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Conserved domains on  [gi|519010973|ref|WP_020166848|]
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MULTISPECIES: dUTP diphosphatase [Methylotenera]

Protein Classification

dUTP diphosphatase( domain architecture ID 10792031)

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
Gene Ontology:  GO:0046872|GO:0004170

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
4-150 2.08e-95

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 271.65  E-value: 2.08e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   4 SVDLKILDNRLHH--MMPSYATQGSAGLDLRACIEHTQTIQPNETVMIPTGMAIHIDNtYYAALILPRSGLGHKHGIVLG 81
Cdd:PRK00601   3 KIDVKILDPRLGKefPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVLG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519010973  82 NLVGLIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTGKH 150
Cdd:PRK00601  82 NLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
4-150 2.08e-95

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 271.65  E-value: 2.08e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   4 SVDLKILDNRLHH--MMPSYATQGSAGLDLRACIEHTQTIQPNETVMIPTGMAIHIDNtYYAALILPRSGLGHKHGIVLG 81
Cdd:PRK00601   3 KIDVKILDPRLGKefPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVLG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519010973  82 NLVGLIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTGKH 150
Cdd:PRK00601  82 NLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 5-149 4.78e-84

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: 242.62  E-value: 4.78e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   5 VDLKILDNRLhhMMPSYATQGSAGLDLRACIEHTQTIQPNETVMIPTGMAIHIDNTYyAALILPRSGLGHKHGIVLGNLV 84
Cdd:COG0756    2 VKIKRLDEDA--PLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGY-EAQVRPRSGLALKHGITLLNSP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519010973  85 GLIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTGK 149
Cdd:COG0756   79 GTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-149 3.40e-59

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: 180.12  E-value: 3.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973    8 KILDNRLHH--MMPSYATQGSAGLDLRACIEhtQTIQPNETVMIPTGMAIHIDNTYYAaLILPRSGLGHKHGIVLGNLVG 85
Cdd:TIGR00576   1 KLKFVKLSPnaPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPDGYYG-RVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519010973   86 LIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVIVPVVQ-AEFHVVDEFTESDRGEGGFGSTGK 149
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 18-148 4.74e-45

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 143.58  E-value: 4.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   18 MPSYATQGSAGLDLRACIEHTqtIQPNETVMIPTGMAIHIDNTYYAaLILPRSGLGHKHGIVLGnlvGLIDSDYQGQLLV 97
Cdd:pfam00692   5 IPTPGSPGDAGYDLYAPYDLT--VKPGGTVLVPTDISIPLPDGTYG-RIFPRSGLAAKGLIVVP---GVIDSDYRGEVKV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 519010973   98 SCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTG 148
Cdd:pfam00692  79 VLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 27-120 1.60e-26

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: 95.25  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  27 AGLDLRACIEHTQ-TIQPNETVMIPTGMAIHIDNtYYAALILPRSGLGhKHGIVLGNlVGLIDSDYQGQLLVSCWNRGKE 105
Cdd:cd07557    1 AGYDLRLGEDFEGiVLPPGETVLVPTGEAIELPE-GYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 519010973 106 AFILNPMERIAQLVI 120
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
4-150 2.08e-95

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 271.65  E-value: 2.08e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   4 SVDLKILDNRLHH--MMPSYATQGSAGLDLRACIEHTQTIQPNETVMIPTGMAIHIDNtYYAALILPRSGLGHKHGIVLG 81
Cdd:PRK00601   3 KIDVKILDPRLGKefPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVLG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519010973  82 NLVGLIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTGKH 150
Cdd:PRK00601  82 NLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 5-149 4.78e-84

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: 242.62  E-value: 4.78e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   5 VDLKILDNRLhhMMPSYATQGSAGLDLRACIEHTQTIQPNETVMIPTGMAIHIDNTYyAALILPRSGLGHKHGIVLGNLV 84
Cdd:COG0756    2 VKIKRLDEDA--PLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGY-EAQVRPRSGLALKHGITLLNSP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519010973  85 GLIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTGK 149
Cdd:COG0756   79 GTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-149 3.40e-59

