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Conserved domains on  [gi|489565860|ref|WP_003470366|]
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dUTP diphosphatase [Xanthomonas translucens]

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;
8-156 1.20e-90

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 260.10  E-value: 1.20e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   8 PLQVKLLDPRFGDSWPLPDYATDASAGLDLRAATEAPLTLAPGDTALIPSGLSIYIADpQLCAVVLPRSGLGHRHGIVLG 87
Cdd:PRK00601   3 KIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVLG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489565860  88 NGTGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGVR 156
Cdd:PRK00601  82 NLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
8-156 1.20e-90

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 260.10  E-value: 1.20e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   8 PLQVKLLDPRFGDSWPLPDYATDASAGLDLRAATEAPLTLAPGDTALIPSGLSIYIADpQLCAVVLPRSGLGHRHGIVLG 87
Cdd:PRK00601   3 KIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVLG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489565860  88 NGTGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGVR 156
Cdd:PRK00601  82 NLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 9-155 6.29e-78

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: 227.59  E-value: 6.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   9 LQVKLLDPrfgdSWPLPDYATDASAGLDLRAATEAPLTLAPGDTALIPSGLSIYIAdPQLCAVVLPRSGLGHRHGIVLGN 88
Cdd:COG0756    2 VKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLLN 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489565860  89 GTGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGV 155
Cdd:COG0756   77 SPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 12-155 6.54e-54

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: 166.64  E-value: 6.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   12 KLLDPRFGDSWPLPDYATDASAGLDLRAATEAplTLAPGDTALIPSGLSIYIadPQLC-AVVLPRSGLGHRHGIVLGNGT 90
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDV--TIPPGERALVPTGIAIEL--PDGYyGRVAPRSGLALKHGVTIDNSP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489565860   91 GLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVR-VALQVVDTFADSARGTGGFGHTGV 155
Cdd:TIGR00576  77 GVIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 20-154 1.85e-42

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 137.42  E-value: 1.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   20 DSWPLPDYATDASAGLDLRAATEapLTLAPGDTALIPSGLSIYIADPqLCAVVLPRSGLGHRHGIVLGngtGLIDADYQG 99
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYD--LTVKPGGTVLVPTDISIPLPDG-TYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489565860  100 PLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTG 154
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 33-126 2.77e-28

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: 100.26  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  33 AGLDLRAATEA-PLTLAPGDTALIPSGLSIYIaDPQLCAVVLPRSGLGhRHGIVLGNgTGLIDADYQGPLLISVWNRGRE 111
Cdd:cd07557    1 AGYDLRLGEDFeGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 489565860 112 PFTIAPGDRIAQLVV 126
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
8-156 1.20e-90

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 260.10  E-value: 1.20e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   8 PLQVKLLDPRFGDSWPLPDYATDASAGLDLRAATEAPLTLAPGDTALIPSGLSIYIADpQLCAVVLPRSGLGHRHGIVLG 87
Cdd:PRK00601   3 KIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVLG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489565860  88 NGTGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGVR 156
Cdd:PRK00601  82 NLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 9-155 6.29e-78

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: 227.59  E-value: 6.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   9 LQVKLLDPrfgdSWPLPDYATDASAGLDLRAATEAPLTLAPGDTALIPSGLSIYIAdPQLCAVVLPRSGLGHRHGIVLGN 88
Cdd:COG0756    2 VKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLLN 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489565860  89 GTGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGV 155
Cdd:COG0756   77 SPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 12-155 6.54e-54

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: 166.64  E-value: 6.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   12 KLLDPRFGDSWPLPDYATDASAGLDLRAATEAplTLAPGDTALIPSGLSIYIadPQLC-AVVLPRSGLGHRHGIVLGNGT 90
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDV--TIPPGERALVPTGIAIEL--PDGYyGRVAPRSGLALKHGVTIDNSP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489565860   91 GLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVR-VALQVVDTFADSARGTGGFGHTGV 155
Cdd:TIGR00576  77 GVIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 20-154 1.85e-42

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 137.42  E-value: 1.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   20 DSWPLPDYATDASAGLDLRAATEapLTLAPGDTALIPSGLSIYIADPqLCAVVLPRSGLGHRHGIVLGngtGLIDADYQG 99
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYD--LTVKPGGTVLVPTDISIPLPDG-TYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489565860  100 PLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTG 154
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 33-126 2.77e-28

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: 100.26  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  33 AGLDLRAATEA-PLTLAPGDTALIPSGLSIYIaDPQLCAVVLPRSGLGhRHGIVLGNgTGLIDADYQGPLLISVWNRGRE 111
Cdd:cd07557    1 AGYDLRLGEDFeGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 489565860 112 PFTIAPGDRIAQLVV 126
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
PLN02547 PLN02547
dUTP pyrophosphatase
 3-155 2.19e-27

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 99.87  E-value: 2.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   3 IPTPYP-LQVKlldpRFGDSWPLPDYATDASAGLDLRAATEAplTLAPGDTALIPSGLSIYIAdPQLCAVVLPRSGLGHR 81
Cdd:PLN02547  10 IQKPSPlLRVK----KLSEKATLPSRGSALAAGYDLSSAYDT--VVPARGKALVPTDLSIAIP-EGTYARIAPRSGLAWK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489565860  82 HGIVLGngTGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGV 155
Cdd:PLN02547  83 HSIDVG--AGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTGV 154
PHA03094 PHA03094
dUTPase; Provisional
 24-156 1.75e-21

