GenomeNet

Database: UniProt
Entry: Q10752
LinkDB: Q10752
Original site: Q10752 
ID   CDC28_SCHPO             Reviewed;        1055 AA.
AC   Q10752; Q9URU1; Q9USV9; Q9UUD7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   16-OCT-2019, entry version 150.
DE   RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28;
DE            EC=3.6.4.13;
DE   AltName: Full=Pre-mRNA-processing protein 8;
GN   Name=cdc28; Synonyms=prp8;
GN   ORFNames=SPBC19C2.01, SPBC21B10.01c, SPBC874.01;
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 [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX   PubMed=8862522; DOI=10.1091/mbc.7.7.1083;
RA   Lundgren K., Allan S., Urushiyama S., Tani T., Ohshima Y.,
RA   Frendewey D., Beach D.;
RT   "A connection between pre-mRNA splicing and the cell cycle in fission
RT   yeast: cdc28+ is allelic with prp8+ and encodes an RNA-dependent
RT   ATPase/helicase.";
RL   Mol. Biol. Cell 7:1083-1094(1996).
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.,
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).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9003295; DOI=10.1007/s004380050304;
RA   Urushiyama S., Tani T., Ohshima Y.;
RT   "Isolation of novel pre-mRNA splicing mutants of Schizosaccharomyces
RT   pombe.";
RL   Mol. Gen. Genet. 253:118-127(1996).
CC   -!- FUNCTION: Involved in pre-mRNA splicing. Is required together with
CC       ATP and at least one other factor, for the first cleavage-ligation
CC       reaction. Functions as a molecular motor in the activation of the
CC       precatalytic spliceosome for the first transesterification
CC       reaction of pre-mRNA splicing by hydrolyzing ATP to cause the
CC       activation of the spliceosome without the occurrence of splicing
CC       (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 {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells show pre-mRNA splicing defects. Cdc28-
CC       P8 temperature-sensitive mutant causes cell-cycle arrest in G2 and
CC       exhibits a splicing defect that leads to accumulation of unspliced
CC       precursors at the restrictive temperature. Temperature-sensitive
CC       pre-mRNA splicing mutant Prp8-1 exhibits a cell-cycle phenotype
CC       identical to cdc28-p8. Prp8-1 mutant produces elongated cells,
CC       accumulates U6 snRNA precursor and has defects in an early step of
CC       TFIID pre-mRNA splicing at the nonpermissive temperature.
CC       {ECO:0000269|PubMed:8862522, ECO:0000269|PubMed:9003295}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. DDX16/PRP8 sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49377.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; U48733; AAC49377.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CU329671; CAB57929.2; -; Genomic_DNA.
DR   PIR; T46568; T46568.
DR   PIR; T50372; T50372.
DR   RefSeq; NP_595686.2; NM_001021581.3.
DR   SMR; Q10752; -.
DR   BioGrid; 277230; 14.
DR   STRING; 4896.SPBC19C2.01.1; -.
DR   iPTMnet; Q10752; -.
DR   MaxQB; Q10752; -.
DR   PaxDb; Q10752; -.
DR   PRIDE; Q10752; -.
DR   EnsemblFungi; SPBC19C2.01.1; SPBC19C2.01.1:pep; SPBC19C2.01.
DR   GeneID; 2540707; -.
DR   KEGG; spo:SPBC19C2.01; -.
DR   EuPathDB; FungiDB:SPBC19C2.01; -.
DR   PomBase; SPBC19C2.01; cdc28.
DR   HOGENOM; HOG000175261; -.
DR   InParanoid; Q10752; -.
DR   KO; K12813; -.
DR   OMA; VYNQWVE; -.
DR   PhylomeDB; Q10752; -.
DR   Reactome; R-SPO-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q10752; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
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; TAS:PomBase.
DR   GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; ISO:PomBase.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1055       Pre-mRNA-splicing factor ATP-dependent
FT                                RNA helicase-like protein cdc28.
FT                                /FTId=PRO_0000055154.
FT   DOMAIN      428    592       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      617    790       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     441    448       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       539    542       DEAH box.
FT   CONFLICT    760    760       R -> W (in Ref. 1; AAC49377).
FT                                {ECO:0000305}.
FT   CONFLICT    969    969       S -> P (in Ref. 1; AAC49377).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1055 AA;  121217 MW;  223694BD85404DCC CRC64;
     MSLEQYVSDK AISLLGMSEP SVVEYLIAEA KGSSSSNNLY QKLVSFGMDG DDPAVKEFAH
     TLYARIPREG SRPKENYNAR KKKEQGILQM ERLNSSYDLL IEPQSHETPG KPLKKKSRSK
     TPKREIARRQ RDEDEWESDE YEEVVDGSAS HPIEEDSVST DFQNHDYEKS SDPETERLND
     LREREEFEER LRRKDLEAAT NEFVEDYSSK FSSEELALRK LADDPESWRK LASELRKKSR
     QQYLKPRAQQ QLEILRREIR DEEQLFAGEK LTQAEIRELE KKKELLRIAE ERQRLEKQAT
     EYQMPEDYFT EQGKLDRKRK EEVLYQRYKD SNEGEQNEVT MGAAEQQRWE AQQINKALLF
     DQNEWLPPGE KQFDFVFDES QQIDFLLDTK LSAENPVDTD KMTDVKVEKS LESSRKSLPV
     YQYKDDLLKA INEYQVLLIV AETGSGKTTQ LPQFLHEAGY TKGNKKICCT QPRRVAAMSV
     AARVAKEMDV RLGQEVGYSI RFENATSEKT VIKYLTDGML LREFLTEPDL ASYSVIIIDE
     AHERTLHTDI LFGLVKDIAR FRPDLKVLIS SATIDAEKFS AYFDEAPVFY VPGRRYPVDI
     YYTPQPEANY IQAAITTILQ IHTTQPAGDI LVFLTGQDEI ELMSENMQEL CRILGKRIPE
     IILCPIYANL PSELQAKIFD PTPPGARKVV LATNIAETSI TIDGVNFVID SGFVKQNMYN
     PRTGMESLVS VPCSRASADQ RAGRAGRVGP GKCFRLYTRR TYNNELDMVT SPEIQRTNLT
     NIVLLLKSLG INNLLDFDFM DAPPPETLMR SLELLYALGA LNNRGELTKL GRQMAEFPTD
     PMLSKSLIAS SKYGCVEEVL SIVSMLGEAS SLFYRPKDKI MEADKARANF TQPGGDHLTL
     LHIWNEWVDT DFSYNWAREN FLQYKSLCRA RDVRDQLANL CERVEIELVT NSSESLDPIK
     KAITAGYFSN AARLDRSGDS YRTVKSNQTV YIHPSSSVAE KKPKVIIYFE LVLTTKEYCR
     QITEIQPEWL LEISPHYFKP ENIEELQKTQ KRHKR
//
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