TDA10_YEAST
ID TDA10_YEAST Reviewed; 290 AA.
AC P42938; D6VUY8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable ATP-dependent kinase TDA10;
DE EC=2.7.-.-;
DE AltName: Full=Topoisomerase I damage affected protein 10;
GN Name=TDA10; OrderedLocusNames=YGR205W; ORFNames=G7737;
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=3514599; DOI=10.1016/s0021-9258(17)38548-4;
RA Staben C., Rabinowitz J.C.;
RT "Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-
RT tetrahydrofolate synthase.";
RL J. Biol. Chem. 261:4629-4637(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND ATP-BINDING.
RX PubMed=14997573; DOI=10.1002/prot.10596;
RA de La Sierra-Gallay I.L., Collinet B., Graille M., Quevillon-Cheruel S.,
RA Liger D., Minard P., Blondeau K., Henckes G., Aufrere R., Leulliot N.,
RA Zhou C.Z., Sorel I., Ferrer J.L., Poupon A., Janin J., van Tilbeurgh H.;
RT "Crystal structure of the YGR205w protein from Saccharomyces cerevisiae:
RT close structural resemblance to E. coli pantothenate kinase.";
RL Proteins 54:776-783(2004).
CC -!- FUNCTION: ATP-dependent kinase whose specificity is not yet known.
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 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GLYK kinase family. {ECO:0000305}.
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DR EMBL; M12878; AAA66317.1; -; Genomic_DNA.
DR EMBL; Z49133; CAA88998.1; -; Genomic_DNA.
DR EMBL; Z72990; CAA97232.1; -; Genomic_DNA.
DR EMBL; AY558273; AAS56599.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08299.1; -; Genomic_DNA.
DR PIR; B29550; B29550.
DR RefSeq; NP_011721.3; NM_001181334.3.
DR PDB; 1ODF; X-ray; 2.25 A; A=1-290.
DR PDBsum; 1ODF; -.
DR AlphaFoldDB; P42938; -.
DR SMR; P42938; -.
DR BioGRID; 33458; 20.
DR DIP; DIP-3866N; -.
DR IntAct; P42938; 5.
DR MINT; P42938; -.
DR STRING; 4932.YGR205W; -.
DR MaxQB; P42938; -.
DR PaxDb; P42938; -.
DR PRIDE; P42938; -.
DR EnsemblFungi; YGR205W_mRNA; YGR205W; YGR205W.
DR GeneID; 853119; -.
DR KEGG; sce:YGR205W; -.
DR SGD; S000003437; TDA10.
DR VEuPathDB; FungiDB:YGR205W; -.
DR eggNOG; KOG2878; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_056986_0_0_1; -.
DR InParanoid; P42938; -.
DR OMA; KSTWTDA; -.
DR BioCyc; YEAST:G3O-30888-MON; -.
DR BRENDA; 2.7.1.31; 984.
DR EvolutionaryTrace; P42938; -.
DR PRO; PR:P42938; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P42938; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0008887; F:glycerate kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Probable ATP-dependent kinase TDA10"
FT /id="PRO_0000214076"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:1ODF"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1ODF"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1ODF"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1ODF"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:1ODF"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:1ODF"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:1ODF"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:1ODF"
SQ SEQUENCE 290 AA; 33337 MW; EEB2DB5995122A29 CRC64;
MCDKSKTVLD YTIEFLDKYI PEWFETGNKC PLFIFFSGPQ GSGKSFTSIQ IYNHLMEKYG
GEKSIGYASI DDFYLTHEDQ LKLNEQFKNN KLLQGRGLPG THDMKLLQEV LNTIFNNNEH
PDQDTVVLPK YDKSQFKGEG DRCPTGQKIK LPVDIFILEG WFLGFNPILQ GIENNDLLTG
DMVDVNAKLF FYSDLLWRNP EIKSLGIVFT TDNINNVYGW RLQQEHELIS KVGKGMTDEQ
VHAFVDRYMP SYKLYLNDFV RSESLGSIAT LTLGIDSNRN VYSTKTRCIE