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: 180.12  E-value: 3.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973    8 KILDNRLHH--MMPSYATQGSAGLDLRACIEhtQTIQPNETVMIPTGMAIHIDNTYYAaLILPRSGLGHKHGIVLGNLVG 85
Cdd:TIGR00576   1 KLKFVKLSPnaPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPDGYYG-RVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519010973   86 LIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVIVPVVQ-AEFHVVDEFTESDRGEGGFGSTGK 149
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 18-148 4.74e-45

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 143.58  E-value: 4.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   18 MPSYATQGSAGLDLRACIEHTqtIQPNETVMIPTGMAIHIDNTYYAaLILPRSGLGHKHGIVLGnlvGLIDSDYQGQLLV 97
Cdd:pfam00692   5 IPTPGSPGDAGYDLYAPYDLT--VKPGGTVLVPTDISIPLPDGTYG-RIFPRSGLAAKGLIVVP---GVIDSDYRGEVKV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 519010973   98 SCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTG 148
Cdd:pfam00692  79 VLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
PLN02547 PLN02547
dUTP pyrophosphatase
 15-148 2.20e-27

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 99.48  E-value: 2.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  15 HHMMPSYATQGSAGLDLRACIEHTqtIQPNETVMIPTGMAIHIDNTYYAAlILPRSGLGHKHGIVLGnlVGLIDSDYQGQ 94
Cdd:PLN02547  25 KATLPSRGSALAAGYDLSSAYDTV--VPARGKALVPTDLSIAIPEGTYAR-IAPRSGLAWKHSIDVG--AGVIDADYRGP 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 519010973  95 LLVSCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTG 148
Cdd:PLN02547 100 VGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 27-120 1.60e-26

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: 95.25  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  27 AGLDLRACIEHTQ-TIQPNETVMIPTGMAIHIDNtYYAALILPRSGLGhKHGIVLGNlVGLIDSDYQGQLLVSCWNRGKE 105
Cdd:cd07557    1 AGYDLRLGEDFEGiVLPPGETVLVPTGEAIELPE-GYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 519010973 106 AFILNPMERIAQLVI 120
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 24-149 1.03e-20

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 82.47  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  24 QGSAGLDLrACIEhTQTIQPNETVMIPTGMAI----------HIDNTYYaaLILPRSGLGhKHGIVLGNLVGLIDSDYQG 93
Cdd:PTZ00143  24 EGDSGLDL-FIVK-DQTIKPGETAFIKLGIKAaafqkdedgsDGKNVSW--LLFPRSSIS-KTPLRLANSIGLIDAGYRG 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 519010973  94 QLLVSCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTGK 149
Cdd:PTZ00143  99 ELIAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTGR 154
PHA03094 PHA03094
dUTPase; Provisional
 18-148 3.62e-20

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 80.58  E-value: 3.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  18 MPSYATQGSAGLDLRACIEHTqtIQPNETVMIPTGMAIHIDNTYYAAlILPRSGLGHKHGIVLGNlvGLIDSDYQGQLLV 97
Cdd:PHA03094  17 IPTRSSPKSAGYDLYSAYDYT--VPPKERILVKTDISLSIPKFCYGR-IAPRSGLSLNYGIDIGG--GVIDEDYRGNIGV 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 519010973  98 SCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTG 148
Cdd:PHA03094  92 IFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 18-148 1.94e-17

