CBK1_CANAL
ID CBK1_CANAL Reviewed; 732 AA.
AC Q5AP53; A0A1D8PEW5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine/threonine-protein kinase CBK1;
DE EC=2.7.11.1;
DE AltName: Full=Cell wall biosynthesis kinase 1;
GN Name=CBK1; OrderedLocusNames=CAALFM_C110380CA;
GN ORFNames=CaO19.12375, CaO19.4909;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=11889116; DOI=10.1128/jb.184.7.2058-2061.2002;
RA McNemar M.D., Fonzi W.A.;
RT "Conserved serine/threonine kinase encoded by CBK1 regulates expression of
RT several hypha-associated transcripts and genes encoding cell wall proteins
RT in Candida albicans.";
RL J. Bacteriol. 184:2058-2061(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH MOB2.
RX PubMed=18843050; DOI=10.1091/mbc.e08-03-0272;
RA Song Y., Cheon S.A., Lee K.E., Lee S.Y., Lee B.K., Oh D.B., Kang H.A.,
RA Kim J.Y.;
RT "Role of the RAM network in cell polarity and hyphal morphogenesis in
RT Candida albicans.";
RL Mol. Biol. Cell 19:5456-5477(2008).
RN [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21593210; DOI=10.1091/mbc.e11-03-0205;
RA Gutierrez-Escribano P., Gonzalez-Novo A., Suarez M.B., Li C.R., Wang Y.,
RA de Aldana C.R., Correa-Bordes J.;
RT "CDK-dependent phosphorylation of Mob2 is essential for hyphal development
RT in Candida albicans.";
RL Mol. Biol. Cell 22:2458-2469(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH BCR1.
RX PubMed=22589718; DOI=10.1371/journal.ppat.1002683;
RA Gutierrez-Escribano P., Zeidler U., Suarez M.B., Bachellier-Bassi S.,
RA Clemente-Blanco A., Bonhomme J., Vazquez de Aldana C.R., d'Enfert C.,
RA Correa-Bordes J.;
RT "The NDR/LATS kinase Cbk1 controls the activity of the transcriptional
RT regulator Bcr1 during biofilm formation in Candida albicans.";
RL PLoS Pathog. 8:E1002683-E1002683(2012).
CC -!- FUNCTION: Serine/threonine-protein kinase required for wild-type hyphal
CC growth and transcriptional regulation of cell-wall-associated genes.
CC Involved in the biofilm formation through phosphorylation of the master
CC regulator of biofilm formation BCR1. {ECO:0000269|PubMed:11889116,
CC ECO:0000269|PubMed:18843050, ECO:0000269|PubMed:21593210,
CC ECO:0000269|PubMed:22589718}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBUNIT: Interacts with MOB2 and BCR1. {ECO:0000269|PubMed:18843050,
CC ECO:0000269|PubMed:22589718}.
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:21593210}. Cell tip
CC {ECO:0000269|PubMed:21593210}. Note=In yeast cells, localizes to the
CC cell cortex of small- and medium-budded cells and to the bud neck in
CC large-budded cells. During hyphal growth, is present at the tip of
CC hyphae and in the region of the septum.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. COT1 subfamily. {ECO:0000305}.
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DR EMBL; CP017623; AOW26667.1; -; Genomic_DNA.
DR RefSeq; XP_723591.2; XM_718498.2.
DR AlphaFoldDB; Q5AP53; -.
DR SMR; Q5AP53; -.
DR BioGRID; 1217932; 72.
DR STRING; 237561.Q5AP53; -.
DR PRIDE; Q5AP53; -.
DR GeneID; 3634838; -.
DR KEGG; cal:CAALFM_C110380CA; -.
DR CGD; CAL0000198853; CBK1.
DR VEuPathDB; FungiDB:C1_10380C_A; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_2_1; -.
DR InParanoid; Q5AP53; -.
DR OrthoDB; 759391at2759; -.
DR PRO; PR:Q5AP53; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005938; C:cell cortex; IDA:CGD.
DR GO; GO:0030428; C:cell septum; IDA:CGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IGI:CGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IEA:EnsemblFungi.
DR GO; GO:0000902; P:cell morphogenesis; IMP:CGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:EnsemblFungi.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036168; P:filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0031579; P:membrane raft organization; IMP:CGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1900433; P:positive regulation of filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:1900442; P:positive regulation of filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:1900233; P:positive regulation of single-species biofilm formation on inanimate substrate; IMP:CGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0050708; P:regulation of protein secretion; IEA:EnsemblFungi.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR InterPro; IPR000961; AGC-kinase_C.
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; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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; Coiled coil; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..732
FT /note="Serine/threonine-protein kinase CBK1"
FT /id="PRO_0000420233"
FT DOMAIN 335..647
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 648..730
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 110..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..310
FT /evidence="ECO:0000255"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 341..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 732 AA; 84500 MW; 7A9CF033CDEF170A CRC64;
MNFDQLTDEQ KQQLYLQHLQ QQQQLQQQQQ QLQQQQHQLQ QQQQSYHLQQ QQAAYQQQNQ
AQLQQDDSYM DEDTSELINQ PPVQLDHGSP IRQQPQMSAF MPSPRFAQSE SFDNHLNVDP
NNTERFTSMD SMNFQPPAST FTQLGNGSST NLSEISSGQN SLLSNHSVNN LPTALTSDTS
PPVQQHPQFQ PQQQQQQQQP QQQQIFQQQQ QQQQQQQQPQ QSRAVVNQSV STEAANSDMT
GSNTKYVYFE RKPNLLSKTT QDKAASIKLT LENYYTSSVS HAIERNQRRL ELENKIANED
IGSSEERKNR QLQNLGKKES QFLRLKRTKL ALEDFHTVKV IGKGAFGEVR LVQKKDTGKI
YAMKTLLKSE MFNKDQLAHV KAERDVLAGS DSPWIVALYY SFQDSQYLYL IMEFLPGGDL
MTMLIRWEVF TEDITRFYIA ECVLAIEAIH KLGFIHRDIK PDNILIDNRG HVKLSDFGLS
TGFHKTHDSN YYNKLLEKEP SNTHLQPNQL TSGRNSVMVD AIHLTMSNRQ TMQTWRKSRR
LMAYSTVGTP DYIAPEIFIH QGYGQECDWW SLGAIMFECL IGWPPFCSEN PHDTYRKILN
WQESFQIPED VHLSPEAEDL IKRFLTSAEN RIGRYGGAEE IKQHPFFRGV DWDSIRDVQA
PFVPRLSSMT DTRHFPTDDL ASVPDNPAMS KAMEQRELDA KNGGGRKNPK EDLPFIGYTY
SRFDYLTRKN AL
