IME2_YEAST
ID IME2_YEAST Reviewed; 645 AA.
AC P32581; D6VW78;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Meiosis induction protein kinase IME2/SME1;
DE EC=2.7.11.1;
GN Name=IME2; Synonyms=SME1; OrderedLocusNames=YJL106W; ORFNames=J0817;
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].
RC STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX PubMed=2196430; DOI=10.1007/bf00261718;
RA Yoshida M., Kawaguchi H., Sakata Y., Kominami K.I., Hirano M., Shima H.,
RA Akada R., Yamashita I.;
RT "Initiation of meiosis and sporulation in Saccharomyces cerevisiae requires
RT a novel protein kinase homologue.";
RL Mol. Gen. Genet. 221:176-186(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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).
CC -!- FUNCTION: Protein kinase which is essential for the initiation of
CC meiosis and sporulation.
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X53262; CAA37351.1; -; Genomic_DNA.
DR EMBL; X85021; CAA59388.1; -; Genomic_DNA.
DR EMBL; Z49381; CAA89401.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08694.1; -; Genomic_DNA.
DR PIR; S20138; S20138.
DR RefSeq; NP_012429.1; NM_001181539.1.
DR AlphaFoldDB; P32581; -.
DR SMR; P32581; -.
DR BioGRID; 33650; 277.
DR DIP; DIP-4610N; -.
DR IntAct; P32581; 34.
DR MINT; P32581; -.
DR STRING; 4932.YJL106W; -.
DR iPTMnet; P32581; -.
DR PaxDb; P32581; -.
DR PRIDE; P32581; -.
DR EnsemblFungi; YJL106W_mRNA; YJL106W; YJL106W.
DR GeneID; 853338; -.
DR KEGG; sce:YJL106W; -.
DR SGD; S000003642; IME2.
DR VEuPathDB; FungiDB:YJL106W; -.
DR eggNOG; KOG0661; Eukaryota.
DR HOGENOM; CLU_000288_176_1_1; -.
DR InParanoid; P32581; -.
DR OMA; ANDHLIQ; -.
DR BioCyc; YEAST:G3O-31560-MON; -.
DR BRENDA; 2.7.11.22; 984.
DR PRO; PR:P32581; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32581; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1902596; P:negative regulation of DNA replication origin binding; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Sporulation; Transferase.
FT CHAIN 1..645
FT /note="Meiosis induction protein kinase IME2/SME1"
FT /id="PRO_0000086023"
FT DOMAIN 38..386
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 645 AA; 73593 MW; C1681A4D8A31FAE8 CRC64;
MVEKRSRQSS SSGSEFSVPP DVDNPPLSIP LKTLSDRYQL IEKLGAGSFG CVTLAKAQFP
LSNILGKQHD IRGTLMDQPK NGHQNYITKT QGVVAIKTMM TKLHTLQDYT RVREIKFILA
IPANDHLIQI FEVFIDSENY QLHIVMECME QNLYQMMKHR RRRVFSIPSL KSILSQILAG
LKHIHEHNFF HRDLKPENIL ITPSTQYFEK EYMNQIGYQD NYVIKLADFG LARHVENKNP
YTAYVSTRWY RSPEILLRSG YYSKPLDIWA FGCVAVEVTV FRALFPGANE IDQIWKILEV
LGTPIKRSDF VNTNHITAPP PGGFWDDASN LVHKLNLKLP YVEGSSLDHL LSSSQLSDLS
EVVKKCLRWD PNERATAQEL CEMPFFENTV ASQVDARGNV TNTEQALIFA GINPVATNTK
PIYFNSSTKL PAETESNDID ISNNDHDSHA MCSPTLNQEK LTLVEFLNEF VEEDNDDHSI
PDVGTDSTIS DSIDETELSK EIRNNLALCQ LPDEEVLDHS LSNIRQLTND IEIINKDEAD
NMEQLFFDLE IPEKDEFQRK QPFNEHADID EDIVLPYVNN SNYTHTDRSH HRGDNVLGDA
SLGDSFNSMP DFTPRNFLIP TLKKSREKFE PHLSNSNQHF GNVTF
