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Conserved domains on  [gi|2027880700|ref|YP_010050588|]
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dUTPase [Arthrobacter phage Wawa]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 173-304 5.50e-32

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: 115.88  E-value: 5.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 173 EVQLPTRAYSDDAGLDLF--VTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRGEL 248
Cdd:COG0756    10 DAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGItLLNsPGTIDSDYRGEI 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 249 FSGVQNMTSKPVHVEAGERIAQLIIigngTR--QIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:COG0756    90 KVILINLGDEPFTIERGDRIAQLVI----APvvQAEFEEVEELDETERGAGGFGSTGR 143
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 173-304 5.50e-32

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: 115.88  E-value: 5.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 173 EVQLPTRAYSDDAGLDLF--VTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRGEL 248
Cdd:COG0756    10 DAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGItLLNsPGTIDSDYRGEI 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 249 FSGVQNMTSKPVHVEAGERIAQLIIigngTR--QIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:COG0756    90 KVILINLGDEPFTIERGDRIAQLVI----APvvQAEFEEVEELDETERGAGGFGSTGR 143
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 172-303 1.11e-30

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 112.00  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 172 AEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNPGIIDAGYRGELFSG 251
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSG-LAAKGLIVVPGVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2027880700 252 VQNMTSKPVHVEAGERIAQLIIIGNGTRQIEPVLvpELNSHARGKNGFGSSG 303
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVE--TLDNTDRGDGGFGSSG 129
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 163-304 9.64e-27

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: 101.93  E-value: 9.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 163 TLQFAPVDgAEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKG--LLVNPGII 240
Cdd:TIGR00576   1 KLKFVKLS-PNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027880700 241 DAGYRGELFSGVQNMTSKPVHVEAGERIAQLII--IGngtRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:TIGR00576  80 DADYRGEIKVILINLGKEDFTVKKGDRIAQLVVekIV---TEVEFEEVEELDETERGEGGFGSTGV 142
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 185-273 1.55e-24

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: 94.48  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 185 AGLDLFVTED---TWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKkGLLV-NPGIIDAGYRGELFSGVQNMTSKPV 260
Cdd:cd07557     1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVhNAGVIDPGYRGEITLELYNLGPEPV 79

                          90
                  ....*....|...
gi 2027880700 261 HVEAGERIAQLII 273
Cdd:cd07557    80 VIKKGDRIAQLVF 92
dut PRK00601
dUTP diphosphatase;
171-304 1.40e-22

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 91.38  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 171 GAEVQLPTRAYSDDAGLDLFVTEDTWV--PANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRG 246
Cdd:PRK00601   14 GKEFPLPAYATEGSAGLDLRACLDEPVtlAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIvLGNlPGTIDSDYRG 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 247 ELFSGVQNMTSKPVHVEAGERIAQLIIIgnGTRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PRK00601   94 ELKVSLWNRGQEPFTIEPGERIAQLVIV--PVVQAEFEEVEEFDETERGAGGFGSTGR 149
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 173-304 5.50e-32

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: 115.88  E-value: 5.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 173 EVQLPTRAYSDDAGLDLF--VTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRGEL 248
Cdd:COG0756    10 DAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGItLLNsPGTIDSDYRGEI 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 249 FSGVQNMTSKPVHVEAGERIAQLIIigngTR--QIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:COG0756    90 KVILINLGDEPFTIERGDRIAQLVI----APvvQAEFEEVEELDETERGAGGFGSTGR 143
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 172-303 1.11e-30

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 112.00  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 172 AEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNPGIIDAGYRGELFSG 251
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSG-LAAKGLIVVPGVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2027880700 252 VQNMTSKPVHVEAGERIAQLIIIGNGTRQIEPVLvpELNSHARGKNGFGSSG 303
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVE--TLDNTDRGDGGFGSSG 129
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 163-304 9.64e-27

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: 101.93  E-value: 9.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 163 TLQFAPVDgAEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKG--LLVNPGII 240
Cdd:TIGR00576   1 KLKFVKLS-PNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027880700 241 DAGYRGELFSGVQNMTSKPVHVEAGERIAQLII--IGngtRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:TIGR00576  80 DADYRGEIKVILINLGKEDFTVKKGDRIAQLVVekIV---TEVEFEEVEELDETERGEGGFGSTGV 142
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 185-273 1.55e-24

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: 94.48  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 185 AGLDLFVTED---TWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKkGLLV-NPGIIDAGYRGELFSGVQNMTSKPV 260
Cdd:cd07557     1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVhNAGVIDPGYRGEITLELYNLGPEPV 79

                          90
                  ....*....|...
gi 2027880700 261 HVEAGERIAQLII 273
Cdd:cd07557    80 VIKKGDRIAQLVF 92
dut PRK00601
dUTP diphosphatase;
171-304 1.40e-22

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 91.38  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 171 GAEVQLPTRAYSDDAGLDLFVTEDTWV--PANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRG 246
Cdd:PRK00601   14 GKEFPLPAYATEGSAGLDLRACLDEPVtlAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIvLGNlPGTIDSDYRG 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 247 ELFSGVQNMTSKPVHVEAGERIAQLIIIgnGTRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PRK00601   94 ELKVSLWNRGQEPFTIEPGERIAQLVIV--PVVQAEFEEVEEFDETERGAGGFGSTGR 149
PLN02547 PLN02547
dUTP pyrophosphatase
 176-303 8.59e-19

