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Protein

Probable ATP-dependent kinase TDA10

Gene

TDA10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent kinase whose specificity is not yet known.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 458ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: SGD
  • kinase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30888-MONOMER.
BRENDAi2.7.1.31. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent kinase TDA10 (EC:2.7.-.-)
Alternative name(s):
Topoisomerase I damage affected protein 10
Gene namesi
Name:TDA10
Ordered Locus Names:YGR205W
ORF Names:G7737
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR205W.
SGDiS000003437. TDA10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Leads to cell death when overexpressing the camptothecin mimetic TOP1-T(722)A mutant.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Probable ATP-dependent kinase TDA10PRO_0000214076Add
BLAST

Proteomic databases

MaxQBiP42938.
PeptideAtlasiP42938.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KAR2P164741EBI-23474,EBI-7876
PTC3P342211EBI-23474,EBI-12805

Protein-protein interaction databases

BioGridi33458. 10 interactions.
DIPiDIP-3866N.
IntActiP42938. 4 interactions.
MINTiMINT-486081.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2417Combined sources
Turni25 – 273Combined sources
Beta strandi32 – 376Combined sources
Helixi44 – 5916Combined sources
Helixi60 – 623Combined sources
Beta strandi65 – 695Combined sources
Helixi70 – 734Combined sources
Helixi77 – 8610Combined sources
Turni87 – 893Combined sources
Helixi91 – 933Combined sources
Beta strandi94 – 963Combined sources
Helixi104 – 11411Combined sources
Beta strandi125 – 1284Combined sources
Turni133 – 1353Combined sources
Helixi136 – 1383Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi154 – 1629Combined sources
Turni172 – 1743Combined sources
Beta strandi176 – 1783Combined sources
Helixi182 – 19514Combined sources
Turni196 – 1983Combined sources
Beta strandi204 – 2129Combined sources
Helixi216 – 23217Combined sources
Helixi238 – 2469Combined sources
Helixi249 – 26214Combined sources
Beta strandi265 – 27511Combined sources
Beta strandi281 – 2877Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ODFX-ray2.25A1-290[»]
ProteinModelPortaliP42938.
SMRiP42938. Positions 5-290.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42938.

Family & Domainsi

Sequence similaritiesi

Belongs to the GLYK kinase family.Curated

Phylogenomic databases

InParanoidiP42938.
KOiK15918.
OMAiEANPDNG.
OrthoDBiEOG70KH13.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P42938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDKSKTVLD YTIEFLDKYI PEWFETGNKC PLFIFFSGPQ GSGKSFTSIQ
60 70 80 90 100
IYNHLMEKYG GEKSIGYASI DDFYLTHEDQ LKLNEQFKNN KLLQGRGLPG
110 120 130 140 150
THDMKLLQEV LNTIFNNNEH PDQDTVVLPK YDKSQFKGEG DRCPTGQKIK
160 170 180 190 200
LPVDIFILEG WFLGFNPILQ GIENNDLLTG DMVDVNAKLF FYSDLLWRNP
210 220 230 240 250
EIKSLGIVFT TDNINNVYGW RLQQEHELIS KVGKGMTDEQ VHAFVDRYMP
260 270 280 290
SYKLYLNDFV RSESLGSIAT LTLGIDSNRN VYSTKTRCIE
Length:290
Mass (Da):33,337
Last modified:November 1, 1995 - v1
Checksum:iEEB2DB5995122A29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12878 Genomic DNA. Translation: AAA66317.1.
Z49133 Genomic DNA. Translation: CAA88998.1.
Z72990 Genomic DNA. Translation: CAA97232.1.
AY558273 Genomic DNA. Translation: AAS56599.1.
BK006941 Genomic DNA. Translation: DAA08299.1.
PIRiB29550.
RefSeqiNP_011721.3. NM_001181334.3.

Genome annotation databases

EnsemblFungiiYGR205W; YGR205W; YGR205W.
GeneIDi853119.
KEGGisce:YGR205W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12878 Genomic DNA. Translation: AAA66317.1.
Z49133 Genomic DNA. Translation: CAA88998.1.
Z72990 Genomic DNA. Translation: CAA97232.1.
AY558273 Genomic DNA. Translation: AAS56599.1.
BK006941 Genomic DNA. Translation: DAA08299.1.
PIRiB29550.
RefSeqiNP_011721.3. NM_001181334.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ODFX-ray2.25A1-290[»]
ProteinModelPortaliP42938.
SMRiP42938. Positions 5-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33458. 10 interactions.
DIPiDIP-3866N.
IntActiP42938. 4 interactions.
MINTiMINT-486081.

Proteomic databases

MaxQBiP42938.
PeptideAtlasiP42938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR205W; YGR205W; YGR205W.
GeneIDi853119.
KEGGisce:YGR205W.

Organism-specific databases

EuPathDBiFungiDB:YGR205W.
SGDiS000003437. TDA10.

Phylogenomic databases

InParanoidiP42938.
KOiK15918.
OMAiEANPDNG.
OrthoDBiEOG70KH13.

Enzyme and pathway databases

BioCyciYEAST:G3O-30888-MONOMER.
BRENDAi2.7.1.31. 984.

Miscellaneous databases

EvolutionaryTraceiP42938.
PROiP42938.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-tetrahydrofolate synthase."
    Staben C., Rabinowitz J.C.
    J. Biol. Chem. 261:4629-4637(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
    Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
    Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Selective ploidy ablation, a high-throughput plasmid transfer protocol, identifies new genes affecting topoisomerase I-induced DNA damage."
    Reid R.J., Gonzalez-Barrera S., Sunjevaric I., Alvaro D., Ciccone S., Wagner M., Rothstein R.
    Genome Res. 21:477-486(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Crystal structure of the YGR205w protein from Saccharomyces cerevisiae: close structural resemblance to E. coli pantothenate kinase."
    de La Sierra-Gallay I.L., Collinet B., Graille M., Quevillon-Cheruel S., Liger D., Minard P., Blondeau K., Henckes G., Aufrere R., Leulliot N., Zhou C.Z., Sorel I., Ferrer J.L., Poupon A., Janin J., van Tilbeurgh H.
    Proteins 54:776-783(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), ATP-BINDING.

Entry informationi

Entry nameiTDA10_YEAST
AccessioniPrimary (citable) accession number: P42938
Secondary accession number(s): D6VUY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4280 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.