MCK1_MAGO7
ID MCK1_MAGO7 Reviewed; 1528 AA.
AC G4NDR3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Mitogen-activated protein kinase kinae kinase MCK1 {ECO:0000303|PubMed:18393612};
DE Short=MAPKKK MCK1 {ECO:0000303|PubMed:18393612};
DE EC=2.7.11.24 {ECO:0000305|PubMed:18393612};
DE AltName: Full=MEKK MCK1 {ECO:0000303|PubMed:18393612};
GN Name=MCK1 {ECO:0000303|PubMed:18393612}; ORFNames=MGG_00883;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18393612; DOI=10.1094/mpmi-21-5-0525;
RA Jeon J., Goh J., Yoo S., Chi M.H., Choi J., Rho H.S., Park J., Han S.S.,
RA Kim B.R., Park S.Y., Kim S., Lee Y.H.;
RT "A putative MAP kinase kinase kinase, MCK1, is required for cell wall
RT integrity and pathogenicity of the rice blast fungus, Magnaporthe oryzae.";
RL Mol. Plant Microbe Interact. 21:525-534(2008).
RN [3]
RP FUNCTION, AND INTERACTION WITH MTS50 AND MIP11.
RX PubMed=28244240; DOI=10.1111/1462-2920.13710;
RA Li G., Zhang X., Tian H., Choi Y.E., Tao W.A., Xu J.R.;
RT "MST50 is involved in multiple MAP kinase signaling pathways in Magnaporthe
RT oryzae.";
RL Environ. Microbiol. 19:1959-1974(2017).
CC -!- FUNCTION: Mitogen-activated protein kinase kinase kinase; part of the
CC MCK1-MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is
CC essential for appressorium formation, penetration and invasive growth
CC (PubMed:18393612, PubMed:28244240). Beside its role in pathogenesis,
CC the MPS1 cascade is active in conidiation and cellular stress responses
CC (By similarity). Targets downstream of the the MPS1-MAPK pathway
CC include transcription factors MIG1 and SWI6, as well as GSK1 and MPG1
CC (PubMed:28244240). {ECO:0000250|UniProtKB:G4N0Z0,
CC ECO:0000269|PubMed:18393612, ECO:0000269|PubMed:28244240}.
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=2.7.11.24;
CC Evidence={ECO:0000305|PubMed:18393612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:18393612};
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=2.7.11.24; Evidence={ECO:0000305|PubMed:18393612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:18393612};
CC -!- SUBUNIT: Interacts with the adapter protein MST50 and MIP11.
CC {ECO:0000269|PubMed:28244240}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to cell-wall-degrading
CC enzymes (PubMed:18393612). Reduces significantly numbers of conidia and
CC develops appressoria in a slightly retarded manner (PubMed:18393612).
CC Impairs the ability of appressoria to penetrate into plant tissues,
CC thereby abolishing pathogenicity (PubMed:18393612).
CC {ECO:0000269|PubMed:18393612}.
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; CM001235; EHA48501.1; -; Genomic_DNA.
DR RefSeq; XP_003718085.1; XM_003718037.1.
DR AlphaFoldDB; G4NDR3; -.
DR SMR; G4NDR3; -.
DR STRING; 318829.MGG_00883T0; -.
DR EnsemblFungi; MGG_00883T0; MGG_00883T0; MGG_00883.
DR GeneID; 2674608; -.
DR KEGG; mgr:MGG_00883; -.
DR VEuPathDB; FungiDB:MGG_00883; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000961_3_0_1; -.
DR InParanoid; G4NDR3; -.
DR OMA; GNLGKMH; -.
DR OrthoDB; 55144at2759; -.
DR PHI-base; PHI:777; -.
DR Proteomes; UP000009058; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProt.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase;
KW Virulence.
