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Database: UniProt
Entry: Q10202
LinkDB: Q10202
Original site: Q10202 
ID   DBP3_SCHPO              Reviewed;         578 AA.
AC   Q10202;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-OCT-2019, entry version 135.
DE   RecName: Full=ATP-dependent RNA helicase dbp3;
DE            EC=3.6.4.13;
GN   Name=dbp3; ORFNames=SPBC17D1.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for 60S ribosomal
CC       subunit synthesis. Involved in efficient pre-rRNA processing,
CC       predominantly at site A3, which is necessary for the normal
CC       formation of 25S and 5.8S rRNAs (By similarity). {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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
DR   EMBL; CU329671; CAA20430.1; -; Genomic_DNA.
DR   PIR; T39709; S67386.
DR   RefSeq; NP_596388.1; NM_001022309.2.
DR   SMR; Q10202; -.
DR   BioGrid; 276746; 14.
DR   STRING; 4896.SPBC17D1.06.1; -.
DR   iPTMnet; Q10202; -.
DR   SwissPalm; Q10202; -.
DR   MaxQB; Q10202; -.
DR   PaxDb; Q10202; -.
DR   PRIDE; Q10202; -.
DR   EnsemblFungi; SPBC17D1.06.1; SPBC17D1.06.1:pep; SPBC17D1.06.
DR   GeneID; 2540213; -.
DR   KEGG; spo:SPBC17D1.06; -.
DR   EuPathDB; FungiDB:SPBC17D1.06; -.
DR   PomBase; SPBC17D1.06; dbp3.
DR   HOGENOM; HOG000268804; -.
DR   InParanoid; Q10202; -.
DR   KO; K14811; -.
DR   OMA; AYGAFFK; -.
DR   PhylomeDB; Q10202; -.
DR   PRO; PR:Q10202; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR   GO; GO:0006364; P:rRNA processing; ISO:PomBase.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    578       ATP-dependent RNA helicase dbp3.
FT                                /FTId=PRO_0000055088.
FT   DOMAIN      196    373       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      402    550       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     209    216       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       167    193       Q motif.
FT   MOTIF       316    319       DEAD box.
SQ   SEQUENCE   578 AA;  63912 MW;  0A84EC77ECCC29FD CRC64;
     MQFCFRILIL YISLSIDNNY LVTTLISLKE NVFLHIFTLT FLFKAFLLKM AKRSVEELKR
     SADEEASVKR KEKKSKHEHK KHKKDKPSAD KDRISKKDKK KSKKGKSKTK EESIEINAEE
     GAKIAQPAIG SANASNHNDE EAYDRYIKKH NISFADPKSS ENLLPILQFD ELDVSAKLRE
     GLKNYKEPTP IQAATWPYLL AGRDVVGIAE TGSGKTVAFG IPALQYLNGL SDNKSVPRVL
     VVSPTRELAI QTYENLNSLI QGTNLKAVVV YGGAPKSEQA RAAKNASVII GTPGRLLDLI
     NDGSIDCSQV GYLVLDEADR MLDTGFEQDI RNIISHTPDP TRNGSRQTVF FSATWPESVR
     ALAATFLKDP VKITIGSDEL AASQNITQIV EILDDPRSKE RMLDNLLRKH LSSGGKDDKI
     LIFVLYKKEA ARVEGTLARK YNVVGIHGDM SQGARLQALN DFKSGKCPVL VATDVAARGL
     DIPKVQLVIN VTFPLTIEDY VHRIGRTGRA NTKGTAITFF TPQDKSHAGE LVNVLRQAKQ
     DIPEGLFKFG TAVKPKLNAY GSRVVDVPVK AATKIVFD
//
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