CBK1_DEBHA
ID CBK1_DEBHA Reviewed; 716 AA.
AC Q6BLJ9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Serine/threonine-protein kinase CBK1;
DE EC=2.7.11.1;
GN Name=CBK1; OrderedLocusNames=DEHA2F12848g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89275.2; -; Genomic_DNA.
DR RefSeq; XP_460922.2; XM_460922.1.
DR AlphaFoldDB; Q6BLJ9; -.
DR SMR; Q6BLJ9; -.
DR STRING; 4959.XP_460922.2; -.
DR EnsemblFungi; CAG89275; CAG89275; DEHA2F12848g.
DR GeneID; 2904251; -.
DR KEGG; dha:DEHA2F12848g; -.
DR VEuPathDB; FungiDB:DEHA2F12848g; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_2_1; -.
DR InParanoid; Q6BLJ9; -.
DR OMA; PERYSEN; -.
DR OrthoDB; 759391at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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..716
FT /note="Serine/threonine-protein kinase CBK1"
FT /id="PRO_0000085693"
FT DOMAIN 315..634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 635..714
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 22..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 321..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 716 AA; 83384 MW; 23ED3580AAEE1AAB CRC64;
MNYDYLTDEQ KQQLYFHQMQ AEQQQHQQQL HYKQQQHIQQ QQQHQQNQQN QQQQPQPPRQ
PFSTFLQNNG SNSDLPQMGT FQQDLQRQNI PNLRFSQQNQ PSDLGQEFQD DDSFMDEDLT
EIHEQPPMQE LNSSPMTHPH SFQQNFQTPT KNDDANLRNQ QFQSVDSERS LDFKPPVTFT
KLNNNSNADL SSPTESSFLK SNLNLPNSNI PPAGASNDPN AQKSNYIYFN RQPNSLNKIA
QDKASSIKLK LENYYQMSVA HAIERNQRRL DLEHKLLNEE SGSSEERKNR QLQNLGKKES
QFLRLRRTKL SLEDFNTVKV IGKGAFGEVR LVQKRDTGKI YAMKTLLKSE MYKKDQLAHV
KAERDVLAGS DSPWVVSLYY SFQDAQYLYL IMEFLPGGDL MTMLIRWQIF TEDITRFYMA
ECVLAIEAIH KLGFIHRDIK PDNILIDIRG HIKLSDFGLS TGFHKTHDSN YYKKLLEKEN
PHHTNPQNGN LQAPSMATNN RNSMMVDAIH LTMSNRQQMQ TWRKSRRLMA YSTVGTPDYI
APEIFVHQGY GQECDWWSLG AIMFECLIGW PPFCSETPHE TYRKILNWQE TLQIPDDIHL
SPESEDLIRK LLTNAENRLG RYNGADELKS HPFFRGVDWD TIRKVDAPFI PKLRSITDTR
FFPTDELENV PDSPALSKAM EQRDQVLQNG GNVKEDLPFI GYTYSRFDYL TRKNAL
