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Conserved domains on  [gi|501231804|ref|WP_012274822|]
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dUTP diphosphatase [Pseudomonas putida]

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;
1-151 1.60e-101

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 287.45  E-value: 1.60e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804   1 MHALQAKILDPRLGSEFPLPTYATPGSAGLDLRALLKEDTVLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501231804  81 LGNLVGLIDSDYQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSGSH 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-151 1.60e-101

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 287.45  E-value: 1.60e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804   1 MHALQAKILDPRLGSEFPLPTYATPGSAGLDLRALLKEDTVLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501231804  81 LGNLVGLIDSDYQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSGSH 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 12-149 1.72e-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: 243.77  E-value: 1.72e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  12 RLGSEFPLPTYATPGSAGLDLRALLKEDTVLEPGQTLLIPTGLSIYIGdPGLAAVILPRSGLGHKHGIVLGNLVGLIDSD 91
Cdd:COG0756    6 RLDEDAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLLNSPGTIDSD 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501231804  92 YQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSG 149
Cdd:COG0756   85 YRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 7-150 1.04e-61

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: 186.29  E-value: 1.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804    7 KILDPRLGSEFPLPTYATPGSAGLDLRALlkEDTVLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLGHKHGIVLGNLVG 86
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501231804   87 LIDSDYQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAH-FDIVEAFDESQRGAGGFGHSGS 150
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVeFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-149 6.83e-50

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 155.91  E-value: 6.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804   16 EFPLPTYATPGSAGLDLRALlkEDTVLEPGQTLLIPTGLSIYIgDPGLAAVILPRSGLGHKHGIVLGnlvGLIDSDYQGE 95
Cdd:pfam00692   2 EAEIPTPGSPGDAGYDLYAP--YDLTVKPGGTVLVPTDISIPL-PDGTYGRIFPRSGLAAKGLIVVP---GVIDSDYRGE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 501231804   96 LMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSG 149
Cdd:pfam00692  76 VKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 28-121 2.46e-29

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: 102.57  E-value: 2.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  28 AGLDLRALLKEDT-VLEPGQTLLIPTGLSIYIgDPGLAAVILPRSGLGhKHGIVLGNlVGLIDSDYQGELMVSCWNRSNT 106
Cdd:cd07557    1 AGYDLRLGEDFEGiVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 501231804 107 PFTIAVGERIAQLVL 121
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-151 1.60e-101

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 287.45  E-value: 1.60e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804   1 MHALQAKILDPRLGSEFPLPTYATPGSAGLDLRALLKEDTVLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501231804  81 LGNLVGLIDSDYQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSGSH 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 12-149 1.72e-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: 243.77  E-value: 1.72e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  12 RLGSEFPLPTYATPGSAGLDLRALLKEDTVLEPGQTLLIPTGLSIYIGdPGLAAVILPRSGLGHKHGIVLGNLVGLIDSD 91
Cdd:COG0756    6 RLDEDAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLLNSPGTIDSD 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501231804  92 YQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSG 149
Cdd:COG0756   85 YRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 7-150 1.04e-61

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: 186.29  E-value: 1.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804    7 KILDPRLGSEFPLPTYATPGSAGLDLRALlkEDTVLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLGHKHGIVLGNLVG 86
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501231804   87 LIDSDYQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAH-FDIVEAFDESQRGAGGFGHSGS 150
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVeFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-149 6.83e-50

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 155.91  E-value: 6.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804   16 EFPLPTYATPGSAGLDLRALlkEDTVLEPGQTLLIPTGLSIYIgDPGLAAVILPRSGLGHKHGIVLGnlvGLIDSDYQGE 95
Cdd:pfam00692   2 EAEIPTPGSPGDAGYDLYAP--YDLTVKPGGTVLVPTDISIPL-PDGTYGRIFPRSGLAAKGLIVVP---GVIDSDYRGE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 501231804   96 LMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSG 149
Cdd:pfam00692  76 VKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
PLN02547 PLN02547
dUTP pyrophosphatase
 19-149 2.89e-30

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 107.19  E-value: 2.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  19 LPTYATPGSAGLDLRAllKEDTVLEPGQTLLIPTGLSIYIgDPGLAAVILPRSGLGHKHGIVLGnlVGLIDSDYQGELMV 98
Cdd:PLN02547  28 LPSRGSALAAGYDLSS--AYDTVVPARGKALVPTDLSIAI-PEGTYARIAPRSGLAWKHSIDVG--AGVIDADYRGPVGV 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501231804  99 SCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSG 149
Cdd:PLN02547 103 ILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 28-121 2.46e-29

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: 102.57  E-value: 2.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  28 AGLDLRALLKEDT-VLEPGQTLLIPTGLSIYIgDPGLAAVILPRSGLGhKHGIVLGNlVGLIDSDYQGELMVSCWNRSNT 106
Cdd:cd07557    1 AGYDLRLGEDFEGiVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 501231804 107 PFTIAVGERIAQLVL 121
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 12-150 7.62e-24

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 90.81  E-value: 7.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  12 RLGSEFPLPTYATPGSAGLDLRALLkeDTVLEPGQTLLIPTGLSIYIgDPGLAAVILPRSGLGHKHGIVLGnlVGLIDSD 91
Cdd:PHA02703  18 RLSPNATIPTRGSPGAAGLDLCSAC--DCIVPAGCRCVVFTDLLIKL-PDGCYGRIAPRSGLAVKHFIDVG--AGVIDAD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501231804  92 YQGELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSGS 150
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGS 151
PHA03094 PHA03094
dUTPase; Provisional
 15-149 1.08e-23