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 81.38  E-value: 8.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGLLVNPGIIDAGYRGELFSGVQNM 255
Cdd:PLN02547   28 LPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVIDADYRGPVGVILFNH 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2027880700 256 TSKPVHVEAGERIAQLIIigngtRQI---EPVLVPELNSHARGKNGFGSSG 303
Cdd:PLN02547  108 SDVDFEVKVGDRIAQLIL-----EKIvtpEVVEVEDLDATVRGAGGFGSTG 153
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 181-304 3.65e-18

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 79.78  E-value: 3.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 181 YSDDAGLDLFVTEDTWVPANGFVDIRSHIKV----------QLPDWSWgFLVGRSSTLRKKGLLVNP-GIIDAGYRGELF 249
Cdd:PTZ00143   23 HEGDSGLDLFIVKDQTIKPGETAFIKLGIKAaafqkdedgsDGKNVSW-LLFPRSSISKTPLRLANSiGLIDAGYRGELI 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2027880700 250 SGVQNMTSKPVHVEAGERIAQLIIIgNGtRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PTZ00143  102 AAVDNIKDEPYTIKKGDRLVQLVSF-DG-EPITFELVDELDETTRGEGGFGSTGR 154
PHA03094 PHA03094
dUTPase; Provisional
 176-303 1.02e-15

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 72.88  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGLLVNPGIIDAGYRGELFSGVQNM 255
Cdd:PHA03094   17 IPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVIDEDYRGNIGVIFINN 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2027880700 256 TSKPVHVEAGERIAQLIIIGNGTRQIEPVLvpELNSHARGKNGFGSSG 303
Cdd:PHA03094   97 GKCTFNIKTGDRIAQIIFERIEYPELKEVQ--SLDSTDRGDQGFGSSG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 176-303 1.03e-15

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 73.09  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGLLVNPGIIDAGYRGELFSGVQNM 255
Cdd:PHA02703   25 IPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDADYRGNVGVVLFNF 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027880700 256 TSKPVHVEAGERIAQLIIigngTRQIEPVL--VPELNSHARGKNGFGSSG 303
Cdd:PHA02703  105 GHNDFEVKKGDRIAQLIC----ERAAFPAVeeVACLDDTDRGAGGFGSTG 150
dut PRK13956
dUTP diphosphatase;
176-304 1.30e-14

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 69.82  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVNP-GIIDAGY------RGE 247
Cdd:PRK13956   18 LPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLvLINSvGVIDGDYygnpanEGH 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027880700 248 LFSGVQNMTSKPVHVEAGERIAQLIIIgngtrqiePVLVPElNSHARGK--NGFGSSGK 304
Cdd:PRK13956   98 IFAQMKNITDQEVVLEVGERIVQGVFM--------PFLIAD-GDQADGErtGGFGSTGK 147
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 192-272 3.53e-11

dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440481  Cd Length: 180  Bit Score: 60.99  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 192 TEDTWV-PANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKkGLLVNP--GIIDAGYRGELFSGVQNMTSKPVHVEAGERI 268
Cdd:COG0717    66 PGDGFIlPPGEFYLARTLEYVRLPDDLVAFLEGRSSLARL-GLFVHTtaGVIDPGFEGRITLELSNTGPLPIKLYPGMRI 144


                  ....
gi 2027880700 269 AQLI 272
Cdd:COG0717   145 AQLV 148
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 197-272 1.26e-09

deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274062  Cd Length: 179  Bit Score: 56.55  E-value: 1.26e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 197 VPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNP--GIIDAGYRGELFSGVQNMTSKPVHVEAGERIAQLI 272
Cdd:TIGR02274  73 IPPGEFALATTLEYVKLPDDVVGFLEGRSS-LARLGLFIHVtaGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLV 149
PHA03130 PHA03130
dUTPase; Provisional
 176-275 3.75e-08

dUTPase; Provisional


Pssm-ID: 222995 [Multi-domain]  Cd Length: 368  Bit Score: 54.14  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAysDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWG--FLVGRSStLRKKGLLVNPGIIDAGyRGELFSgVQ 253
Cdd:PHA03130  207 LPKRA--EDAGIDIVVHKRVEVPAGGTVVIQPSLRVLLAAGGPEayYVLGRSS-LNARGVLVTPTRWLPG-RQCAFS-VH 281

                          90       100
                  ....*....|....*....|..
gi 2027880700 254 NMTSKPVHVEAGERIAQLIIIG 275
Cdd:PHA03130  282 NITGAPVTLEAGSKVAQLLVAG 303
PHA03124 PHA03124
dUTPase; Provisional
 182-304 4.73e-07

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 50.71  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 182 SDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNP-GIIDAGYRGelFSgVQNMTSKPV 260
Cdd:PHA03124  288 AEDAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSS-MNLKGLLVDPeHVQDDDWIS--FN-ITNIRDAAA 363

