MKH1_SCHPO
ID MKH1_SCHPO Reviewed; 1116 AA.
AC Q10407;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=MAP kinase kinase kinase mkh1;
DE EC=2.7.11.25;
GN Name=mkh1; ORFNames=SPAC1F3.02c;
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=SP66;
RX PubMed=9199286; DOI=10.1128/mcb.17.7.3508;
RA Sengar A.S., Markley N.A., Marini N.J., Young D.;
RT "Mkh1, a MEK kinase required for cell wall integrity and proper response to
RT osmotic and temperature stress in Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 17:3508-3519(1997).
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: May regulate cell morphology, cell wall integrity, salt
CC resistance, cell cycle reentry from stationary-phase arrest, and
CC filamentous growth in response to stress. Activates the MAP kinase
CC kinase skh1/pek1 by phosphorylation.
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=2.7.11.25;
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=2.7.11.25;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; U53872; AAB62319.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA94620.1; -; Genomic_DNA.
DR PIR; T38073; T38073.
DR RefSeq; NP_593005.1; NM_001018404.2.
DR AlphaFoldDB; Q10407; -.
DR SMR; Q10407; -.
DR BioGRID; 278650; 194.
DR IntAct; Q10407; 1.
DR STRING; 4896.SPAC1F3.02c.1; -.
DR iPTMnet; Q10407; -.
DR MaxQB; Q10407; -.
DR PaxDb; Q10407; -.
DR PRIDE; Q10407; -.
DR EnsemblFungi; SPAC1F3.02c.1; SPAC1F3.02c.1:pep; SPAC1F3.02c.
DR GeneID; 2542175; -.
DR KEGG; spo:SPAC1F3.02c; -.
DR PomBase; SPAC1F3.02c; mkh1.
DR VEuPathDB; FungiDB:SPAC1F3.02c; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_281062_0_0_1; -.
DR InParanoid; Q10407; -.
DR OMA; GGAQYIE; -.
DR PhylomeDB; Q10407; -.
DR BRENDA; 2.7.11.25; 5613.
DR PRO; PR:Q10407; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IMP:PomBase.
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:0000196; P:cell wall integrity MAPK cascade; IMP:PomBase.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1116
FT /note="MAP kinase kinase kinase mkh1"
FT /id="PRO_0000086331"
FT DOMAIN 825..1094
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 510..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 955
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 831..839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 854
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1116 AA; 125133 MW; 7AFDB3EC62EED47B CRC64;
MAADIGSQSS GSLEERFEQS LHLQNVDKQD WSLNSVLQFL KLYKFNKEWE DVFIKSRIEM
DLFINLADQS KAEEFAFKNK LSKESAIQLS SCIRKTLLAP SSTRVPSKNS SYETLTYSAK
DSSDDVFTET NSGFRSSNQN SSLKSFQSVP DSNVNVFGGF GGSVVDNNEL LSTGKNSHQT
TSLNLEGSPI NLHAYKGTVT SIINDDSRNI NKKTLSKQPV SEHKEKQTSF LRRFRVPGFS
RDKDKTKDCP SSNSNPFHLA SSNVKTLDAS LDQGEWVPRI HRLESQIGLI SKKKSFVLAT
MDDMKFTVVD ITNVQNATQL RKLIAKSMYL DISIDQFDLF LTEVGGAQYI EILDDRKLDI
ARLYSDEFGT IKFFVKPSQN EESGMDSDTY LSFGTKSSST YKADDDSIYH RKEDFKKQPS
YPVLTSDFEI TDAGPNLSLS GHQPDNKYYK GFSSAPNLAV VPELPSRRFR GFEKIRGAKG
EMATKILDAT EAQSEKNKFT VCRPHKKVTL KMPLNSGSSA PQSPSSNTSA SVLTRNFVAH
RDPPPPPTET SSLRRKNTLT RRPSIRHARS SPYIDTGHNE ASKFSHTSFD PKASSKSSNS
LKESVEALSE IPFEDAPALD ESDLSGDPFW AIQPKQSSSQ VPKENHHNIQ SKLSINTEAA
TDLKANELSS PKTPEYCRGD DRSISLSPLS YRLRKSKHIR ESPPSSKVIN SGNWEVRPSA
DDLYEDVDRF FPRYDLDKVL VVDQSRMVSS PSKVSIRPKM KSVRLLAREA SEARKEIRHN
ARRNKSGNLL RRSSTKLWGS RIVELKPDTT ITSGSVVSQN ATFKWMKGEL IGNGTYGKVF
LAMNINTGEL IAVKQVEIPQ TINGRHDQLR KDIVDSINAE ISMIADLDHL NIVQYLGFEK
TETDISIFLE YVSGGSIGRC LRNYGPFEEQ LVRFVSRQVL YGLSYLHSKG IIHRDLKADN
LLIDFDGVCK ISDFGISKHS DNVYDNDANL SMQGSIFWMA PEVIHNDHQG YSAKVDVWSL
GCVVLEMLAG RRPWSTDEAI QAMFKLGTEK KAPPIPSELV SQVSPEAIQF LNACFTVNAD
VRPTAEELLN HPFMKCDEEF NFKDTNLYDM LCKRKS
