ID TDA1_YEAST Reviewed; 586 AA.
AC Q03533; D6W0B8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=Serine/threonine-protein kinase TDA1;
DE AltName: Full=Topoisomerase I damage affected protein 1;
DE EC=2.7.11.1;
GN Name=TDA1; OrderedLocusNames=YMR291W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11062466; DOI=10.1038/81576;
RA Zhu H., Klemic J.F., Chang S., Bertone P., Casamayor A., Klemic K.G.,
RA Smith D., Gerstein M., Reed M.A., Snyder M.;
RT "Analysis of yeast protein kinases using protein chips.";
RL Nat. Genet. 26:283-289(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504; SER-509 AND SER-578, AND
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).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=21173034; DOI=10.1101/gr.109033.110;
RA Reid R.J., Gonzalez-Barrera S., Sunjevaric I., Alvaro D., Ciccone S.,
RA Wagner M., Rothstein R.;
RT "Selective ploidy ablation, a high-throughput plasmid transfer protocol,
RT identifies new genes affecting topoisomerase I-induced DNA damage.";
RL Genome Res. 21:477-486(2011).
RN [12]
RP INTERACTION WITH RIM11.
RX PubMed=21460040; DOI=10.1101/gad.1998811;
RA Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M.,
RA Gerstein M., Snyder M.;
RT "Diverse protein kinase interactions identified by protein microarrays
RT reveal novel connections between cellular processes.";
RL Genes Dev. 25:767-778(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Serine/threonine protein kinase shown to have protein
CC phosphorylation activity in vitro. {ECO:0000269|PubMed:11062466}.
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 -!- SUBUNIT: Interacts with RIM11. {ECO:0000269|PubMed:21460040}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Leads to cell death when overexpressing the
CC camptothecin mimetic TOP1-T(722)A mutant.
CC {ECO:0000269|PubMed:21173034}.
CC -!- MISCELLANEOUS: Present with 10200 molecules/cell in log phase SD
CC medium. {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; X80836; CAA56800.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10192.1; -; Genomic_DNA.
DR PIR; S47452; S47452.
DR RefSeq; NP_014019.1; NM_001182799.1.
DR AlphaFoldDB; Q03533; -.
DR SMR; Q03533; -.
DR BioGRID; 35471; 178.
DR DIP; DIP-1641N; -.
DR IntAct; Q03533; 9.
DR MINT; Q03533; -.
DR STRING; 4932.YMR291W; -.
DR GlyGen; Q03533; 16 sites, 1 O-linked glycan (16 sites).
DR iPTMnet; Q03533; -.
DR MaxQB; Q03533; -.
DR PaxDb; 4932-YMR291W; -.
DR PeptideAtlas; Q03533; -.
DR EnsemblFungi; YMR291W_mRNA; YMR291W; YMR291W.
DR GeneID; 855336; -.
DR KEGG; sce:YMR291W; -.
DR AGR; SGD:S000004905; -.
DR SGD; S000004905; TDA1.
DR VEuPathDB; FungiDB:YMR291W; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000176527; -.
DR HOGENOM; CLU_465513_0_0_1; -.
DR InParanoid; Q03533; -.
DR OMA; FEGHHHV; -.
DR OrthoDB; 1121238at2759; -.
DR BioCyc; YEAST:G3O-32961-MONOMER; -.
DR BioGRID-ORCS; 855336; 10 hits in 13 CRISPR screens.
DR PRO; PR:Q03533; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03533; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
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; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..586
FT /note="Serine/threonine-protein kinase TDA1"
FT /id="PRO_0000086153"
FT DOMAIN 39..351
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 538
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 586 AA; 66220 MW; 584D620D5F798EF6 CRC64;
MTTASSSASQ LQQRLPEEKP WPQLSGSNAD AQTFKCKYVT NHNSLGDGNF SVVKECMNIH
TKDLYAMKLI KKQTVKNKIQ LIQREFDLLR SISEKIRDME KKNEHSLDIF EGHHHILQLF
DYFETADNIV LITQLCQKGD LYEKIVENQC LDLETQVTSY CACLVSVLEF LHSQGIVHRD
LKAENVLFRL RVNENEKNLQ GEHHGDFKYD LLAHDLVLAD FGLAAEYNTS KVNSLKEFVG
TISYIAPEIV KCKGVGEMTP DQVGKLDKYG CPVDIWALGV LTYFMAFGYT PFDCTTDDET
LECISKCDYY VDEQMMHDPK YEQFWNFVQC CFTIDPAVRR SAKNLKQHPF IKDYFATSNS
LNTKDTPNFS FHPTIRRVSS TASMHTLRSP SKSRKTTTLA YLNMDGGSSE TSTAFSSKMD
LPDLYVDRTI NSRERSLNRI RDTLKKTLSM TSLKPAGTFD YLHANKNGTS LSSSKSGLVK
KNSTFVLDPK PPKNSLMNGC FSTTPESRSN FNTPKTLSRQ GSSTSVKKYV NEVDLLLTPR
TASMSSNDTT AINDYDTTND KNPARKHAAS FQVNVDDSDG DETMQI
//