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2027880700 261 HVEAGERIAQLIIIGNGT-----------RQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PHA03124  364 FFHAGDRIAQLIALEDKLeflgepdalpwKIVNSVQDEKKNLSSRGDGGFGSSGK 418
PHA03123 PHA03123
dUTPase; Provisional
 183-281 2.34e-06

dUTPase; Provisional


Pssm-ID: 165395 [Multi-domain]  Cd Length: 402  Bit Score: 48.45  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 183 DDAGLDLFVTEDTWVPANGFvdirshIKVQLP---DWSW------GFLVGRSSTLRKkGLLVNPGIIDAGYRGELFsgVQ 253
Cdd:PHA03123  243 EDAGYDICAPFEITLKANEF------IKITLPfiqDLDLnhpnidAYIFGRSSKNRI-GIIVCPTAWIAGEHCEFY--IF 313

                          90       100
                  ....*....|....*....|....*...
gi 2027880700 254 NMTSKPVHVEAGERIAQLIIIGNGTRQI 281
Cdd:PHA03123  314 NATGDDIIIKPGDKIAQVLLIDHNNQSI 341
PHA03127 PHA03127
dUTPase; Provisional
 133-303 3.10e-06

dUTPase; Provisional


Pssm-ID: 222993 [Multi-domain]  Cd Length: 322  Bit Score: 48.07  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 133 WQFATIEAMDWLADQKLPSFAKGNPARERktLQFAPVD-----GAEVQLPTRAY-----SDDAGLDLFVTEDTWVPANGF 202
Cdd:PHA03127  115 WAPPCIETIPEAGLALRLTLARLAKTTPR--LAACDDTaragqGAGVEVPFFETfapkrDEDAGYDIAMPYTAVLAPGEN 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 203 VDIRSHIkVQLPD--WSWGFLVGRSStLRKKGLLVNPGIIDAGYRGELFsgVQNMTSKPVHVEAGERIAQLIIIgngtrq 280
Cdd:PHA03127  193 LHVRLPV-AYAAGahAAAPYVFGRSS-LNLRGIVVLPTAWPPGEPCRFV--IRNVTQEPVVAAAGQRVAQLLLL------ 262

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027880700 281 IEPV--LVPELNSH----------------------------------ARGKNGFGSSG 303
Cdd:PHA03127  263 EEPLewLPTELNDRepfpttpraappapmahrlrwrfvadfaavapssARGDRGFGSTG 321
dut PHA01707
2'-deoxyuridine 5'-triphosphatase
 211-287 4.08e-05

2'-deoxyuridine 5'-triphosphatase


Pssm-ID: 107053  Cd Length: 158  Bit Score: 43.00  E-value: 4.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027880700 211 VQLPDWSWGFLVGRSsTLRKKGLLVNPGIIDAGYRGELFSGVQNmTSKPVHVEAGERIAQLIIigngTRQIEPVLVP 287
Cdd:PHA01707   71 IKLPNDIIAFCNLRS-TFARKGLLIPPTIVDAGFEGQLTIELVG-SSIPVKLKSGERFLHLIF----ARTLTPVEKP 141
PHA03131 PHA03131
dUTPase; Provisional
 181-274 3.51e-04

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 41.52  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 181 YSDDAGLDLFVTEDTWVP---ANGF-------VDIRSHIKVqlpdwswgfLVGRSStLRKKGLLVNPgiidAGYRGELFS 250
Cdd:PHA03131  129 YPDDAGFDVSLPQDLVIFpttTFTFtlslccpPISPHFVPV---------IFGRSG-LASKGLTVKP----TKWRRSGLQ 194

                          90       100
                  ....*....|....*....|....*
gi 2027880700 251 -GVQNMTSKPVHVEAGERIAQLIII 274
Cdd:PHA03131  195 lKLYNYTDETIFLPAGSRICQVVFM 219
PHA03129 PHA03129
dUTPase; Provisional
 178-274 3.03e-03

dUTPase; Provisional


Pssm-ID: 222994 [Multi-domain]  Cd Length: 436  Bit Score: 39.09  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 178 TRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWS---WGFlvGRSStLRKKGLLVNPGIIDAGyrGELFSGVQN 254
Cdd:PHA03129  281 NPKRLEDAGYDIPAPRDIELEPLSSTTIKIQQRYNCKDSSvipCIF--GRSS-MNLRGLIVLPSRWLPN--SWLTLTICN 355

                          90       100
                  ....*....|....*....|
gi 2027880700 255 MTSKPVHVEAGERIAQLIII 274
Cdd:PHA03129  356 LTEKTVFIKAGDRIAQLLLV 375
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 211-274 8.78e-03

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 36.47  E-value: 8.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027880700 211 VQLPDWSWGFLVGRSSTLRKkGLLVNPGIIDAGY--RGELFSGVQNmtSKPVHVEAGERIAQLIII 274
Cdd:PRK02253   87 VNIPEDHVGFAYPRSSLLRN-GCTLETAVWDAGYegRGEGLLVVHN--PHGIRLERGARIAQLVFA 149
 
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.
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