KKQ8_CANGA
ID KKQ8_CANGA Reviewed; 766 AA.
AC Q6FJ85;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable serine/threonine-protein kinase KKQ8;
DE EC=2.7.11.1;
GN Name=KKQ8; OrderedLocusNames=CAGL0M08360g;
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NPR/HAL subfamily. HAL5 sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; CR380959; CAG62685.1; -; Genomic_DNA.
DR RefSeq; XP_449709.1; XM_449709.1.
DR AlphaFoldDB; Q6FJ85; -.
DR SMR; Q6FJ85; -.
DR STRING; 5478.XP_449709.1; -.
DR EnsemblFungi; CAG62685; CAG62685; CAGL0M08360g.
DR GeneID; 2891268; -.
DR KEGG; cgr:CAGL0M08360g; -.
DR CGD; CAL0136865; CAGL0M08360g.
DR VEuPathDB; FungiDB:CAGL0M08360g; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_016904_0_0_1; -.
DR InParanoid; Q6FJ85; -.
DR OMA; VGSEPYV; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
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:0030003; P:cellular cation homeostasis; IEA:EnsemblFungi.
DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:EnsemblFungi.
DR GO; GO:0008104; P:protein localization; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..766
FT /note="Probable serine/threonine-protein kinase KKQ8"
FT /id="PRO_0000333585"
FT DOMAIN 449..752
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 603
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 455..463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 766 AA; 85781 MW; C7A827898C85833E CRC64;
MPEHEERHSH GVNRSLSLGS SMRSLFKSQR SRGPSDRGAN GTPGPAQKVD IRVDTASASR
EHTPVVHKTP QSANPELQQP RHHLGLPNIL KLNLTPTNSN PQSKSGSPVS QNTSQESLIT
DTDIEVEDYR PSKDSRRTVR NASPMSSNGN LPINANTVIG PDTSSNNIDS MLDGTGLRPF
YEEADSSDYI ENLRSFPLPT GHYAPGFIQP PKSPTSSRVP SRSNSRKGRE HAGTVSAAQL
PRYNETPGKC ILDLEYFKLY EDGHHVHTLK VMTSVNSDAN GNSHNHASKN DGHLDLPKGD
DGSVVRQKSK FSLSGFFKPH SKEDIANADE KLKYAVSLLP RNKICSKVET DRDTFAPVFT
KTRSHVQSGS DDSSDDDEEL DDPSIPKIVN KNAAVGSQEL KLINNLSEKI RMGLSTAAKN
KHNQSSKHRT PSGAGVQDEN QPAFADLYGK CVAVVGHGAY GVVKVCARTR DEKDDLPATK
TYMDSKKIYF AVKELKPRPS DPIEKFSTRI TSEFIIGHSL SHYYDKNGEQ SAPNILSIID
LLEYNDTFIE VMEFCPAGDL YSLLTARKNK IGKPLHPLEA DCFMKQLLKG IQFMHDHGVA
HCDLKPENIL LHPNGLLKIC DFGTSCVFQT AWERHVHFQT GLQGSEPYVA PEEYNPKKEY
DPRLVDCWSI GIVYCTMIMG HYLWRNAARG KDSLYDSFYE EMASKKEFYV FEELRHINQE
INRLRRIALY QIFQPNPEKR ISIDKLLQTG WMRHTKCCVP YKNIPR
