DBP6_SCHPO
ID DBP6_SCHPO Reviewed; 604 AA.
AC Q76PD3; O74491; P78908;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ATP-dependent RNA helicase dbp6;
DE EC=3.6.4.13;
GN Name=dbp6; ORFNames=SPCC285.03;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-604.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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 -!- SUBUNIT: Associated with pre-ribosomal particles. {ECO:0000250}.
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. DDX51/DBP6
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA20842.1; -; Genomic_DNA.
DR EMBL; D89259; BAA13920.1; -; mRNA.
DR PIR; T41249; T41249.
DR PIR; T43184; T43184.
DR RefSeq; NP_588332.1; NM_001023323.2.
DR AlphaFoldDB; Q76PD3; -.
DR SMR; Q76PD3; -.
DR BioGRID; 275390; 1.
DR STRING; 4896.SPCC285.03.1; -.
DR iPTMnet; Q76PD3; -.
DR MaxQB; Q76PD3; -.
DR PaxDb; Q76PD3; -.
DR PRIDE; Q76PD3; -.
DR EnsemblFungi; SPCC285.03.1; SPCC285.03.1:pep; SPCC285.03.
DR GeneID; 2538809; -.
DR KEGG; spo:SPCC285.03; -.
DR PomBase; SPCC285.03; dbp6.
DR VEuPathDB; FungiDB:SPCC285.03; -.
DR eggNOG; KOG0350; Eukaryota.
DR HOGENOM; CLU_003041_15_3_1; -.
DR InParanoid; Q76PD3; -.
DR OMA; TEQYCVT; -.
DR PhylomeDB; Q76PD3; -.
DR PRO; PR:Q76PD3; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; ISO: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: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 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 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..604
FT /note="ATP-dependent RNA helicase dbp6"
FT /id="PRO_0000232296"
FT DOMAIN 167..379
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 406..573
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 149..157
FT /note="Q motif"
FT MOTIF 292..295
FT /note="DEAD box"
FT COMPBIAS 22..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 120
FT /note="V -> F (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="N -> Y (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="F -> L (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="R -> W (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 502..504
FT /note="DVA -> HFS (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="L -> F (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="R -> P (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 557..558
FT /note="RR -> KK (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 578..579
FT /note="VA -> FP (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="V -> L (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="Y -> C (in Ref. 2; BAA13920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 68345 MW; 099005F2FD2CCD03 CRC64;
MSVEVDKSSH SKPKIEKKSK RNKRKWLNDE NKTHVTASEA AIERLKKSAS FSQAAQQALK
QSRKEDNERD IEMQDVDAEA QPHDLLPIPQ PSVEDFVDSK PHVKNITSVL PKWLAEPITV
DPNTTVEFSS LNISSKLVER LQKQNITRGF AVQAAVLPLL LQDGRHGPMY SYGGDVCVSA
ATGSGKTLSY VIPIVQCLSH RTVPRLRCVV IVPTRELTVQ VAKTFEYYMS GAGLQVCAWT
GQKSLRHETY QLNGDENECR IDVLVSTPGR LVDHIRNDES FSLQHLRYMV IDEADRLLDQ
SFQDWVDTVM MEISHPKCLQ NKSNILDLDQ NISPTFLPDI DTLLPYRLPS PLQKLVFSAT
LTRDPSKIAS LKLHNPRLVL VQNKDMEVDD GGEIEDDAIV FSVPPTLQEY HVSVSSEKPI
LLYHLIHSKN LTNILCFVKS NEAAARLHRL LELIHESLNQ SFSCGLFTSS LSRDERKKII
SRFATGDLNL LVCSDLMARG IDVANTQNVI NYDPPLSVRS YVHRIGRTAR AGREGFAWTL
VQSHEGHHFS KLVKQLRRTL PIKRIKIEFS HISEEFVVAY DKALEALRVE VFNSRYPQQK
SFLT