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 84.43  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  24 LPDYATDASAGLDLRAATEapLTLAPGDTALIPSGLSIYIadPQLC-AVVLPRSGLGHRHGIVLGNGtgLIDADYQGPLL 102
Cdd:PHA03094  17 IPTRSSPKSAGYDLYSAYD--YTVPPKERILVKTDISLSI--PKFCyGRIAPRSGLSLNYGIDIGGG--VIDEDYRGNIG 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489565860 103 ISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGVR 156
Cdd:PHA03094  91 VIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSGLR 144
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 17-156 4.95e-19

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 78.49  E-value: 4.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  17 RFGDSWPLPDYATDASAGLDLRAATEApltlapgdtaLIPSGLS------IYIADPQLC-AVVLPRSGLGHRHGIVLGng 89
Cdd:PHA02703  18 RLSPNATIPTRGSPGAAGLDLCSACDC----------IVPAGCRcvvftdLLIKLPDGCyGRIAPRSGLAVKHFIDVG-- 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489565860  90 TGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGVR 156
Cdd:PHA02703  86 AGVIDADYRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGSG 152
dut PRK13956
dUTP diphosphatase;
18-155 3.62e-18

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 75.99  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  18 FGDSWPLPDYATDASAGLDLRAATEapLTLAPGDTALIPSGLSIYIADPQLCaVVLPRSGLGHRHGIVLGNGTGLIDADY 97
Cdd:PRK13956  12 FTNENLLPKRETAHAAGYDLKVAER--TVIAPGEIKLVPTGVKAYMQPGEVL-YLYDRSSNPRKKGLVLINSVGVIDGDY 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489565860  98 ------QGPLLISVWNRGREPFTIAPGDRIAQLVVMPVVrvalqVVDtfADSARG--TGGFGHTGV 155
Cdd:PRK13956  89 ygnpanEGHIFAQMKNITDQEVVLEVGERIVQGVFMPFL-----IAD--GDQADGerTGGFGSTGK 147
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 30-155 2.03e-17

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 74.00  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  30 DASAGLDLRAATEAplTLAPGDTALIPSGLSIYIADPQLCA--------VVLPRSGLGhRHGIVLGNGTGLIDADYQGPL 101
Cdd:PTZ00143  24 EGDSGLDLFIVKDQ--TIKPGETAFIKLGIKAAAFQKDEDGsdgknvswLLFPRSSIS-KTPLRLANSIGLIDAGYRGEL 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489565860 102 LISVWNRGREPFTIAPGDRIAQLVVMPVVRVALQVVDTFADSARGTGGFGHTGV 155
Cdd:PTZ00143 101 IAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTGR 154
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 44-125 2.56e-08

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 50.59  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  44 PLTLAPGDTALIPSGLSIYIADpQLCAVVLPRSGLGhRHGIVLGNGTGLIDADYQGPLLISVWNRGREPFTIAPGDRIAQ 123
Cdd:COG0717   69 GFILPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQ 146


                 ..
gi 489565860 124 LV 125
Cdd:COG0717  147 LV 148
PHA03131 PHA03131
dUTPase; Provisional
 5-127 1.24e-07

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 49.22  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   5 TPYPLQVKLLDPrfgdswplPDYATDAsaGLDLRAATEapLTLAPGDTALIpsglSIYIADPQLC----AVVLPRSGLGH 80
Cdd:PHA03131 115 TPILTDDSLLNP--------PQYPDDA--GFDVSLPQD--LVIFPTTTFTF----TLSLCCPPISphfvPVIFGRSGLAS 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489565860  81 RhGIvlgngtgLIDAD--YQGPLLISVWNRGREPFTIAPGDRIAQLVVM 127
Cdd:PHA03131 179 K-GL-------TVKPTkwRRSGLQLKLYNYTDETIFLPAGSRICQVVFM 219
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 34-125 4.14e-07

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: 47.31  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860   34 GLDLRAATEAPLTLAPGDTALIPSGLSIYIADpQLCAVVLPRSGLGhRHGIVLGNGTGLIDADYQGPLLISVWNRGREPF 113
Cdd:TIGR02274  60 SYLFEVEEGEEFVIPPGEFALATTLEYVKLPD-DVVGFLEGRSSLA-RLGLFIHVTAGRIDPGFEGNITLELFNAGKLPV 137

                          90
                  ....*....|..
gi 489565860  114 TIAPGDRIAQLV 125
Cdd:TIGR02274 138 KLRPGMRIAQLV 149
PHA03131 PHA03131
dUTPase; Provisional
 44-119 2.01e-03

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 37.28  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565860  44 PLTLAPGDTALIPSGLsiYIADPQLCAVVL----PRSGLGHrhgivlgngTGLIDADYQGPLLISVWNRGREPFTIAPGD 119
Cdd:PHA03131  35 PILVRPGEPTVVPLGL--YIRRPPGFAFILwgstSKNVTCH---------TGLIDPGYRGELKLILLNKTKYNVTLRPGE 103
 
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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