ID   MIK1_SCHPO              Reviewed;         581 AA.
AC   P30290;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Mitosis inhibitor protein kinase mik1;
DE            EC=2.7.11.1;
GN   Name=mik1; ORFNames=SPBC660.14;
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=1706223; DOI=10.1016/0092-8674(91)90266-2;
RA   Lundgren K., Walworth N., Booher R., Dembski M., Kirschner M., Beach D.;
RT   "mik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of
RT   cdc2.";
RL   Cell 64:1111-1122(1991).
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: Protein kinase that acts both on serines and on tyrosines. It
CC       acts as a negative regulator of entry into mitosis (G2 to M
CC       transition). Phosphorylates and inhibits cdc2.
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. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; M60834; AAA91278.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA22534.1; -; Genomic_DNA.
DR   PIR; A37913; A37913.
DR   RefSeq; NP_595093.1; NM_001021000.2.
DR   AlphaFoldDB; P30290; -.
DR   SMR; P30290; -.
DR   BioGRID; 277402; 61.
DR   STRING; 284812.P30290; -.
DR   iPTMnet; P30290; -.
DR   PaxDb; 4896-SPBC660-14-1; -.
DR   EnsemblFungi; SPBC660.14.1; SPBC660.14.1:pep; SPBC660.14.
DR   GeneID; 2540885; -.
DR   KEGG; spo:SPBC660.14; -.
DR   PomBase; SPBC660.14; mik1.
DR   VEuPathDB; FungiDB:SPBC660.14; -.
DR   eggNOG; KOG0601; Eukaryota.
DR   HOGENOM; CLU_468646_0_0_1; -.
DR   InParanoid; P30290; -.
DR   OMA; QPHTPCK; -.
DR   PhylomeDB; P30290; -.
DR   PRO; PR:P30290; -.
DR   Proteomes; UP000002485; Chromosome II.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IGI:PomBase.
DR   GO; GO:0110031; P:negative regulation of G2/MI transition of meiotic cell cycle; IMP:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
DR   CDD; cd14052; PTKc_Wee1_fungi; 1.
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   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR   PANTHER; PTHR11042:SF180; MITOSIS INHIBITOR PROTEIN KINASE MIK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Kinase; Magnesium; Metal-binding;
KW   Mitosis; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..581
FT                   /note="Mitosis inhibitor protein kinase mik1"
FT                   /id="PRO_0000086327"
FT   DOMAIN          289..561
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          43..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        417
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         295..303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         422
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   581 AA;  65934 MW;  371E0CEDB2CA1CE3 CRC64;
     MDSSTTIPIT PTRTPCFFNI SSSFNEHSPL NFYDEPIYNF SSGHEENQSH KSSKLTFFKP
     SNTKRSPHTP MQNNAKAIRL STTVRHGIFK NSDLDGCSKP FAFSSGLKLS KKIVDASTPI
     DLKRKRAVTS LSTGLLSKRE KWSLWEGNLT NPRSEQPHTP CKKGTKIKLK PPQSPLSPTT
     SLLARKCKHI DLDTFSRLDH PNSDSSDETF EMEELPSLSY GSEDLLEFCE TPCKSQPIFL
     SSSHVNNWDE KDVPSSLSWT PTSPIFLNIN SADDYEEEED WTSDLRIRFQ QVKPIHESDF
     SFVYHVSSIN PPTETVYVVK MLKKNAAKFT GKERHLQEVS ILQRLQACPF VVNLVNVWSY
     NDNIFLQLDY CENGDLSLFL SELGLLQVMD PFRVWKMLFQ LTQALNFIHL LEFVHLDVKP
     SNVLITRDGN LKLGDFGLAT SLPVSSMVDL EGDRVYIAPE ILASHNYGKP ADVYSLGLSM
     IEAATNVVLP ENGVEWQRLR SGDYSNLPNL KDLLLSKEKV QINKVRCAES LQCLLQRMTH
     PYVDCRPTTQ DLLAMPEMIF ISEHSQKAAI IYEDHNSWLE T
//