CBK1_KLULA
ID CBK1_KLULA Reviewed; 718 AA.
AC P31034; Q6CRM8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine/threonine-protein kinase CBK1;
DE EC=2.7.11.1;
GN Name=CBK1; OrderedLocusNames=KLLA0D07810g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-235.
RX PubMed=8477753; DOI=10.1111/j.1432-1033.1993.tb17827.x;
RA Dehoux P., Davies J., Cannon M.;
RT "Natural cycloheximide resistance in yeast. The role of ribosomal protein
RT L41.";
RL Eur. J. Biochem. 213:841-848(1993).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35264.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR382124; CAH00507.1; -; Genomic_DNA.
DR EMBL; M94988; AAA35264.1; ALT_FRAME; Genomic_DNA.
DR PIR; S32480; S32480.
DR RefSeq; XP_453411.1; XM_453411.1.
DR AlphaFoldDB; P31034; -.
DR SMR; P31034; -.
DR STRING; 28985.XP_453411.1; -.
DR EnsemblFungi; CAH00507; CAH00507; KLLA0_D07810g.
DR GeneID; 2893513; -.
DR KEGG; kla:KLLA0_D07810g; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_2_1; -.
DR InParanoid; P31034; -.
DR OMA; PERYSEN; -.
DR Proteomes; UP000000598; Chromosome D.
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..718
FT /note="Serine/threonine-protein kinase CBK1"
FT /id="PRO_0000085694"
FT DOMAIN 303..631
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 632..716
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 309..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 718 AA; 83132 MW; FF67C8CB75F8DC63 CRC64;
MYGGYSNQNY YQQPSGRPND FQQQGNMPFS EPSQPMFSTN YMKQQGSQPS LQDRLTQQQS
QPQSHNNQYY PNGGFTDVPN LNYPATPPPT QSIYSHNNNS NSKVYQSAQH TSPGQYSVAS
ESGLYIPPPL QQQQNGQQSP VRSVHQQTQQ TPPTFTQQQS SSQPQSPQHN TYHAQQQQQQ
QQQQQQTQQA QQQGQRQTQQ QSQQQAQQQN GSANNYMYFE RRPDLLTKTT QDKAAAVKLK
IENFYQSSVG YAIERNQRRL ELESELASQD WSEERKNRQL ASLGKKESQF LRLRRTRLSL
DDFNSVKVIG KGAFGEVRLV QKKDTGKIYA MKTLLKSEMY NKDQLAHVKA ERDVLAGSDS
PWVVSLYYSF QDSQYLYLIM EFLPGGDLMT MLIRWQIFTE DVTRFYMAEC ILAIEVIHKL
GFIHRDIKPD NILIDIRGHI KLSDFGLSTG FHKTHDSSYY KKLLQEDEAK KQQQQQQQQQ
QLNLQKPQLP NETNNGNRNT MLVDAIHLTM TNRQQMQTWR KSRRLMAYST VGTPDYIAPE
IFLYQGYGQE CDWWSLGAIM YECLIGWPPF CSETPQETYR KIMNFEQTLQ FPDDIHISYE
AEDLIRRLLT HSENRLGRHG GADEIKAHPF FSGVDWNTIR QVEAPYIPKL SSVTDTRFFP
TDELENVPDS PAMAQAARQR EQMMTQQQGV PQSNAKEDLP FIGYTYSRFD YLTRKNAL
