MEK1_YEAST
ID MEK1_YEAST Reviewed; 497 AA.
AC P24719; D6W346;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Meiosis-specific serine/threonine-protein kinase MEK1;
DE EC=2.7.11.1;
GN Name=MEK1; Synonyms=MRE4; OrderedLocusNames=YOR351C; ORFNames=O6357;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1752435; DOI=10.1101/gad.5.12b.2392;
RA Rockmill B., Roeder G.S.;
RT "A meiosis-specific protein kinase homolog required for chromosome synapsis
RT and recombination.";
RL Genes Dev. 5:2392-2404(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1741279; DOI=10.1093/nar/20.3.449;
RA Leem S.-H., Ogawa H.;
RT "The MRE4 gene encodes a novel protein kinase homologue required for
RT meiotic recombination in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 20:449-457(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-497.
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8948102;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT chromosome XV reveals 18 open reading frames including a new pyruvate
RT kinase and three homologues to chromosome I genes.";
RL Yeast 12:1475-1481(1996).
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; X61208; CAA43522.1; -; Genomic_DNA.
DR EMBL; X63112; CAA44825.1; -; Genomic_DNA.
DR EMBL; X95720; CAA65038.1; -; Genomic_DNA.
DR EMBL; Z75259; CAA99680.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11112.1; -; Genomic_DNA.
DR PIR; S20174; S20174.
DR RefSeq; NP_014996.3; NM_001183771.3.
DR PDB; 5YYX; X-ray; 1.68 A; A=20-139.
DR PDB; 5YYZ; X-ray; 1.80 A; A=20-139.
DR PDBsum; 5YYX; -.
DR PDBsum; 5YYZ; -.
DR AlphaFoldDB; P24719; -.
DR SMR; P24719; -.
DR BioGRID; 34736; 191.
DR DIP; DIP-675N; -.
DR IntAct; P24719; 38.
DR STRING; 4932.YOR351C; -.
DR iPTMnet; P24719; -.
DR PaxDb; P24719; -.
DR PRIDE; P24719; -.
DR EnsemblFungi; YOR351C_mRNA; YOR351C; YOR351C.
DR GeneID; 854533; -.
DR KEGG; sce:YOR351C; -.
DR SGD; S000005878; MEK1.
DR VEuPathDB; FungiDB:YOR351C; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00960000189172; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; P24719; -.
DR OMA; NHVYVRD; -.
DR BioCyc; YEAST:G3O-33822-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P24719; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P24719; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 3D-structure; ATP-binding; Kinase; Meiosis; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..497
FT /note="Meiosis-specific serine/threonine-protein kinase
FT MEK1"
FT /id="PRO_0000086321"
FT DOMAIN 47..102
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 162..444
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 168..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5YYX"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:5YYX"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5YYX"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:5YYX"
SQ SEQUENCE 497 AA; 56850 MW; 7E197338881EF6D0 CRC64;
MRPLYSCNLA TKDDIEMAGG VAPAHLEVNV GGYNTEQTIP IVKHQLVKVG RNDKECQLVL
TNPSISSVHC VFWCVFFDED SIPMFYVKDC SLNGTYLNGL LLKRDKTYLL KHCDVIELSQ
GSEENDIKKT RLVFMINDDL QSSLDPKLLD QMGFLREVDQ WEITNRIVGN GTFGHVLITH
NSKERDEDVC YHPENYAVKI IKLKPNKFDK EARILLRLDH PNIIKVYHTF CDRNNHLYIF
QDLIPGGDLF SYLAKGDCLT SMSETESLLI VFQILQALNY LHDQDIVHRD LKLDNILLCT
PEPCTRIVLA DFGIAKDLNS NKERMHTVVG TPEYCAPEVG FRANRKAYQS FSRAATLEQR
GYDSKCDLWS LGVITHIMLT GISPFYGDGS ERSIIQNAKI GKLNFKLKQW DIVSDNAKSF
VKDLLQTDVV KRLNSKQGLK HIWIAKHLSQ LERLYYKKIL CNNEGPKLES INSDWKRKLP
KSVIISQAIP KKKKVLE
