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InterPro: IPR003594 ATPase-like, ATP-binding domain

Protein matchesHelp
UniProtKB
Matches:
70830 proteins
AccessionHelp IPR003594 ATPase-like_ATP-bd
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004358 Signal transduction histidine kinase-related protein, C-terminal
IPR020575 Heat shock protein Hsp90, N-terminal
Found in IPR001241 DNA topoisomerase, type IIA, subunit B or N-terminal
IPR001404 Chaperone protein htpG
IPR002099 DNA mismatch repair protein
IPR005467 Signal transduction histidine kinase, core
IPR005734 DNA topoisomerase VI, subunit B
IPR005737 DNA topoisomerase IV, subunit B, Gram-negative
IPR005740 DNA topoisomerase IV, subunit B, Gram-positive
IPR006290 Signal transduction histidine kinase, heavy metal sensor
IPR008358 Signal transduction histidine kinase/phosphatase, lantibiotic regulatory protein MprB
IPR010193 Anti-sigma B factor
IPR010194 Anti-sigma F factor
IPR011186 DNA mismatch repair protein Mlh1
IPR011557 DNA gyrase, subunit B
IPR012129 Phytochrome A/B/C/D/E
IPR014285 Nitrogen fixation negative regulator NifL
IPR014525 Signal transduction histidine kinase, hybrid-type, ethylene sensor
IPR014763 DNA mismatch repair protein, N-terminal
IPR015434 Post Meiotic Segregation 2
IPR015566 Molecular chaperone, heat shock protein, endoplasmin
IPR016380 Signal transduction histidine kinase, nitrate/nitrite-sensing
IPR016381 Signal transduction histidine kinase, DegS
IPR016781 Anti-sigma regulatory factor, PmgA, predicted
IPR017171 Signal transduction histidine kinase, MctS
IPR017202 Signal transduction histidine kinase, LiaS
IPR017204 Signal transduction histidine kinase, STH3221, predicted
IPR017205 Signal transduction histidine kinase, ChrS
IPR017206 Signal transduction histidine kinase, hybrid-type, BC3207, predicted
IPR020667 DNA mismatch repair protein, MutL
Contains IPR014762 DNA mismatch repair, conserved site
IPR019805 Heat shock protein Hsp90, conserved site
GO Term annotationHelp
Function GO:0005524 ATP binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This domain is found in several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases [1], heat shock protein HSP90 [2, 3, 4], phytochrome-like ATPases and DNA mismatch repair proteins. The fold of this domain consists of two layers, alpha/beta, which contains an 8-stranded mixed beta-sheet.

More information about this protein can be found at Protein of the Month: DNA Topoisomerase [5].

Structural linksHelp
PDB - click here
Database linksHelp
PANDIT: PF02518
Blocks: IPB003594
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003594 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O55028 [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial

P02828 Heat shock protein 83

P02829 ATP-dependent molecular chaperone HSP82

P07900 Heat shock protein HSP 90-alpha

P34534 Putative DNA topoisomerase 2, mitochondrial

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001154 DNA topoisomerase II, eukaryotic-type
IPR001241 DNA topoisomerase, type IIA, subunit B or N-terminal
IPR020568 Ribosomal protein S5 domain 2-type fold
IPR013506 DNA topoisomerase, type IIA, subunit B, region 2
IPR019805 Heat shock protein Hsp90, conserved site
IPR005467 Signal transduction histidine kinase, core
IPR003594 ATPase-like, ATP-binding domain
IPR020575 Heat shock protein Hsp90, N-terminal
IPR020576 Heat shock protein Hsp90, C-terminal
IPR013760 DNA topoisomerase, type IIA, central
IPR018522 DNA topoisomerase, type IIA, conserved site
IPR013757 DNA topoisomerase, type IIA, subunit A, alpha-helical
IPR018955 Branched-chain alpha-ketoacid dehydrogenase kinase/Pyruvate dehydrogenase kinase, mitochondrial
IPR013759 DNA topoisomerase, type IIA, subunit B or N-terminal, alpha-beta
IPR002205 DNA topoisomerase, type IIA, subunit A or C-terminal
IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup
IPR001404 Chaperone protein htpG
IPR004358 Signal transduction histidine kinase-related protein, C-terminal
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Bellon S, Parsons JD, Wei Y, Hayakawa K, Swenson LL, Charifson PS, Lippke JA, Aldape R, Gross CH.
Crystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase.
Antimicrob. Agents Chemother. 48 1856-64 2004 [PubMed: 15105144]
http://dx.doi.org/10.1128/AAC.48.5.1856-1864.2004
2. Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT.
Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone.
J. Biol. Chem. 279 46162-71 2004 [PubMed: 15292259]
http://dx.doi.org/10.1074/jbc.M405253200
3. Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH.
The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37).
Cell 116 87-98 2004 [PubMed: 14718169]
http://dx.doi.org/10.1016/S0092-8674(03)01027-4
4. Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, Drysdale M, Collier A, Massey A, Davies N, Fink A, Fromont C, Aherne W, Boxall K, Sharp S, Workman P, Hubbard RE.
Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms.
Chem. Biol. 11 775-85 2004 [PubMed: 15217611]
http://dx.doi.org/10.1016/j.chembiol.2004.03.033
5. McDowall J.
Protein of the Month: DNA Topoisomerase.
2006

Additional ReadingHelp
Brough PA, Aherne W, Barril X, Borgognoni J, Boxall K, Cansfield JE, Cheung KM, Collins I, Davies NG, Drysdale MJ, Dymock B, Eccles SA, Finch H, Fink A, Hayes A, Howes R, Hubbard RE, James K, Jordan AM, Lockie A, Martins V, Massey A, Matthews TP, McDonald E, Northfield CJ, Pearl LH, Prodromou C, Ray S, Raynaud FI, Roughley SD, Sharp SY, Surgenor A, Walmsley DL, Webb P, Wood M, Workman P, Wright L.
4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer.
J. Med. Chem. 51 2008 196-218 [PubMed: 18020435]
http://dx.doi.org/10.1021/jm701018h
Zhao X, Copeland DM, Soares AS, West AH.
Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog.
J. Mol. Biol. 375 2008 1141-51 [PubMed: 18076904]
http://dx.doi.org/10.1016/j.jmb.2007.11.045
Congreve M, Chessari G, Tisi D, Woodhead AJ.
Recent developments in fragment-based drug discovery.
J. Med. Chem. 51 2008 3661-80 [PubMed: 18457385]
http://dx.doi.org/10.1021/jm8000373
Lin Z, Ho CW, Grierson D.
AtTRP1 encodes a novel TPR protein that interacts with the ethylene receptor ERS1 and modulates development in Arabidopsis.
J. Exp. Bot. 60 2009 3697-714 [PubMed: 19567478]
http://dx.doi.org/10.1093/jxb/erp209
Green T, Grigorian A, Klyuyeva A, Tuganova A, Luo M, Popov KM.
Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2.
J. Biol. Chem. 283 2008 15789-98 [PubMed: 18387944]
http://dx.doi.org/10.1074/jbc.M800311200
Martin CJ, Gaisser S, Challis IR, Carletti I, Wilkinson B, Gregory M, Prodromou C, Roe SM, Pearl LH, Boyd SM, Zhang MQ.
Molecular characterization of macbecin as an Hsp90 inhibitor.
J. Med. Chem. 51 2008 2853-7 [PubMed: 18357975]
http://dx.doi.org/10.1021/jm701558c
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InterPro 23.1