MKK2_ASPFC
ID MKK2_ASPFC Reviewed; 503 AA.
AC B0XPE4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Mitogen-activated protein kinase kinae mkk2 {ECO:0000303|PubMed:19715768};
DE Short=MAPKK mkk2 {ECO:0000303|PubMed:19715768};
DE EC=2.7.11.24 {ECO:0000305|PubMed:19715768};
GN Name=mkk2 {ECO:0000303|PubMed:19715768}; ORFNames=AFUB_006190;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19715768; DOI=10.1016/j.fgb.2009.08.005;
RA Valiante V., Jain R., Heinekamp T., Brakhage A.A.;
RT "The MpkA MAP kinase module regulates cell wall integrity signaling and
RT pyomelanin formation in Aspergillus fumigatus.";
RL Fungal Genet. Biol. 46:909-918(2009).
CC -!- FUNCTION: Mitogen-activated kinase kinase (MAPKK), part of the cell
CC wall integrity (CWI) signaling pathway composed by three protein
CC kinases bck1, mkk2 and mpkA and responsible for the maintaining of
CC cell-wall integrity balance (PubMed:19715768). The CWI pathway
CC regulates also the oxidative stress response, as well as the production
CC of some secondary metabolites including pyomelanin (PubMed:19715768).
CC {ECO:0000269|PubMed:19715768}.
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:19715768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:19715768};
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:19715768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:19715768};
CC -!- DISRUPTION PHENOTYPE: Leads to the formation of thicker hyphae, which
CC appear less elongated and form more branched hyphae (PubMed:19715768).
CC Results in increased sensitivity to cell wall integrity inhibitors such
CC as glucanex, SDS, congo red and calcofluor white (PubMed:19715768).
CC Impairs phosphorylation of the MAPK mpkA (PubMed:19715768).
CC {ECO:0000269|PubMed:19715768}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; DS499594; EDP55917.1; -; Genomic_DNA.
DR SMR; B0XPE4; -.
DR EnsemblFungi; EDP55917; EDP55917; AFUB_006190.
DR VEuPathDB; FungiDB:AFUB_006190; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR PhylomeDB; B0XPE4; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:EnsemblFungi.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:EnsemblFungi.
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; Transferase.
FT CHAIN 1..503
FT /note="Mitogen-activated protein kinase kinae mkk2"
FT /id="PRO_0000454885"
FT DOMAIN 211..481
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 217..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 503 AA; 54781 MW; A763A873AA99F4BA CRC64;
MSSSPVPLLR PPVPGNRGNG PRPPKLTLGI PPSPNSRPVD GNGVGPAAAA PEAPQPQRPS
TRPAPPQLRL ATPMGSSSDV PQEVPRLANG RPAPPPLATT GLNESTGHSR SSSFTYLDGK
ASGPASASSS NYSALSFAMG LRQPHGSTPD PSSAISSVYS DREGGVQMER DNSVNGLLPD
LDKLSLEKGR PLDVDDLDDE GWLAASEQKK IIELGSLGEG AGGAVTRCKL KDGKTVFALK
IITTDPNPDV KKQIVRELNF NKDCASEHIC RYYGAFMDKS TGTISIAMEF CEGGSLDSIY
KEVKKLGGRT GEKVLGKIAE GVLNGLTYLH SRKIIHRDIK PSNILLCRNG QVKLCDFGVS
GEFGTKGDAN TFIGTSYYMA PERITGQSYT ITSDVWSLGV TLLEVAQHRF PFPADGTEMQ
PRAGLIDLLT YIVRQPIPKL KDEPENRIRW SDNFKYFIEC CLEKEPPRRA TPWRMLEHPW
MLDMKNKKVN MANFVRQVWG WQD
