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Database: UniProt
Entry: O60173
LinkDB: O60173
Original site: O60173 
ID   DBP7_SCHPO              Reviewed;         709 AA.
AC   O60173;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   13-NOV-2019, entry version 123.
DE   RecName: Full=ATP-dependent RNA helicase dbp7;
DE            EC=3.6.4.13;
GN   Name=dbp7; ORFNames=SPBC21H7.04;
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-binding RNA helicase involved in the biogenesis of
CC       60S ribosomal subunits and is required for the normal formation of
CC       25S and 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
DR   EMBL; CU329671; CAA18864.1; -; Genomic_DNA.
DR   PIR; T39930; T39930.
DR   RefSeq; NP_595929.1; NM_001021837.2.
DR   SMR; O60173; -.
DR   BioGrid; 277046; 3.
DR   STRING; 4896.SPBC21H7.04.1; -.
DR   iPTMnet; O60173; -.
DR   MaxQB; O60173; -.
DR   PaxDb; O60173; -.
DR   PRIDE; O60173; -.
DR   EnsemblFungi; SPBC21H7.04.1; SPBC21H7.04.1:pep; SPBC21H7.04.
DR   GeneID; 2540518; -.
DR   KEGG; spo:SPBC21H7.04; -.
DR   EuPathDB; FungiDB:SPBC21H7.04; -.
DR   PomBase; SPBC21H7.04; dbp7.
DR   HOGENOM; HOG000268799; -.
DR   InParanoid; O60173; -.
DR   KO; K14806; -.
DR   OMA; FSRIQWL; -.
DR   PhylomeDB; O60173; -.
DR   PRO; PR:O60173; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR025313; DUF4217.
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; 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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    709       ATP-dependent RNA helicase dbp7.
FT                                /FTId=PRO_0000232259.
FT   DOMAIN      172    366       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      404    580       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     185    192       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       138    167       Q motif.
FT   MOTIF       301    304       DEAD box.
SQ   SEQUENCE   709 AA;  78831 MW;  E9E91C1DF92F51AD CRC64;
     MADEPLLLNF VVDNAQSRKP EALKSSRRWT DRARDRKRQK RNSNESSKST VKRNSGTNGA
     STDYKNSQKE KVINPVFDPR KPAHELKGNK RDNTFVTSLF TGDDSEHFSQ DVGQNLEDNQ
     ISNIGTTKEA SNAPIKTTNF AGVQLDTQLA DHLNNKMNIS APTAIQSCCL PALLNTDDKD
     AFIEAQTGSG KTLAYLLPIV QRLIRLPKNL HTRTSGIYAV IMAPTRELCQ QIYNVANKLN
     NNPLSHWIVS CNVIGGEKKK SEKARIRKGV NILIGTPGRL ADHLENTEAL DVSQVRWVVL
     DEGDRLMDMG FEETLTKILS YLESQSSIIK KDLSIPSRKV TMLCSATMKD TVKRLSDSAL
     KDALYLKSSI VEETNDGYSQ APEQLLQRYV VVPPKLRLVS LVALLRSHVR SYKKIIIFLS
     CSDSVDFHFE AFRCAINADE MEEAVKEKPD SEGDIISNAP ALRIDGKSNV YRLHGSLSQQ
     IRTSTLNLFS SSEDSGSHIL LCTDVAARGL DLPNVDLVVQ YDAPFSTDDY LHRIGRTARA
     GHNGAAIMFL LPKESEYINL LKSSVSANIL EQPNGPSGLL SAGFSQGKTN TNDWQDRATE
     WQLELERFIL ENEPMRNIAK RAFTSYVRAY ATHLSSERSI FNMRDLHLGH IAKSFALREA
     PGKISGANSS KPRKQGGSVD KGKSKSSKDI AALMHRKAME HYSTEHNIG
//
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