DBP9_SCHPO
ID DBP9_SCHPO Reviewed; 595 AA.
AC O60080;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ATP-dependent RNA helicase dbp9;
DE EC=3.6.4.13;
GN Name=dbp9; ORFNames=SPCC1494.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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. DDX56/DBP9
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAA19304.1; -; Genomic_DNA.
DR PIR; T41007; T41007.
DR RefSeq; NP_588531.1; NM_001023519.2.
DR AlphaFoldDB; O60080; -.
DR SMR; O60080; -.
DR BioGRID; 275358; 3.
DR STRING; 4896.SPCC1494.06c.1; -.
DR SwissPalm; O60080; -.
DR MaxQB; O60080; -.
DR PaxDb; O60080; -.
DR PRIDE; O60080; -.
DR EnsemblFungi; SPCC1494.06c.1; SPCC1494.06c.1:pep; SPCC1494.06c.
DR GeneID; 2538776; -.
DR KEGG; spo:SPCC1494.06c; -.
DR PomBase; SPCC1494.06c; dbp9.
DR VEuPathDB; FungiDB:SPCC1494.06c; -.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; O60080; -.
DR OMA; GYEKDFK; -.
DR PhylomeDB; O60080; -.
DR PRO; PR:O60080; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0006364; P:rRNA processing; ISO:PomBase.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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..595
FT /note="ATP-dependent RNA helicase dbp9"
FT /id="PRO_0000232345"
FT DOMAIN 45..223
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 233..485
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 574..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..42
FT /note="Q motif"
FT MOTIF 171..174
FT /note="DEAD box"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 595 AA; 67451 MW; 98FB3F42AD5C1F62 CRC64;
MEKSGGIREE SSEKTFSDFN LDPRLQRAIH KCEFEKPTSV QSETIPLALE GKDLVAQART
GSGKTAAYLI PILELLLKQK QIDENQRGIF ALLLVPTREL AQQVYNVLEK LTAFCSKHIR
FINVATNSSD TVQRPLLLDL PDIVIATPSR CVVHVASGVL PLDKLKFLVI DEADLMLSFG
YNEDMKTLSR SLPRGTQSFL MSATLSKNIA SLQKLVCRNP FILAVKDKEA SGKLTQYVVK
CSEQDKFLLA YILLKLRLIK GKILIFVNEI NRCYRLKLFL EQFGLKSLVL NSELPVNSRL
HILEQYNKGL YQIIIATDES GMMGEIEELE NNVDFVEEEV ISTDQPTLDK MKDQENADVN
DESILAAAKD KSKKKKRVKQ DKEYGVARGL DFENVACVLN FDMPSNTKSY IHRIGRTARA
GKPGTAMSFV VPKSEVGKHK PTSLESCKKD ESVLRRLEKK QISLQPYSFD KNQIDAFRYR
MEDALRAVTT VAVSAARAAE LKQELLISEK LKSYFAENPD ELLSLTHDTV SSVRLGHTQR
HLRHVPEYLL PKGMQAVNKD IGFVPFKKNN RRKVFKSRKN PKHRHDPLRS MKRKS