FT CHAIN 1..1528
FT /note="Mitogen-activated protein kinase kinae kinase MCK1"
FT /id="PRO_0000453098"
FT DOMAIN 1238..1507
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1244..1252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1528 AA; 166014 MW; 37A1D7D6EF1AED87 CRC64;
MYPGSSQSRP YQVPPPPPMS PPLSQMHQQM SFVPPPPPPL NRYQTTPNLG ASAPPPPPPG
PPPASALNPQ APWNGAWGGV PAPRQAYDNR SGMYAQAPIQ QYNPQAHAAT APGLNIPPPP
LQTDAPMSDT YNPGQDPMFD GFMPDLSFDL EQETMGSSQT WQTTSSSSTN TASVNDNVQS
NAPTEERTRR NNSASITGTQ SSSNVPGIPS DITASWSLDK VIAWLQMNSF SRDWQETFKS
LNIHGAQFLE LGSGHFGRGN FGMMHQQVYP KLAKVCTASG TGWDQPRERE EGKRMRRLIR
GLVHARAVPD SARVPSSHGR QGSINSRGND KGTHDGSDSP NTPSSQSRST TIPTFPDGSS
FSNHRGVLKN IDIDRHSSPK LNGDSPAASP NPVMASSTPK SSTLSVSPHS SRFGNNVRNS
TDSVKAIYGS GIPADAQKMM SNSNLDELIN GRGARQSPSD LGDNSAGTDS PVSARDTKLP
FRQRMQAKDI DGNLSSPNGE GSLSPQMYRN GLGLDDYLRF KKPGGSIYLM ATADGWNYRV
VDVTDVETVL DLRSEISRGL GIPDEDGVEF YLTELGKSDH SQPLDDNQLM NHNKSRADAE
GTLKLFVKPP PMSQQSTWSA GDTGQRHRFG TSSSMSRQQN TLKDDQSEEA RLRAQREYKA
EIDRKGREYL AIRKAKLESN NNGLSSSTEG IGIVGKPVDF DTPRHSPYED KNTDRMFPTR
NAPAPPVAPS ATLNRVNSLM TGQRRVQGSM DGYPSQRVPP GVGTTTSPKE MSEDRRRQPM
SGSQPMGGIT SALVDMGRNL GGVALPNRGV SANNVPSKPS PPYRVATAPV SGRDFVSPDN
RAAFPRSQTA GDLSPISQMP ANFAAYQEPN PSPRGFGAAP VSSAAHKRAP SGPDIDFTEP
EVSFDRPAPS TAQNEAQSDD DSGDDSDDGL FVIPIAARKA SMKKAKSRAS VTFDASDSGD
GKRPALTVNT ARDRKSVSFN SPQSARTGDD DDDSGRQRRT PKSDMWDSED GKLGRRKSFK
MDVWANRPPA EALINNLEDF FPGMDVDQPV LEEGDQEQNI DGSPVAPSPI AEVDETQSPG
HLQINATPLN SLPPSRVQSM YNESDTLGSD ESTLKALERP PSFQSLAQRS VRRSGGLGRM
KSIREKARGA HEAHKRYTQT SMAAPQGLSR SGGTPATETQ PTQNNSSALL RRKSTKMFNA
NIVQIRPNRD SMLVPDIPQD SISSSSRGAP KHPTTFRWFK GQLIGKGTYG RVYLGMNATT
GEFLAVKEVE VNPRAAAGDK KRMKELVAAL DQEIETMQHL DHVNIVQYLG CERKETSISI
FLEYISGGSI GSCLRKNGKF EESVVQSLTR QTLSGLAYLH REGILHRDLK ADNILLDVDG
TAKISDFGIS KKTDNIYGND KSNSMQGSVF WMAPEVIRSQ GEGYSAKVDI WSLGCVVLEM
FAGRRPWAKE EAVGAIYKIA NGEIPPIPED VQDTISPIAV AFMMDCFTVD SHDRPTANKL
LSQHPFCELD PNYNFLDSEL YAKIRGTY
