BCK1_ASPFC
ID BCK1_ASPFC Reviewed; 1617 AA.
AC B0XXN8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Mitogen-activated protein kinase kinae kinase bck1 {ECO:0000303|PubMed:19715768};
DE Short=MAPKKK bck1 {ECO:0000303|PubMed:19715768};
DE EC=2.7.11.24 {ECO:0000305|PubMed:19715768};
GN Name=bck1 {ECO:0000303|PubMed:19715768}; ORFNames=AFUB_038060;
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 kinase (MAPKKK), part of the
CC cell 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS499596; EDP52640.1; -; Genomic_DNA.
DR EnsemblFungi; EDP52640; EDP52640; AFUB_038060.
DR VEuPathDB; FungiDB:AFUB_038060; -.
DR HOGENOM; CLU_000961_3_0_1; -.
DR PhylomeDB; B0XXN8; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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..1617
FT /note="Mitogen-activated protein kinase kinae kinase bck1"
FT /id="PRO_0000454886"
FT DOMAIN 1323..1596
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1453
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1329..1337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1617 AA; 175919 MW; 1AB12BFE38D84FBE CRC64;
MDGQRQQTYI PAPPPPSATQ PSQSHMLSLP PPPPRHLPTQ PQGVMPPPPP GPPPGPPPGP
GYGASKLANS QLQQQNNLGW QHNWARQALS QGFLPPPPPP PMVPTNQAYG RQTSFSVPNA
DGPITSATYV PGSNTFGAGV GIPGFDAHTR PSYEAYGTMS GSDRIRGPVH HLYESSGGDG
SAYKRDGTVP PTPSARTMPS SLALHDNAQE SVASSLPGAT AQNHQSQTGQ TNEPTKSPSH
RQNNSNTLLG GMSPSEAAVQ WPLDRVLLWL AKNGFSRDWQ ETFKTLQIEG ADFLDIGHGA
NGRGNFNKMH NEVFPQLAKE CEASGTGWDK ERELGEGKRM RRLIRQIHDD DSFDVGIPAQ
KRRESQAPSE GAPDTSPKLS HEPQSAGPHS GTIENSPNLR APQLAQPHRH SVQMRSVTLP
IPTTHDIASS DFSQKDGISS RSDFSRSVLV GLGVDHRRQS PSMSSDNGNL VAPFRSYEDS
PKSGSPATQH ATLNQGLSSS STGDLSVKYE HSRGNSSDST MGRRYYESRK GQETIRPSPQ
EMCSRQWTGE TSSSYPKEHK GIFNFLKKRS KGGDSTHPSP EEPNLESPTS PVNLRQNGPH
LPYTKPSFNA SDMSLGERPS SASMSDHERL RGKPAQKGKK WSFVTLDGWN YRLVDITDMD
SVETLRAAIC HNLGIADWAS AQIFLTEPGQ SDHEEPLNDT MLALCRRTKS DSIGSLKLFV
RGTHLQPVPN HVPNFAGLGV PLPDKHTASP THHLPRKPLD DEALSRIPPQ PQTGPASPQL
GIRPQQPKTP AAKFPARDAP QHTEGMSPVE GDQQVGISPE PDKADLLARH EEHKREVERK
QKAYLSSKGP PQPRNDSYGE TGYRRAGVID FDERRVSPYE DKKADTLVPL RKPPSAPQES
YTLTRINSLR KKDGDRPRAQ PAVQTHGLGA VLASMGRMTS AIGTPAPSVP TPTSAGGKQT
NFGSFGSPTQ GNTKSAPQSS PEKESLDNPG NPAEHRHTKS TAPEIPKPTL QSRKSYGPEF
DFEETEVSFQ RSPRPQDDSD EDSDDGLFAI PLSNNKASTK ENDSGSGTSE AQKRTEKPAL
TVNTESRLRK GLSVSFRSPS ATRESFADAN GDSGGREGAS FLMAASPEDE RPPPRRDSFA
RGDIWASRPP VEGVIDNLDD FFPDIDLDAP YLDGQGVSPP SSPANRAPPE NDLHKKENQP
SSSYTGEMNA NAGDTLGSNE PTLKPQGGDV VARRNINRSG GGLTRGKSIR EVAKGANQAS
RSRSIHTGNQ KSGEILRRKS TKMFGAKIMQ IKPKPGSRLS QLDPIPQNNT PSGVPQRQPT
FRIIRGQLIG KGTYGRVYLG INADNGEVLA VKQVEINPRL AGQDTDRVKE MVAAMDQEID
TMQHLEHPNI VQYLGCERGE FSISIYLEYI SGGSIGSCLR KHGKFEESVV KSLTRQTLSG
LAYLHDQGIL HRDLKADNIL LDLDGTCKIS DFGISKKTDD IYGNDSSNSM QGSVFWMAPE
VIQSQGQGYS AKVDIWSLGC VVLEMFAGRR PWSKEEAIGA IFKLGSLSQA PPIPDDVSMT
ISPAALAFMY DCFTVPYRDS SERPTAQTLL TRHPFCEEDP NYNFLDTELY AKIRHVL
