MEK1_SCHPO
ID MEK1_SCHPO Reviewed; 445 AA.
AC Q10292;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Meiosis-specific serine/threonine-protein kinase mek1;
DE EC=2.7.11.1;
GN Name=mek1; ORFNames=SPAC14C4.03;
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].
RC STRAIN=972 / ATCC 24843;
RA Lyne M.H., Bryant J.A., Aves S.J.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
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: Probable protein kinase required for meiotic recombination.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily. {ECO:0000305}.
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DR EMBL; Z71478; CAA96101.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11196.1; -; Genomic_DNA.
DR PIR; T43420; T43420.
DR RefSeq; NP_594908.1; NM_001020340.1.
DR AlphaFoldDB; Q10292; -.
DR SMR; Q10292; -.
DR BioGRID; 278101; 10.
DR STRING; 4896.SPAC14C4.03.1; -.
DR iPTMnet; Q10292; -.
DR PaxDb; Q10292; -.
DR PRIDE; Q10292; -.
DR EnsemblFungi; SPAC14C4.03.1; SPAC14C4.03.1:pep; SPAC14C4.03.
DR GeneID; 2541604; -.
DR KEGG; spo:SPAC14C4.03; -.
DR PomBase; SPAC14C4.03; mek1.
DR VEuPathDB; FungiDB:SPAC14C4.03; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q10292; -.
DR OMA; MEYNSET; -.
DR PhylomeDB; Q10292; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-69473; G2/M DNA damage checkpoint.
DR Reactome; R-SPO-69541; Stabilization of p53.
DR Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SPO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR PRO; PR:Q10292; -.
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:0030998; C:linear element; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM: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:0051598; P:meiotic recombination checkpoint signaling; IMP:PomBase.
DR GO; GO:1904514; P:positive regulation of initiation of premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007131; P:reciprocal meiotic recombination; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Meiosis; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..445
FT /note="Meiosis-specific serine/threonine-protein kinase
FT mek1"
FT /id="PRO_0000086320"
FT DOMAIN 62..116
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 160..421
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 166..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 445 AA; 51151 MW; 6D62D79E9A1B45B0 CRC64;
MDFLSHAMLS RSESTQILCE LSQIDESTMD PQYTEDDVLA RLFVFSSSSP QTVLNVKKYE
DVSVGRSNTC NYQLLQFTAS YKHFRVYSVL IDDDMDPLVY CEDQSSNGTF LNHRLIGKGN
SVLLSDGDIL DVRHCASFLF QQKYTTDNDF HHEYAGERFN ITQRLLGIGG FSRIYMAMDN
NTGGQYACKI IDKKKISTKR FFEDHEMTIL RKLDHPNIIK VNMEYNSETQ FFIFEEMVTG
GDLFSYLTKL GTVPEVTTLF IMFQILQGLK YLHEQNIIHR DLKLENILIA SSSDTIFRII
LTDFGVARCM QKGKRLSTFV GTPEYTAPEI QRLKGRSQVE KENSSGYGKE VDLWSLGVIM
FLLLSGNSPS FADGVKEKQV DFRDPVWKSV SRQAKDLISN LLKTNPPDRF TVKQCLSHPW
FARHSSRLTK LYETRILKPL KHSRL
