SAKA_ASPFC
ID SAKA_ASPFC Reviewed; 366 AA.
AC B0XR80;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Mitogen-activated protein kinase sakA {ECO:0000303|PubMed:26878695};
DE Short=MAPK sakA {ECO:0000303|PubMed:26878695};
DE EC=2.7.11.24 {ECO:0000305|PubMed:26878695};
GN Name=sakA {ECO:0000303|PubMed:26878695}; ORFNames=AFUB_012420;
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=26878695; DOI=10.1111/mmi.13354;
RA Bruder Nascimento A.C., Dos Reis T.F., de Castro P.A., Hori J.I., Bom V.L.,
RA de Assis L.J., Ramalho L.N., Rocha M.C., Malavazi I., Brown N.A.,
RA Valiante V., Brakhage A.A., Hagiwara D., Goldman G.H.;
RT "Mitogen activated protein kinases SakA(HOG1) and MpkC collaborate for
RT Aspergillus fumigatus virulence.";
RL Mol. Microbiol. 100:841-859(2016).
CC -!- FUNCTION: Mitogen-activated protein kinase (MAPK), part of the high-
CC osmolarity glycerol (HOG) pathway (PubMed:26878695). With mpkC, plays a
CC role in the osmotic and oxidative stress responses (PubMed:26878695).
CC Involved in paradoxical growth, the cell wall integrity (CWI) pathway
CC and biofilm formation (PubMed:26878695). SakA and mpkC collaborate
CC during virulence and mpkC could act by modulating sakA activity upon
CC exposure to several types of stresses and during cell wall biosynthesis
CC (PubMed:26878695). {ECO:0000269|PubMed:26878695}.
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:26878695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:26878695};
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:26878695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:26878695};
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:26878695}.
CC Note=Translocates to the nucleus upon osmotic stress and cell wall
CC damage. {ECO:0000269|PubMed:26878695}.
CC -!- DISRUPTION PHENOTYPE: Increases the sensitivity to osmotic and
CC oxidative stresses as well as to cell wall damaging agents
CC (PubMed:26878695). Affects virulence when mpkC is also deleted
CC (PubMed:26878695). The single sakA deletion decreases mpkA
CC phosphorylation and the double sakA/mpkC deletion abolishes mpkA
CC phosphorylation (PubMed:26878695). {ECO:0000269|PubMed:26878695}.
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; DS499594; EDP56531.1; -; Genomic_DNA.
DR SMR; B0XR80; -.
DR EnsemblFungi; EDP56531; EDP56531; AFUB_012420.
DR VEuPathDB; FungiDB:AFUB_012420; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR PhylomeDB; B0XR80; -.
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 GO; GO:0051403; P:stress-activated MAPK cascade; IEA:InterPro.
DR CDD; cd07856; STKc_Sty1_Hog1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008352; MAPK_p38-like.
DR InterPro; IPR038783; MAPK_Sty1/Hog1.
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 PRINTS; PR01773; P38MAPKINASE.
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 Activator; ATP-binding; Kinase; Magnesium; Nucleotide-binding; Nucleus;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..366
FT /note="Mitogen-activated protein kinase sakA"
FT /id="PRO_0000454884"
FT DOMAIN 20..299
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 366 AA; 41960 MW; 45B8F9234DAD334A CRC64;
MAEFVRAQIF GTTFEITSRY TDLQPVGMGA FGLVCSARDQ LTGQPVAVKK IMKPFSTPVL
SKRTYRELKL LKHLRHENII SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY
FLYQILRGLK YVHSAGVVHR DLKPSNILIN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
APEIMLTWQK YDVEVDIWSA GCIFAEMLEG KPLFPGKDHV NQFSIITELL GTPPDDVIQT
ICSENTLRFV KSLPKRERQP LANKFKNADP EAVDLLERML VFDPKKRIRA GEALAHEYLS
PYHDPTDEPE AEEKFDWSFN DADLPVDTWK IMMYSEILDF HNIDQGNDAG QVLMEGGVAQ
AQQNYA
