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MPKB_ASPFC
ID   MPKB_ASPFC              Reviewed;         353 AA.
AC   B0Y8W7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Mitogen-activated protein kinase mpkB {ECO:0000303|PubMed:30914505};
DE            Short=MAPK mpkB {ECO:0000303|PubMed:30914505};
DE            EC=2.7.11.24 {ECO:0000305|PubMed:30914505};
GN   Name=mpkB {ECO:0000303|PubMed:30914505}; ORFNames=AFUB_078810;
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, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=30914505; DOI=10.1128/mbio.00215-19;
RA   Manfiolli A.O., Siqueira F.S., Dos Reis T.F., Van Dijck P., Schrevens S.,
RA   Hoefgen S., Foege M., Strassburger M., de Assis L.J., Heinekamp T.,
RA   Rocha M.C., Janevska S., Brakhage A.A., Malavazi I., Goldman G.H.,
RA   Valiante V.;
RT   "Mitogen-activated protein kinase cross-talk interaction modulates the
RT   production of melanins in Aspergillus fumigatus.";
RL   MBio 10:0-0(2019).
CC   -!- FUNCTION: Mitogen-activated protein kinase (MAPK) that plays a role in
CC       conidiation and regulation of secondary metabolite biosynthesis
CC       (PubMed:30914505). Acts as a repressor of dihydroxynaphthalene (DHN)-
CC       melanin production (PubMed:30914505). {ECO:0000269|PubMed:30914505}.
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:30914505};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC         Evidence={ECO:0000305|PubMed:30914505};
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:30914505};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC         Evidence={ECO:0000305|PubMed:30914505};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|RuleBase:RU361165};
CC   -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC       phosphorylation. {ECO:0000255|RuleBase:RU361165}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30914505}.
CC       Note=Translocates into the nucleus upon exposure to caspofungin stress,
CC       and this is dependent on the cross-talk interaction with mpkA.
CC       {ECO:0000269|PubMed:30914505}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a strong increase of
CC       dihydroxynaphthalene (DHN)-melanin production (PubMed:30914505).
CC       Results in about 3-fold less glucosamine and a lower level of alpha-
CC       linked mannose within the cell wall (PubMed:30914505). Does not affect
CC       virulence (PubMed:30914505). {ECO:0000269|PubMed:30914505}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; DS499599; EDP49848.1; -; Genomic_DNA.
DR   EnsemblFungi; EDP49848; EDP49848; AFUB_078810.
DR   VEuPathDB; FungiDB:AFUB_078810; -.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   PhylomeDB; B0Y8W7; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
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; PS01351; MAPK; 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; Magnesium; Nucleotide-binding; Nucleus;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..353
FT                   /note="Mitogen-activated protein kinase mpkB"
FT                   /id="PRO_0000454882"
FT   DOMAIN          21..309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         27..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   353 AA;  40853 MW;  3F6299212C820D21 CRC64;
     MVQQPPQGGS RKISFNVSEQ YEIQDVIGEG AYGVVCSAIH KPSGQKVAIK KITPFDHSMF
     CLRTLREMKL LRYFNHENII SILDIQRPRN YESFNEVYLI QELMETDMHR VIRTQDLSDD
     HCQYFIYQTL RALKAMHSAN VLHRDLKPSN LLLNANCDLK VCDFGLARSA ASTDDNSGFM
     TEYVATRWYR APEIMLTFKE YTKAIDVWSV GCILAEMLSG KPLFPGKDYH HQLTLILDVL
     GTPTMEDYYG IKSRRAREYI RSLPFKKKIP FKALFPKSNE LALDLLEKLL AFNPAKRITV
     EEALRHPYLE PYHDPDDEPT APPIPEGFFD FDKNKDALSK EQLKTLIYEE IMR
 
 
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