DBF20_YEAST
ID DBF20_YEAST Reviewed; 564 AA.
AC P32328; D6W4B0; E9P8X8; Q06105;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Serine/threonine-protein kinase DBF20;
DE EC=2.7.11.1;
GN Name=DBF20; OrderedLocusNames=YPR111W;
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=1916278; DOI=10.1016/0378-1119(91)90465-n;
RA Toyn J.H., Araki H., Sugino A., Johnston L.H.;
RT "The cell-cycle-regulated budding yeast gene DBF2, encoding a putative
RT protein kinase, has a homologue that is not under cell-cycle control.";
RL Gene 104:63-70(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Is probably a Ser/Thr-protein kinase that may function in
CC initiation of DNA synthesis and also in late nuclear division.
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 -!- INTERACTION:
CC P32328; P40484: MOB1; NbExp=7; IntAct=EBI-5588, EBI-11119;
CC -!- MISCELLANEOUS: Present with 3320 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; M62506; AAB05204.1; -; Genomic_DNA.
DR EMBL; U32445; AAB68081.1; -; Genomic_DNA.
DR EMBL; AY692855; AAT92874.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11526.1; -; Genomic_DNA.
DR PIR; S59776; S59776.
DR RefSeq; NP_015436.1; NM_001184208.1.
DR AlphaFoldDB; P32328; -.
DR SMR; P32328; -.
DR BioGRID; 36278; 70.
DR ComplexPortal; CPX-5341; DBF20-MOB1 kinase complex.
DR DIP; DIP-3817N; -.
DR IntAct; P32328; 34.
DR MINT; P32328; -.
DR STRING; 4932.YPR111W; -.
DR iPTMnet; P32328; -.
DR MaxQB; P32328; -.
DR PaxDb; P32328; -.
DR PRIDE; P32328; -.
DR EnsemblFungi; YPR111W_mRNA; YPR111W; YPR111W.
DR GeneID; 856227; -.
DR KEGG; sce:YPR111W; -.
DR SGD; S000006315; DBF20.
DR VEuPathDB; FungiDB:YPR111W; -.
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000176430; -.
DR HOGENOM; CLU_000288_67_4_1; -.
DR InParanoid; P32328; -.
DR OMA; FPAFTER; -.
DR BioCyc; YEAST:G3O-34251-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P32328; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32328; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0000917; P:division septum assembly; IMP:SGD.
DR GO; GO:0010458; P:exit from mitosis; IGI:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0061013; P:regulation of mRNA catabolic process; IMP:SGD.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
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 Pfam; PF00433; Pkinase_C; 1.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..564
FT /note="Serine/threonine-protein kinase DBF20"
FT /id="PRO_0000085917"
FT DOMAIN 169..469
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 470..547
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 24..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 175..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22204"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 536
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22204"
FT CONFLICT 81
FT /note="K -> E (in Ref. 4; AAT92874)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="E -> Q (in Ref. 1; AAB05204)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="R -> S (in Ref. 1; AAB05204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 65880 MW; D1C0BD5BCE96A61B CRC64;
MFSRSDREVD DLAGNMSHLG FYDLNIPKPT SPQAQYRPAR KSENGRLTPG LPRSYKPCDS
DDQDTFKNRI SLNHSPKKLP KDFHERASQS KTQRVVNVCQ LYFLDYYCDM FDYVISRRQR
TKQVLRYLEQ QRSVKNVSNK VLNEEWALYL QREHEVLRKR RLKPKHKDFQ ILTQVGQGGY
GQVYLAKKKD SDEICALKIL NKKLLFKLNE TNHVLTERDI LTTTRSDWLV KLLYAFQDPE
SLYLAMEFVP GGDFRTLLIN TRILKSGHAR FYISEMFCAV NALHELGYTH RDLKPENFLI
DATGHIKLTD FGLAAGTVSN ERIESMKIRL EEVKNLEFPA FTERSIEDRR KIYHNMRKTE
INYANSMVGS PDYMALEVLE GKKYDFTVDY WSLGCMLFES LVGYTPFSGS STNETYENLR
YWKKTLRRPR TEDRRAAFSD RTWDLITRLI ADPINRVRSF EQVRKMSYFA EINFETLRTS
SPPFIPQLDD ETDAGYFDDF TNEEDMAKYA DVFKRQNKLS AMVDDSAVDS KLVGFTFRHR
DGKQGSSGIL YNGSEHSDPF STFY
