ID CSK1_SCHPO Reviewed; 306 AA.
AC P36615;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Serine/threonine-protein kinase csk1;
DE EC=2.7.11.22;
DE AltName: Full=CAK-activating kinase;
DE Short=CAKAK;
GN Name=csk1; ORFNames=SPAC1D4.06c;
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].
RX PubMed=8467814; DOI=10.1002/j.1460-2075.1993.tb05817.x;
RA Molz L., Beach D.;
RT "Characterization of the fission yeast mcs2 cyclin and its associated
RT protein kinase activity.";
RL EMBO J. 12:1723-1732(1993).
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 FUNCTION.
RX PubMed=9857180; DOI=10.1093/emboj/17.24.7230;
RA Hermand D., Pihlak A., Westerling T., Damagnez V., Vandenhaute J.,
RA Cottarel G., Makela T.P.;
RT "Fission yeast Csk1 is a CAK-activating kinase (CAKAK).";
RL EMBO J. 17:7230-7238(1998).
CC -!- FUNCTION: Acts as a CAK-activating kinase that specifically activates
CC crk1 of the crk1-mcs2 CAK complex. {ECO:0000269|PubMed:9857180}.
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=2.7.11.22;
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=2.7.11.22;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; S59896; AAB26194.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93215.1; -; Genomic_DNA.
DR PIR; S39151; S39151.
DR RefSeq; NP_593019.1; NM_001018418.1.
DR AlphaFoldDB; P36615; -.
DR SMR; P36615; -.
DR BioGRID; 279750; 92.
DR STRING; 284812.P36615; -.
DR MaxQB; P36615; -.
DR PaxDb; 4896-SPAC1D4-06c-1; -.
DR EnsemblFungi; SPAC1D4.06c.1; SPAC1D4.06c.1:pep; SPAC1D4.06c.
DR GeneID; 2543327; -.
DR KEGG; spo:SPAC1D4.06c; -.
DR PomBase; SPAC1D4.06c; csk1.
DR VEuPathDB; FungiDB:SPAC1D4.06c; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; P36615; -.
DR OMA; FPDWNKF; -.
DR PhylomeDB; P36615; -.
DR BRENDA; 2.7.11.22; 5613.
DR PRO; PR:P36615; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; EXP:PomBase.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; ISO:PomBase.
DR GO; GO:0007165; P:signal transduction; IC:PomBase.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF581; SERINE_THREONINE-PROTEIN KINASE CSK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..306
FT /note="Serine/threonine-protein kinase csk1"
FT /id="PRO_0000085881"
FT DOMAIN 11..306
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 306 AA; 34672 MW; E670D87547523D0C CRC64;
MKSVGHFVPW LTDIRHLTDG TISEVFVGER KNSKKLYVIK VQGLVFKRPP HDAMRGKLIL
ESIGHPHIER IVDSFIDNEA GSVYLITSFK SFVLSDVMDE ISIDTKCKIV LQISSALEYL
EKHGILHRDI HPNNILLDSM NGPAYLSDFS IAWSKQHPGE EVQELIPQIG TGHYRAIETL
FGCHSYGHEV DRWTFGILIA ELFSNQALFD DGSSEGWPSE LRLTSSIIQT LGTPNPSMWP
ELSTFPDWNK FIFHEYPPKP WSEILPSVDT SIQYIVSHLV TYSNRASPSF VIESFPKVSA
RLSQYA
//
