CBK1_CANGA
ID CBK1_CANGA Reviewed; 773 AA.
AC Q6FP74;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine/threonine-protein kinase CBK1;
DE EC=2.7.11.1;
GN Name=CBK1; OrderedLocusNames=CAGL0J06072g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Protein kinase that seems to play a role in the regulation of
CC cell morphogenesis and proliferation. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. COT1 subfamily. {ECO:0000305}.
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DR EMBL; CR380956; CAG60921.1; -; Genomic_DNA.
DR RefSeq; XP_447970.1; XM_447970.1.
DR AlphaFoldDB; Q6FP74; -.
DR SMR; Q6FP74; -.
DR STRING; 5478.XP_447970.1; -.
DR EnsemblFungi; CAG60921; CAG60921; CAGL0J06072g.
DR GeneID; 2889779; -.
DR KEGG; cgr:CAGL0J06072g; -.
DR CGD; CAL0133578; CBK1.
DR VEuPathDB; FungiDB:CAGL0J06072g; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_2_1; -.
DR InParanoid; Q6FP74; -.
DR OMA; KIINWQE; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0005938; C:cell cortex; IEA:EnsemblFungi.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
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; IEA:UniProtKB-KW.
DR GO; GO:0007118; P:budding cell apical bud growth; IEA:EnsemblFungi.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:EnsemblFungi.
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:0000920; P:septum digestion after cytokinesis; IEA:EnsemblFungi.
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; 2.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..773
FT /note="Serine/threonine-protein kinase CBK1"
FT /id="PRO_0000085692"
FT DOMAIN 370..686
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 687..771
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 50..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 493
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 376..384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 773 AA; 88741 MW; 7CD0EEFE7D38C398 CRC64;
MFGGEYDHAY DANNGQRFQP PVLDAMEFEK PGSPSVGDHF LRQQISNQSL HDQYSSHMEQ
QQQQQQQQHN AAYGAGFTDI PQLHPSTPPH GLVQKISNGN FHPAMNQGGN IPSTSNMNNM
FNTPPPTMGN NPLYSHDNNS TNLLQDNLNQ ARSQFSPDRY SVDSDFNNGA GNHVMANGNY
NINGSQSSSP YHQPQTFYTN SNLSSGQLSA HRSSPQRQPA QPLQQTTFTQ LPQPSLPPQQ
QQQQQQQQQQ QQQQQPKFQS MVPPQQTQLQ QQQQQELQNA GSYMYFERRP DLLSKSTQDK
AAAVKLKVEN YYQQSVKYAI ERNERRVELE TELGSHNWSE ERNARQLASL GKKESQFLRL
RRTRLSLEDF HTVQVIGKGA FGEVRLVQKK DTGKIYAMKT LLKSEMYKKD QLAHVKAERD
VLAGTDSPWI VSLYYSFQDA QYLYLIMEFL PGGDLMTMLI RWQLFTEDVT RFYMAECILA
IETIHKLGFI HRDIKPDNIL IDIRGHIKLS DFGLSTGFHK THDSNYYKKL LQQDEATTKN
GAPNDAGDGS NNRQTMIVDS INLTMSNRQQ IQTWRKSRRL MAYSTVGTPD YIAPEIFLYQ
GYGQDCDWWS LGAIMYECLI GWPPFCSETP QETYRKIMNF EQTLQFPEDV HISYEAEDLI
RRLLTHSNQR LGRQGGADEI KSHPFFRGVD WNTIRQVEAP YIPKLSSITD TRFFPTDELE
NVPDSPAMAQ AAKQREQMMK NGVNPNQNQV KEDLPFIGYT YSRFDYLTRK NAL
