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: 17-Jan-2013
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:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
1DUP_A        29 AGLDLRACLnd--------------------------------------aVELAPgDTTLVPTGLAIHiadpslAAMMLP 70
1XS6_A        31 ATVDVRLGNkfrtfrghtaafidlsgpkdevsaaldrvmsdeivldegeaFYLHPgELALAVTLESVTlpa-dlVGWLDG 109
gi 13541467   30 NGYDVRVESilade-------------------------------kevdeTIVGTmKHFLVSTLEVLRlpe-nvIANIWI 77
gi 10639765   47 NGYDLRVDAidveg-------------------------------rqyseFEIGKnVHFLVSTIEILKipd-dvVGMIWT 94
gi 48477202   29 NGYDLRINDii-------------------------------------pgNDIKKgTVFFVSSYEEIKlpd-niIGLLFI 70
gi 224407693  35 VGYDLRVGQngfswnnkr-----------------------evdierdggIEIEPmDTVVIETLESITlsk-evGATIHA 90
gi 229163439  30 GSINLTASKlawrvsdk-------------------------nsavkdniIEIPPnDTVCIYTNEAIWvsk-wiGGTYHP 83
gi 218437724  30 ASYNLTASKfawslkeks------------------------qidtadgkIIIPPrDTALIETEEVIWvse-kiSGTYHS 84
gi 172035299  30 SSYNLTASQlawdlstrk-----------------------siydssqnkITIQPkTTALIETNESIWvsq-kiSGTYYS 85
gi 124484904  30 SSYDLRSAEd----------------------------------------ITITKgELTLVPTMEFVSlpe-dlCATLWG 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
Feature 1        ###              ###  #   ##                        
1DUP_A        71 RSGLghkhGIVLgnlvgLIDSDYQGQLMISVWNRgqdSFTIQPGERIAQMIF 122
1XS6_A       110 RSSLar-lGLMVhvtahRIDPGWSGCIVLAFYNSgklPLALRPGMLIGALSF 160
gi 13541467   78 RSSYar-rGVIGsf--gTIDAGYHGSLTLSFFNAg-pDLHISRGDRIAQVIF 125
gi 10639765   95 RSSFar-kGIFGsf--gAIDAGYHGNLTLSFFNAg-sAVNLRRGERIAQIVF 142
gi 48477202   71 RSSFar-kGIFGsf--gVVDAGYMGNLTLSFYNAl-nDVKIERYERIVQIVF 118
gi 224407693  91 MATRvtaqGLSHis--tTVDPGWTGKLLISCHNYrdsPVELRQGDPLCTICF 140
gi 229163439  84 RVSLvs-kGLGHis--tTLDPGWAGLSLIAVNNPtnkPVSIIVGESLVSIML 132
gi 218437724  85 RVSIvs-qGIGHin--tTLDPDYLGSSLIALHNNtdvSIELIVGKPFVTLTF 133
gi 172035299  86 RVREvs-kGTGHis--tTLDPNYIGCSLIALRNHsqsPIEITPETDPFVTLI 134
gi 124484904  69 RSSFgr-kGVVLga--gYIDPGFRGNLTLCMANYgpeDIQVTKGMRVVQMLI 117

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