EFAB98 CRC64;
MPRRAASPTP SENEVDIAGA LFNNDSDFED NSSKHHTKKG AVTNSGLDLD FNDLLGNGDD
GLPSFNGEGD DDEAFIASLT RSSQRKSSNI QGKSVKKGGG FQAMGLNAHL LRAITRKGFS
VPTPIQRKAI PLILERKDVV GMARTGSGKT AAFVIPMIER LKGHSPRVGS RALIMSPSRE
LALQTLKVVK ELGRGTDLKT VLLVGGDSLE EQFGMMASNP DIIIATPGRF LHLKVEMNLS
LASIKYVVFD EADRLFEMGF ATELTEILHA LPPSRQTLLF SATLPSSLVE FARAGLQEPS
LVRLDAETKV SPDLESAFFA VKGGEKEGAL LHLLHDVIKV PLGPPEGTKE ESDELQARKR
KREYRPNPKE KPTEYSTIIF TATKHHVEYI ANLLKLAGFA VSYVYGSLDQ TARLIQVDNF
RRGRTHILVV TDVAARGIDM PALANVINYD FPSQPKIFVH RVGRTARAGQ RGWAYGLVRQ
SDVPYLLDLQ LFLGRKLIIG HDQKNPSFAA DVVVGTLKRD GVDVNIEWVE KALKESADLK
ALKGVAAKAE KLYMKTRNSA SSQSAKRARE VTQSRGWTQL HPLFGEEAAE AQAARDDLLS
RINRFKPQET IFELGPKGKS SRNKAAEVVR NMRSRFKERK TTNDEDDEDV DMEDAEGKPD
GEETNAFEDF EDEEEEGEAE EAEEAEAKED PYADDSDSEM EVTVSSSMHT KKKGGPVNFQ
DPEIFMSYTP RTTSLAEEKA YGVHSGGYSG NSFVEAARDA TMDLTNDESA KNFGLPTKSK
MRWDKRHSKY VAVANDEDGS KGAKMIRGES GVKIAASFKS GRFDRWRKDN RLGKLPTIGE
TEKSQLIRNF GAQPGQPRYK HKMEKAPKDA DKFRDDYHVR KKRVAEAKEK RIGKYKDGEG
SKRELKTATD IRKARAVAEK KREKNARPAK RQKR
//
