CDS1_SCHPO
ID CDS1_SCHPO Reviewed; 460 AA.
AC Q09170; O42642;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Serine/threonine-protein kinase cds1;
DE EC=2.7.11.1;
DE AltName: Full=Checkpoint kinase cds1;
GN Name=cds1; ORFNames=SPCC18B5.11c;
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 [MRNA], AND FUNCTION.
RX PubMed=7723827; DOI=10.1038/374817a0;
RA Murakami H., Okayama H.;
RT "A kinase from fission yeast responsible for blocking mitosis in S phase.";
RL Nature 374:817-819(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RAD26, AND
RP PHOSPHORYLATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9450932; DOI=10.1101/gad.12.3.382;
RA Lindsay H.D., Griffiths D.J.F., Edwards R.J., Christensen P.U.,
RA Murray J.M., Osman F., Walworth N., Carr A.M.;
RT "S-phase-specific activation of Cds1 kinase defines a subpathway of the
RT checkpoint response in Schizosaccharomyces pombe.";
RL Genes Dev. 12:382-395(1998).
RN [3]
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 [4]
RP FUNCTION IN PHOSPHORYLATION OF RAD60.
RX PubMed=12897162; DOI=10.1128/mcb.23.16.5939-5946.2003;
RA Boddy M.N., Shanahan P., McDonald W.H., Lopez-Girona A., Noguchi E.,
RA Yates J.R. III, Russell P.;
RT "Replication checkpoint kinase Cds1 regulates recombinational repair
RT protein Rad60.";
RL Mol. Cell. Biol. 23:5939-5946(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-443, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [6]
RP FUNCTION.
RX PubMed=22682245; DOI=10.1016/j.cell.2012.04.030;
RA Hu J., Sun L., Shen F., Chen Y., Hua Y., Liu Y., Zhang M., Hu Y., Wang Q.,
RA Xu W., Sun F., Ji J., Murray J.M., Carr A.M., Kong D.;
RT "The intra-s phase checkpoint targets dna2 to prevent stalled replication
RT forks from reversing.";
RL Cell 149:1221-1232(2012).
CC -!- FUNCTION: Has a role in the DNA replication-monitoring S/G2 checkpoint
CC system. It is responsible for blocking mitosis in the S phase. It
CC monitors DNA synthesis by interacting with DNA polymerase alpha and
CC sends a signal to block the onset of mitosis while DNA synthesis is in
CC progress. Phosphorylates rad60 and dna2. {ECO:0000269|PubMed:12897162,
CC ECO:0000269|PubMed:22682245, ECO:0000269|PubMed:7723827,
CC ECO:0000269|PubMed:9450932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with rad26. {ECO:0000269|PubMed:9450932}.
CC -!- INTERACTION:
CC Q09170; O42913: nrm1; NbExp=2; IntAct=EBI-3650524, EBI-15720278;
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:18257517,
CC ECO:0000269|PubMed:9450932}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily. {ECO:0000305}.
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DR EMBL; X85040; CAA59410.1; -; mRNA.
DR EMBL; AJ222869; CAA11019.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB52158.1; -; Genomic_DNA.
DR PIR; S58882; S58882.
DR RefSeq; NP_587941.1; NM_001022932.2.
DR AlphaFoldDB; Q09170; -.
DR SMR; Q09170; -.
DR BioGRID; 275533; 122.
DR DIP; DIP-46174N; -.
DR IntAct; Q09170; 2.
DR STRING; 4896.SPCC18B5.11c.1; -.
DR iPTMnet; Q09170; -.
DR MaxQB; Q09170; -.
DR PaxDb; Q09170; -.
DR PRIDE; Q09170; -.
DR EnsemblFungi; SPCC18B5.11c.1; SPCC18B5.11c.1:pep; SPCC18B5.11c.
DR GeneID; 2538959; -.
DR KEGG; spo:SPCC18B5.11c; -.
DR PomBase; SPCC18B5.11c; cds1.
DR VEuPathDB; FungiDB:SPCC18B5.11c; -.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_000288_63_47_1; -.
DR InParanoid; Q09170; -.
DR OMA; FLHDHSS; -.
DR PhylomeDB; Q09170; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:Q09170; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0033315; P:meiotic G2/MI DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1903466; P:regulation of mitotic DNA replication initiation; IMP:PomBase.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..460
FT /note="Serine/threonine-protein kinase cds1"
FT /id="PRO_0000085846"
FT DOMAIN 60..116
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 167..433
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 438..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 173..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 61
FT /note="R -> G (in Ref. 1; CAA59410)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="F -> C (in Ref. 1; CAA59410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 52014 MW; 4CEB963D3376DB54 CRC64;
MEEPEEATQA TQEAPLHVSQ NIAKQVVNNE NVFMKLVMTR MLDGKTEVIP LTTDVHNGFW
RFGRHKSCEV VLNGPRVSNF HFEIYQGHRN DSDESENVVF LHDHSSNGTF LNFERLAKNS
RTILSNGDEI RIGLGVPKDE ISFLCQVPVK HSRDSQKNMI KSENSHYEII RTLGSGTFAV
VKLAVEVNSG KWYAIKIINK RKILLTSSEK RATEMFQREI DILKSLHHPG VVQCHEIFEN
DDELFIVMEY VEGGDLMDFL IANGSIDEQD CKPLLKQLLE TLLHLHKQGV THRDIKPENI
LITNDFHLKI SDFGLAKVIH GTGTFLETFC GTMGYLAPEV LKSKNVNLDG GYDDKVDIWS
LGCVLYVMLT ASIPFASSSQ AKCIELISKG AYPIEPLLEN EISEEGIDLI NRMLEINPEK
RISESEALQH PWFYTVSTHE HRTPPSSSEH EATEQLNSSS