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 74.25  E-value: 1.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  18 MPSYATQGSAGLDLraCIEHTQTIQPNETVMIPTGMAIHIDNTYYAAlILPRSGLGHKHGIVLGnlVGLIDSDYQGQLLV 97
Cdd:PHA02703  25 IPTRGSPGAAGLDL--CSACDCIVPAGCRCVVFTDLLIKLPDGCYGR-IAPRSGLAVKHFIDVG--AGVIDADYRGNVGV 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 519010973  98 SCWNRGKEAFILNPMERIAQLVIVPVVQAEFHVVDEFTESDRGEGGFGSTG 148
Cdd:PHA02703 100 VLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTG 150
dut PRK13956
dUTP diphosphatase;
17-149 3.56e-15

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 67.90  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  17 MMPSYATQGSAGLDLRACieHTQTIQPNETVMIPTGMAIHIDNTYYAALiLPRSGLGHKHGIVLGNLVGLIDSDY----- 91
Cdd:PRK13956  17 LLPKRETAHAAGYDLKVA--ERTVIAPGEIKLVPTGVKAYMQPGEVLYL-YDRSSNPRKKGLVLINSVGVIDGDYygnpa 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 519010973  92 -QGQLLVSCWNRGKEAFILNPMERIAQLVIVPvvqaeFHVVDEFTESDRGEGGFGSTGK 149
Cdd:PRK13956  94 nEGHIFAQMKNITDQEVVLEVGERIVQGVFMP-----FLIADGDQADGERTGGFGSTGK 147
PHA03124 PHA03124
dUTPase; Provisional
 25-149 1.50e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 43.39  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  25 GSAGLDLRAciEHTQTIQPNETVMIPTGMAIHIdNTYYAALILPRSGLGHKHgiVLGNLVGLIDSDYqgqLLVSCWNRGK 104
Cdd:PHA03124 289 EDAGYDIRA--PEDCTILPGGSTRIILPQKLAC-GKFRAAFILGRSSMNLKG--LLVDPEHVQDDDW---ISFNITNIRD 360

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519010973 105 EAFILNPMERIAQLVIVP---------------VVQAefhVVDEF-TESDRGEGGFGSTGK 149
Cdd:PHA03124 361 AAAFFHAGDRIAQLIALEdkleflgepdalpwkIVNS---VQDEKkNLSSRGDGGFGSSGK 418
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 41-123 3.07e-05

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: 41.92  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973   41 IQPNETVMIPTGMAIHIDNtYYAALILPRSGLGHKhGIVLGNLVGLIDSDYQGQLLVSCWNRGKEAFILNPMERIAQLVI 120
Cdd:TIGR02274  73 IPPGEFALATTLEYVKLPD-DVVGFLEGRSSLARL-GLFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVF 150


                  ...
gi 519010973  121 VPV 123
Cdd:TIGR02274 151 ERL 153
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 41-143 1.54e-04

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 39.81  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  41 IQPNETVMIPTGMAIHIDNtYYAALILPRSGLGhKHGIVLGNLVGLIDSDYQGQ--LLVScwNRGKEAFILNPMERIAQL 118
Cdd:COG0717   72 LPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRitLELS--NTGPLPIKLYPGMRIAQL 147

                         90       100
                 ....*....|....*....|....*
gi 519010973 119 VivpvvqaeFHVVDEFTESDRGEGG 143
Cdd:COG0717  148 V--------FFRLSGPAERPYGRGG 164
PHA03131 PHA03131
dUTPase; Provisional
 19-121 3.99e-03

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 36.12  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519010973  19 PSYAtqGSAGLDLRA----CIEHTQTIqpneTVMIPTGMAIHIDNtyYAALILPRSGLGHKhGIvlgnlvgLIDSD--YQ 92
Cdd:PHA03131 127 PQYP--DDAGFDVSLpqdlVIFPTTTF----TFTLSLCCPPISPH--FVPVIFGRSGLASK-GL-------TVKPTkwRR 190

                         90       100
                 ....*....|....*....|....*....
gi 519010973  93 GQLLVSCWNRGKEAFILNPMERIAQLVIV 121
Cdd:PHA03131 191 SGLQLKLYNYTDETIFLPAGSRICQVVFM 219
 
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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