DBP8_SCHPO
ID DBP8_SCHPO Reviewed; 453 AA.
AC Q9HGM5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATP-dependent RNA helicase dbp8;
DE EC=3.6.4.13;
GN Name=dbp8; ORFNames=SPBC543.06c;
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 40S ribosomal subunit
CC biogenesis and is required for the normal formation of 18S rRNAs
CC through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC vegetative growth (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 box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX49/DBP8
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAC05248.1; -; Genomic_DNA.
DR RefSeq; NP_596794.1; NM_001023814.2.
DR AlphaFoldDB; Q9HGM5; -.
DR SMR; Q9HGM5; -.
DR BioGRID; 277584; 1.
DR STRING; 4896.SPBC543.06c.1; -.
DR MaxQB; Q9HGM5; -.
DR PaxDb; Q9HGM5; -.
DR EnsemblFungi; SPBC543.06c.1; SPBC543.06c.1:pep; SPBC543.06c.
DR GeneID; 2541069; -.
DR KEGG; spo:SPBC543.06c; -.
DR PomBase; SPBC543.06c; dbp8.
DR VEuPathDB; FungiDB:SPBC543.06c; -.
DR eggNOG; KOG0340; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; Q9HGM5; -.
DR OMA; EIKQESM; -.
DR PhylomeDB; Q9HGM5; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q9HGM5; -.
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; ISM:PomBase.
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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..453
FT /note="ATP-dependent RNA helicase dbp8"
FT /id="PRO_0000232291"
FT DOMAIN 38..214
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 230..393
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 413..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..35
FT /note="Q motif"
FT MOTIF 160..163
FT /note="DEAD box"
FT COMPBIAS 413..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 453 AA; 50771 MW; 7DBE88C5DBD45DC7 CRC64;
MSEHTRKSFS DLGISPWLID TLKALAIYEP TDIQEGVIAQ ILEGRNCIGG AKTGSGKTAA
FALPIIEKWS KDPSGIFALI LTPTRELAIQ IDEQFAALGA NLNLKHALIV GGMDMIRQSI
DLSKRPHVVV ATPGRLADLI RSNGEETIAG LRRIKFLVMD EADRLLSPTF ADDLDDCFSV
LPASEDRQTL LFTATVTDAI RQLKYQPQKN NKPPLWLYEV ETDNISVPST LQQSYIFVSS
QVREAYLVHL LTIPENAKKS AIIFVNRTRT AELIYSILRL LELRVTELHS EMVQRERINS
LGRFRAEAAK ILVATDVASR GLDIPSVQLV INFDLPRDPD DYIHRVGRTA RAGRSGESIS
IVTERDVDLV HAIEDRVGTK LSEYEHVSEN KMLEYIKEVT DAKRQASLEM IDRGFGERRQ
KRNEKRLMAN GISNKLKNSG RKKKAKNTLS TEK