DBP7_SCHPO
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 03-AUG-2022, entry version 135.
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; 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 -!- 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; CU329671; CAA18864.1; -; Genomic_DNA.
DR PIR; T39930; T39930.
DR RefSeq; NP_595929.1; NM_001021837.2.
DR AlphaFoldDB; O60173; -.
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 PomBase; SPBC21H7.04; dbp7.
DR VEuPathDB; FungiDB:SPBC21H7.04; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; O60173; -.
DR OMA; QMGFERW; -.
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: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:0042254; P:ribosome biogenesis; IBA:GO_Central.
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; 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..709
FT /note="ATP-dependent RNA helicase dbp7"
FT /id="PRO_0000232259"
FT DOMAIN 172..366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 404..580
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 13..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 138..167
FT /note="Q motif"
FT MOTIF 301..304
FT /note="DEAD box"
FT COMPBIAS 20..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
