1DUP,1SJN,1F7O,1Q5H,2HXD,1XS6,2QXX,2ZDC,2R9Q,1VYQ,2BAZ,3ECY,2P9O,3F4F,2BT1,2BT1


Conserved Protein Domain Family
trimeric_dUTPase

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cd07557: trimeric_dUTPase 
Click on image for an interactive view with Cn3D
Trimeric dUTP diphosphatases
Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.
Statistics
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PSSM-Id: 143638
View PSSM: cd07557
Aligned: 292 rows
Threshold Bit Score: 53.6521
Threshold Setting Gi: 210464478
Created: 30-Sep-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitetrimer
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:active sites are at the trimer interface, each monomer is part of two active sites
  • Structure:1XS6; Escherichia coli dCTP deaminase with bound dUTP, contacts at 4A
    View structure with Cn3D
  • Structure:1SJN; Mycobacterium tuberculosis dUTPase with bound Mg and alpha,beta-imido-dUTP, contacts at 4A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                        
1DUP_A        29 AGLDLRACLnd--------------------------------------aVELAPgDTTLVPTGLAIHiadpslAAMMLP 70  Escherichia coli
1XS6_A        31 ATVDVRLGNkfrtfrghtaafidlsgpkdevsaaldrvmsdeivldegeaFYLHPgELALAVTLESVTlpa-dlVGWLDG 109 Escherichia coli
NP_111155     30 NGYDVRVESilade-------------------------------kevdeTIVGTmKHFLVSTLEVLRlpe-nvIANIWI 77  Thermoplasma vo...
CAC11737      47 NGYDLRVDAidveg-------------------------------rqyseFEIGKnVHFLVSTIEILKipd-dvVGMIWT 94  Thermoplasma ac...
YP_022908     29 NGYDLRINDii-------------------------------------pgNDIKKgTVFFVSSYEEIKlpd-niIGLLFI 70  Picrophilus tor...
YP_002623123  35 VGYDLRVGQngfswnnkr-----------------------evdierdggIEIEPmDTVVIETLESITlsk-evGATIHA 90  Microcoleus cht...
ZP_04291390   30 GSINLTASKlawrvsdk-------------------------nsavkdniIEIPPnDTVCIYTNEAIWvsk-wiGGTYHP 83  Bacillus cereus...
YP_002376053  30 ASYNLTASKfawslkeks------------------------qidtadgkIIIPPrDTALIETEEVIWvse-kiSGTYHS 84  Cyanothece sp. ...
YP_001801800  30 SSYNLTASQlawdlstrk-----------------------siydssqnkITIQPkTTALIETNESIWvsq-kiSGTYYS 85  Cyanothece sp. ...
YP_001029520  30 SSYDLRSAEd----------------------------------------ITITKgELTLVPTMEFVSlpe-dlCATLWG 68  Methanocorpuscu...
Feature 1        ###              ###  #   ##                        
1DUP_A        71 RSGLghkhGIVLgnlvgLIDSDYQGQLMISVWNRgqdSFTIQPGERIAQMIF 122 Escherichia coli
1XS6_A       110 RSSLar-lGLMVhvtahRIDPGWSGCIVLAFYNSgklPLALRPGMLIGALSF 160 Escherichia coli
NP_111155     78 RSSYar-rGVIGsf--gTIDAGYHGSLTLSFFNAg-pDLHISRGDRIAQVIF 125 Thermoplasma volcanium GSS1
CAC11737      95 RSSFar-kGIFGsf--gAIDAGYHGNLTLSFFNAg-sAVNLRRGERIAQIVF 142 Thermoplasma acidophilum
YP_022908     71 RSSFar-kGIFGsf--gVVDAGYMGNLTLSFYNAl-nDVKIERYERIVQIVF 118 Picrophilus torridus DSM 9790
YP_002623123  91 MATRvtaqGLSHis--tTVDPGWTGKLLISCHNYrdsPVELRQGDPLCTICF 140 Microcoleus chthonoplastes PCC 7420
ZP_04291390   84 RVSLvs-kGLGHis--tTLDPGWAGLSLIAVNNPtnkPVSIIVGESLVSIML 132 Bacillus cereus R309803
YP_002376053  85 RVSIvs-qGIGHin--tTLDPDYLGSSLIALHNNtdvSIELIVGKPFVTLTF 133 Cyanothece sp. PCC 7424
YP_001801800  86 RVREvs-kGTGHis--tTLDPNYIGCSLIALRNHsqsPIEITPETDPFVTLI 134 Cyanothece sp. ATCC 51142
YP_001029520  69 RSSFgr-kGVVLga--gYIDPGFRGNLTLCMANYgpeDIQVTKGMRVVQMLI 117 Methanocorpusculum labreanum Z

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