NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446563560|ref|WP_000640906|]
View 

dUTP diphosphatase [Escherichia coli]

Protein Classification

dUTP diphosphatase( domain architecture ID 10786453)

dUTP diphosphatase is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA

EC:  3.6.1.23
SCOP:  4002970

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
4-147 1.96e-55

dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis


:

Pssm-ID: 440519 [Multi-domain]  Cd Length: 143  Bit Score: 170.97  E-value: 1.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   4 VKVKRLHPAAKLPAYATSGSAAMD-----FEAVEIKPcvdsnGAISSswwVYTGLAMEIPPGWCLKLYPRSGLGCKKHTR 78
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDlraalDEPVTLKP-----GERAL---VPTGLAIALPPGYEAQVRPRSGLALKHGIT 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446563560  79 LANCVGIIDSDYRGEIMAKLITDpGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:COG0756   74 LLNSPGTIDSDYRGEIKVILINL-GDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGST 141
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
4-147 1.96e-55

dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440519 [Multi-domain]  Cd Length: 143  Bit Score: 170.97  E-value: 1.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   4 VKVKRLHPAAKLPAYATSGSAAMD-----FEAVEIKPcvdsnGAISSswwVYTGLAMEIPPGWCLKLYPRSGLGCKKHTR 78
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDlraalDEPVTLKP-----GERAL---VPTGLAIALPPGYEAQVRPRSGLALKHGIT 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446563560  79 LANCVGIIDSDYRGEIMAKLITDpGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:COG0756   74 LLNSPGTIDSDYRGEIKVILINL-GDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGST 141
dut PRK00601
dUTP diphosphatase;
4-147 2.30e-46

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 148.39  E-value: 2.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   4 VKVKRLHPAAKLPAYATSGSAAMDFEAVEIKPCVDSNGAISsswWVYTGLAMEIPPGWCLKLYPRSGLGCKKHTRLANCV 83
Cdd:PRK00601   8 ILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERA---LVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNLP 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446563560  84 GIIDSDYRGEIMAKLItDPGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:PRK00601  85 GTIDSDYRGELKVSLW-NRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGST 147
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
3-147 1.44e-45

deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 273149 [Multi-domain]  Cd Length: 142  Bit Score: 145.84  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560    3 YVKVKRLHPAAKLPAYATSGSAAMD---FEAVEIKPcvDSNGAISsswwvyTGLAMEIPPGWCLKLYPRSGLGCKKHTRL 79
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDlraAEDVTIPP--GERALVP------TGIAIELPDGYYGRVAPRSGLALKHGVTI 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446563560   80 ANCVGIIDSDYRGEIMAKLItDPGGEGVCLKPGMAVMQGIFERVEQ-VSLVEVEELNETERGAGGFGST 147
Cdd:TIGR00576  73 DNSPGVIDADYRGEIKVILI-NLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGST 140
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
13-147 2.04e-21

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 83.88  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   13 AKLPAYATSGSAAMDFEA---VEIKPcvdsNGAISsswwVYTGLAMEIPPGWCLKLYPRSGLGcKKHtrLANCVGIIDSD 89
Cdd:pfam00692   3 AEIPTPGSPGDAGYDLYApydLTVKP----GGTVL----VPTDISIPLPDGTYGRIFPRSGLA-AKG--LIVVPGVIDSD 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446563560   90 YRGEIMAKlITDPGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:pfam00692  72 YRGEVKVV-LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSS 128
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
23-120 1.13e-15

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.


Pssm-ID: 143638 [Multi-domain]  Cd Length: 92  Bit Score: 67.90  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560  23 SAAMDFEAVEIKPcvdsNGAISsswwVYTGLAMEIPPGWCLKLYPRSGLGcKKHTRLANcVGIIDSDYRGEIMAkLITDP 102
Cdd:cd07557    6 RLGEDFEGIVLPP----GETVL----VPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITL-ELYNL 74
                         90
                 ....*....|....*...
gi 446563560 103 GGEGVCLKPGMAVMQGIF 120
Cdd:cd07557   75 GPEPVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
4-147 1.96e-55

dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440519 [Multi-domain]  Cd Length: 143  Bit Score: 170.97  E-value: 1.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   4 VKVKRLHPAAKLPAYATSGSAAMD-----FEAVEIKPcvdsnGAISSswwVYTGLAMEIPPGWCLKLYPRSGLGCKKHTR 78
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDlraalDEPVTLKP-----GERAL---VPTGLAIALPPGYEAQVRPRSGLALKHGIT 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446563560  79 LANCVGIIDSDYRGEIMAKLITDpGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:COG0756   74 LLNSPGTIDSDYRGEIKVILINL-GDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGST 141
dut PRK00601
dUTP diphosphatase;
4-147 2.30e-46

