CDC28_SCHPO
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 03-AUG-2022, entry version 162.
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; 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; Schizosaccharomycetaceae;
OC 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., Frendewey D.,
RA 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., 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 [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 ATP
CC 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 reaction of
CC pre-mRNA splicing by hydrolyzing ATP to cause the activation of the
CC spliceosome without the occurrence of splicing (By similarity).
CC {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-P8
CC 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 pre-
CC mRNA splicing mutant Prp8-1 exhibits a cell-cycle phenotype identical
CC to cdc28-p8. Prp8-1 mutant produces elongated cells, accumulates U6
CC snRNA precursor and has defects in an early step of TFIID pre-mRNA
CC splicing at the nonpermissive temperature. {ECO:0000269|PubMed:8862522,
CC ECO:0000269|PubMed:9003295}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX16/PRP8 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49377.1; Type=Frameshift; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q10752; -.
DR SMR; Q10752; -.
DR BioGRID; 277230; 15.
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 PomBase; SPBC19C2.01; cdc28.
DR VEuPathDB; FungiDB:SPBC19C2.01; -.
DR eggNOG; KOG0923; Eukaryota.
DR eggNOG; KOG0925; Eukaryota.
DR HOGENOM; CLU_001832_7_0_1; -.
DR InParanoid; Q10752; -.
DR OMA; PHYHKKK; -.
DR PhylomeDB; Q10752; -.
DR PRO; PR:Q10752; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005681; C:spliceosomal complex; IC: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; 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 Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1055
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase-
FT like protein cdc28"
FT /id="PRO_0000055154"
FT DOMAIN 428..592
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 617..790
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 67..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 539..542
FT /note="DEAH box"
FT COMPBIAS 67..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 441..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 760
FT /note="R -> W (in Ref. 1; AAC49377)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="S -> P (in Ref. 1; AAC49377)"
FT /evidence="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
