KIN3_YEAST
ID KIN3_YEAST Reviewed; 435 AA.
AC P22209; D6VPM5;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Serine/threonine-protein kinase KIN3;
DE EC=2.7.11.1;
GN Name=KIN3; Synonyms=NPK1; OrderedLocusNames=YAR018C; ORFNames=FUN52;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1644305; DOI=10.1016/0378-1119(92)90502-g;
RA Barton A.B., Davies C.J., Hutchison C.A. III, Kaback D.B.;
RT "Cloning of chromosome I DNA from Saccharomyces cerevisiae: analysis of the
RT FUN52 gene, whose product has homology to protein kinases.";
RL Gene 117:137-140(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1495480; DOI=10.1007/bf00272358;
RA Schweitzer B., Philippsen P.;
RT "NPK1, a nonessential protein kinase gene in Saccharomyces cerevisiae with
RT similarity to Aspergillus nidulans nimA.";
RL Mol. Gen. Genet. 234:164-167(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-369.
RC STRAIN=SB303;
RX PubMed=2199332; DOI=10.1016/0378-1119(90)90442-t;
RA Jones D.G.L., Rosamond J.;
RT "Isolation of a novel protein kinase-encoding gene from yeast by
RT oligodeoxyribonucleotide probing.";
RL Gene 90:87-92(1990).
CC -!- FUNCTION: This protein is probably a serine/threonine protein kinase.
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M67445; AAA34399.2; -; Genomic_DNA.
DR EMBL; X60549; CAA43042.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04964.1; -; Genomic_DNA.
DR EMBL; M55416; AAB04029.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06995.1; -; Genomic_DNA.
DR PIR; S23580; S23580.
DR RefSeq; NP_009410.1; NM_001178217.1.
DR AlphaFoldDB; P22209; -.
DR SMR; P22209; -.
DR BioGRID; 31800; 306.
DR DIP; DIP-1646N; -.
DR ELM; P22209; -.
DR IntAct; P22209; 21.
DR MINT; P22209; -.
DR STRING; 4932.YAR018C; -.
DR iPTMnet; P22209; -.
DR MaxQB; P22209; -.
DR PaxDb; P22209; -.
DR PRIDE; P22209; -.
DR EnsemblFungi; YAR018C_mRNA; YAR018C; YAR018C.
DR GeneID; 851273; -.
DR KEGG; sce:YAR018C; -.
DR SGD; S000000071; KIN3.
DR VEuPathDB; FungiDB:YAR018C; -.
DR eggNOG; KOG0591; Eukaryota.
DR GeneTree; ENSGT00940000156989; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; P22209; -.
DR OMA; PSRPEDY; -.
DR BioCyc; YEAST:G3O-28874-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P22209; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P22209; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
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; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..435
FT /note="Serine/threonine-protein kinase KIN3"
FT /id="PRO_0000086134"
FT DOMAIN 25..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 92
FT /note="F -> L (in Ref. 6; AAB04029)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="V -> L (in Ref. 6; AAB04029)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="E -> Q (in Ref. 6; AAB04029)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="V -> I (in Ref. 6; AAB04029)"
FT /evidence="ECO:0000305"
FT CONFLICT 235..238
FT /note="AKSL -> SQIS (in Ref. 6; AAB04029)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="K -> R (in Ref. 6; AAB04029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 51203 MW; 7CB49CD6A93CA019 CRC64;
MHRRQFFQEY RSPQQQQGHP PRSEYQVLEE IGRGSFGSVR KVIHIPTKKL LVRKDIKYGH
MNSKERQQLI AECSILSQLK HENIVEFYNW DFDEQKEVLY LYMEYCSRGD LSQMIKHYKQ
EHKYIPEKIV WGILAQLLTA LYKCHYGVEL PTLTTIYDRM KPPVKGKNIV IHRDLKPGNI
FLSYDDSDYN INEQVDGHEE VNSNYYRDHR VNSGKRGSPM DYSQVVVKLG DFGLAKSLET
SIQFATTYVG TPYYMSPEVL MDQPYSPLSD IWSLGCVIFE MCSLHPPFQA KNYLELQTKI
KNGKCDTVPE YYSRGLNAII HSMIDVNLRT RPSTFELLQD IQIRTARKSL QLERFERKLL
DYENELTNIE KILEKQAIEY ERELSQLKEQ FTQAVEERAR EVISGKKVGK VPESINGYYG
KKFAKPAYHW QTRYR
