DBP2_SCHPO
ID DBP2_SCHPO Reviewed; 550 AA.
AC P24782;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ATP-dependent RNA helicase dbp2;
DE EC=3.6.4.13;
DE AltName: Full=p68-like protein;
GN Name=dbp2; ORFNames=SPBP8B7.16c;
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 [GENOMIC DNA / MRNA].
RX PubMed=1996094; DOI=10.1128/mcb.11.3.1326-1333.1991;
RA Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J.,
RA Lane D.P.;
RT "p68 RNA helicase: identification of a nucleolar form and cloning of
RT related genes containing a conserved intron in yeasts.";
RL Mol. Cell. Biol. 11:1326-1333(1991).
RN [2]
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-dependent RNA helicase involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing. {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: Associates with polysomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; X52648; CAA36873.1; -; Genomic_DNA.
DR EMBL; L11574; AAA35319.1; -; mRNA.
DR EMBL; CU329671; CAA21801.1; -; Genomic_DNA.
DR PIR; T40810; S14048.
DR RefSeq; NP_596523.1; NM_001022444.2.
DR AlphaFoldDB; P24782; -.
DR SMR; P24782; -.
DR BioGRID; 277894; 9.
DR IntAct; P24782; 1.
DR STRING; 4896.SPBP8B7.16c.1; -.
DR iPTMnet; P24782; -.
DR MaxQB; P24782; -.
DR PaxDb; P24782; -.
DR PRIDE; P24782; -.
DR EnsemblFungi; SPBP8B7.16c.1; SPBP8B7.16c.1:pep; SPBP8B7.16c.
DR GeneID; 2541383; -.
DR KEGG; spo:SPBP8B7.16c; -.
DR PomBase; SPBP8B7.16c; dbp2.
DR VEuPathDB; FungiDB:SPBP8B7.16c; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_16_9_1; -.
DR InParanoid; P24782; -.
DR OMA; STMPKFE; -.
DR PhylomeDB; P24782; -.
DR Reactome; R-SPO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P24782; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:PomBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..550
FT /note="ATP-dependent RNA helicase dbp2"
FT /id="PRO_0000054998"
FT DOMAIN 153..328
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 340..503
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..533
FT /note="RNA-binding RGG-box"
FT REGION 525..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 122..150
FT /note="Q motif"
FT MOTIF 276..279
FT /note="DEAD box"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 235
FT /note="R -> L (in Ref. 1; CAA36873)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> L (in Ref. 1; CAA36873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 61548 MW; 3BD1636D14275451 CRC64;
MSYRDNEYSG NYNGKEDGYN SRGRYGGGYR NNYSRGGGRG GFNDGASYGY DQRGQGRNFY
ESDGPGANLV KKDWKNETLI PFQKDFYKEH ENVRNRSDAE VTEYRKEKEI VVHGLNVPKP
VTTFEEAGFP NYVLKEVKQL GFEAPTPIQQ QAWPMAMSGR DMVGISATGS GKTLSYCLPA
IVHINAQPLL SPGDGPIVLV LAPTRELAVQ IQQECTKFGK SSRIRNTCVY GGVPRGPQIR
DLIRGVEICI ATPGRLLDML DSNKTNLRRV TYLVLDEADR MLDMGFEPQI RKIVDQIRPD
RQTVMFSATW PKEVQRLARD YLNDYIQVTV GSLDLAASHN IKQIVEVVDN ADKRARLGKD
IEEVLKDRDN KVLIFTGTKR VADDITRFLR QDGWPALAIH GDKAQDERDW VLNEFRTGKS
PIMVATDVAS RGIDVKGITH VFNYDFPGNT EDYVHRIGRT GRAGAKGTAY TYFTSDNAKQ
ARELVSILSE AKQDIDPKLE EMARYSSGGR GGNYRRGGYG RGGFRRGGGY GNRNRGFTGS
NSAPLARSRW