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 148.39  E-value: 2.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   4 VKVKRLHPAAKLPAYATSGSAAMDFEAVEIKPCVDSNGAISsswWVYTGLAMEIPPGWCLKLYPRSGLGCKKHTRLANCV 83
Cdd:PRK00601   8 ILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERA---LVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNLP 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446563560  84 GIIDSDYRGEIMAKLItDPGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:PRK00601  85 GTIDSDYRGELKVSLW-NRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGST 147
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
3-147 1.44e-45

deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 273149 [Multi-domain]  Cd Length: 142  Bit Score: 145.84  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560    3 YVKVKRLHPAAKLPAYATSGSAAMD---FEAVEIKPcvDSNGAISsswwvyTGLAMEIPPGWCLKLYPRSGLGCKKHTRL 79
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDlraAEDVTIPP--GERALVP------TGIAIELPDGYYGRVAPRSGLALKHGVTI 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446563560   80 ANCVGIIDSDYRGEIMAKLItDPGGEGVCLKPGMAVMQGIFERVEQ-VSLVEVEELNETERGAGGFGST 147
Cdd:TIGR00576  73 DNSPGVIDADYRGEIKVILI-NLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGST 140
PLN02547 PLN02547
dUTP pyrophosphatase
5-147 2.71e-24

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 92.16  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   5 KVKRLHPAAKLPAYATSGSAAMDFEAVEiKPCVDSNG-AIssswwVYTGLAMEIPPGWCLKLYPRSGLGCKKHTRLAncV 83
Cdd:PLN02547  18 RVKKLSEKATLPSRGSALAAGYDLSSAY-DTVVPARGkAL-----VPTDLSIAIPEGTYARIAPRSGLAWKHSIDVG--A 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446563560  84 GIIDSDYRGEIMAKLItDPGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:PLN02547  90 GVIDADYRGPVGVILF-NHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGST 152
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
13-147 2.04e-21

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 83.88  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   13 AKLPAYATSGSAAMDFEA---VEIKPcvdsNGAISsswwVYTGLAMEIPPGWCLKLYPRSGLGcKKHtrLANCVGIIDSD 89
Cdd:pfam00692   3 AEIPTPGSPGDAGYDLYApydLTVKP----GGTVL----VPTDISIPLPDGTYGRIFPRSGLA-AKG--LIVVPGVIDSD 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446563560   90 YRGEIMAKlITDPGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:pfam00692  72 YRGEVKVV-LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSS 128
PHA02703 PHA02703
ORF007 dUTPase; Provisional
4-161 2.27e-20

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 82.34  E-value: 2.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   4 VKVKRLHPAAKLPAYATSGSAAMDFeaVEIKPCVDSNGAissSWWVYTGLAMEIPPGWCLKLYPRSGLGCKKHTRLAncV 83
Cdd:PHA02703  14 LRVVRLSPNATIPTRGSPGAAGLDL--CSACDCIVPAGC---RCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVG--A 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446563560  84 GIIDSDYRGEIMAKLItDPGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGSTSEDRVEIKRTPLQY 161
Cdd:PHA02703  87 GVIDADYRGNVGVVLF-NFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGSGACEGCGDTVWY 163
PHA03094 PHA03094
dUTPase; Provisional
3-147 5.39e-20

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 80.58  E-value: 5.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560   3 YVKVKRLHPAAKLPAYATSGSAAMD-FEAVE--IKPcvdsngaiSSSWWVYTGLAMEIPPGWCLKLYPRSGLGckkhtrL 79
Cdd:PHA03094   5 PVRCVKLSNFAKIPTRSSPKSAGYDlYSAYDytVPP--------KERILVKTDISLSIPKFCYGRIAPRSGLS------L 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446563560  80 ANCV----GIIDSDYRGEIMAKLITDpGGEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAGGFGST 147
Cdd:PHA03094  71 NYGIdiggGVIDEDYRGNIGVIFINN-GKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSS 141
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
65-148 3.43e-17

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 73.61  E-value: 3.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560  65 LYPRSGLGcKKHTRLANCVGIIDSDYRGEIMAKL--ITDpggEGVCLKPGMAVMQGIFERVEQVSLVEVEELNETERGAG 142
Cdd:PTZ00143  72 LFPRSSIS-KTPLRLANSIGLIDAGYRGELIAAVdnIKD---EPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEG 147

                 ....*.
gi 446563560 143 GFGSTS 148
Cdd:PTZ00143 148 GFGSTG 153
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
23-120 1.13e-15

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.


Pssm-ID: 143638 [Multi-domain]  Cd Length: 92  Bit Score: 67.90  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560  23 SAAMDFEAVEIKPcvdsNGAISsswwVYTGLAMEIPPGWCLKLYPRSGLGcKKHTRLANcVGIIDSDYRGEIMAkLITDP 102
Cdd:cd07557    6 RLGEDFEGIVLPP----GETVL----VPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITL-ELYNL 74
                         90
                 ....*....|....*...
gi 446563560 103 GGEGVCLKPGMAVMQGIF 120
Cdd:cd07557   75 GPEPVVIKKGDRIAQLVF 92
dut PRK13956
dUTP diphosphatase;
15-147 4.20e-10

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 54.80  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563560  15 LPAYATSGSAAMDF---EAVEIKPcvdsnGAISsswWVYTGLAMEIPPGWCLKLYPRSGLGCKKHTRLANCVGIIDSDY- 90
Cdd:PRK13956  18 LPKRETAHAAGYDLkvaERTVIAP-----GEIK---LVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYy 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446563560  91 -----RGEIMAKL--ITDpggEGVCLKPGMAVMQGIFerveqVSLVEVEELNETERGAGGFGST 147
Cdd:PRK13956  90 gnpanEGHIFAQMknITD---QEVVLEVGERIVQGVF-----MPFLIADGDQADGERTGGFGST 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH