KKQ8_YEAS7
ID KKQ8_YEAS7 Reviewed; 724 AA.
AC A6ZZF6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Probable serine/threonine-protein kinase KKQ8;
DE EC=2.7.11.1;
GN Name=KKQ8; ORFNames=SCY_3216;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN60111.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFW02000150; EDN60111.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A6ZZF6; -.
DR SMR; A6ZZF6; -.
DR PRIDE; A6ZZF6; -.
DR EnsemblFungi; EDN60111; EDN60111; SCY_3216.
DR HOGENOM; CLU_016904_1_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..724
FT /note="Probable serine/threonine-protein kinase KKQ8"
FT /id="PRO_0000337757"
FT DOMAIN 412..712
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 563
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 418..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36004"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36004"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36004"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36004"
SQ SEQUENCE 724 AA; 82532 MW; 08004CC9039FFB13 CRC64;
MVMQEEKKRQ QPVTRRVRSF SESFKNLFRP PRSRDSSPIN VTRIPYRSSS TSPKRSSEPP
RRSTVSAQIL DPKNSPIRQR SYTLKCCTPG LSHPFRQTGS GASNSPTRHR SISGEEQEIV
NSLPEYKRSA SHTFHGIRRP RSRSSSVSSC DSSNGTTSSS DSQWAMDSLL DDSDNDLTPY
RGSNKDILKS KDRAPYNYID DYNKKALRRA TSYPNPLPSK QFYNERLYTR RSHPDEESLE
SLPRSAGADV QCIIEQNGFK VYEDGSHEHN IKLSGVIAKL EKGNSLPVHR QGLLSRPRLG
ITLSGLFKHH KNECDIENAS SLLPNVEKSQ TNHEKRTGQS PNDSNRSSPT QGREDYLKIV
NPDASLGSDE LKLINSLSSR IHKSLQNYLQ EKNLKPAECI GEQAPTFQDN YGHPVGLVGA
GAYGEVKLCA RLRNEKDSPP FETYHDSKYI YYAVKELKPK PDSDLEKFCT KITSEFIIGH
SLSHYHKNGK KPAPNILNVF DILEDSSSFI EVMEFCPAGD LYGMLVGKSK LKGRLHPLEA
DCFMKQLLHG VKFMHDHGIA HCDLKPENIL FYPHGLLKIC DFGTSSVFQT AWERRVHAQK
GIIGSEPYVA PEEFVDGEYY DPRLIDCWSC GVVYITMILG HHLWKVASRE KDMSYDEFYK
EMQRKNQFRV FEELKHVNSE LATNRKIALY RIFQWEPRKR ISVGKLLDMQ WMKSTNCCLI
YDST