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 89.82  E-value: 1.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  15 SEFP-LPTYATPGSAGLDLRALLkeDTVLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLGHKHGIVLGNlvGLIDSDYQ 93
Cdd:PHA03094  12 SNFAkIPTRSSPKSAGYDLYSAY--DYTVPPKERILVKTDISLSIPK-FCYGRIAPRSGLSLNYGIDIGG--GVIDEDYR 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501231804  94 GELMVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSG 149
Cdd:PHA03094  87 GNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 25-149 6.76e-21

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 82.86  E-value: 6.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  25 PGSAGLDLraLLKEDTVLEPGQTLLIPTGLSIYIGDP--------GLAAVILPRSGLGhKHGIVLGNLVGLIDSDYQGEL 96
Cdd:PTZ00143  24 EGDSGLDL--FIVKDQTIKPGETAFIKLGIKAAAFQKdedgsdgkNVSWLLFPRSSIS-KTPLRLANSIGLIDAGYRGEL 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501231804  97 MVSCWNRSNTPFTIAVGERIAQLVLVPVVQAHFDIVEAFDESQRGAGGFGHSG 149
Cdd:PTZ00143 101 IAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTG 153
dut PRK13956
dUTP diphosphatase;
19-149 1.13e-19

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 79.45  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  19 LPTYATPGSAGLDLRAllKEDTVLEPGQTLLIPTGLSIYIgDPGLAAVILPRSGLGHKHGIVLGNLVGLIDSDY------ 92
Cdd:PRK13956  18 LPKRETAHAAGYDLKV--AERTVIAPGEIKLVPTGVKAYM-QPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnpan 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501231804  93 QGELMVSCWNRSNTPFTIAVGERIAQLVLVPvvqahFDIVEAFDESQRGAGGFGHSG 149
Cdd:PRK13956  95 EGHIFAQMKNITDQEVVLEVGERIVQGVFMP-----FLIADGDQADGERTGGFGSTG 146
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 4-124 5.15e-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: 46.92  E-value: 5.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804    4 LQAKILDPRLGSEFPLPTYAT--------PGSAGLDLRALLKEDT-VLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLG 74
Cdd:TIGR02274  26 LQPAGVDLRLGNEFRVFRNHTgavidpenPKEAVSYLFEVEEGEEfVIPPGEFALATTLEYVKLPD-DVVGFLEGRSSLA 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 501231804   75 HKhGIVLGNLVGLIDSDYQGELMVSCWNRSNTPFTIAVGERIAQLVLVPV 124
Cdd:TIGR02274 105 RL-GLFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFERL 153
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 9-121 6.60e-07

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 46.36  E-value: 6.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804   9 LDPRLGSEFPLPTYATPGSAGLDLRAL-------LKEDTVLEPGQTLLIPTGLSIYIGDpGLAAVILPRSGLGhKHGIVL 81
Cdd:COG0717   32 YDLRLGNEFRVFENHNSGVIDPKKRDLteeieiePGDGFILPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFV 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501231804  82 GNLVGLIDSDYQG--ELMVScwNRSNTPFTIAVGERIAQLVL 121
Cdd:COG0717  110 HTTAGVIDPGFEGriTLELS--NTGPLPIKLYPGMRIAQLVF 149
PHA03131 PHA03131
dUTPase; Provisional
 41-114 3.76e-05

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 42.29  E-value: 3.76e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501231804  41 VLEPGQTLLIPTGLSIyIGDPGLAAVIL---PRSGLGHkhgivlgnlVGLIDSDYQGELMVSCWNRSNTPFTIAVGE 114
Cdd:PHA03131  37 LVRPGEPTVVPLGLYI-RRPPGFAFILWgstSKNVTCH---------TGLIDPGYRGELKLILLNKTKYNVTLRPGE 103
PHA03124 PHA03124
dUTPase; Provisional
 25-149 4.08e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 42.24  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  25 PGSAGLDLRAllKEDTVLEPGQTLLIPTGLSIYIGdPGLAAVILPRSGLGHKHgiVLGNLVGLIDSDYqgeLMVSCWNRS 104
Cdd:PHA03124 288 AEDAGYDIRA--PEDCTILPGGSTRIILPQKLACG-KFRAAFILGRSSMNLKG--LLVDPEHVQDDDW---ISFNITNIR 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804 105 NTPFTIAVGERIAQLVLVP---------------VVQAHFDivEAFDESQRGAGGFGHSG 149
Cdd:PHA03124 360 DAAAFFHAGDRIAQLIALEdkleflgepdalpwkIVNSVQD--EKKNLSSRGDGGFGSSG 417
PHA03131 PHA03131
dUTPase; Provisional
 19-122 4.82e-05

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 41.90  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231804  19 LPTYatPGSAGLDLRalLKEDTVLEPGQTllipTGLSIYIGDPGLA----AVILPRSGLGHKhGIvlgnlvgLID-SDYQ 93
Cdd:PHA03131 126 PPQY--PDDAGFDVS--LPQDLVIFPTTT----FTFTLSLCCPPISphfvPVIFGRSGLASK-GL-------TVKpTKWR 189

                         90       100       110
                 ....*....|....*....|....*....|
gi 501231804  94 GE-LMVSCWNRSNTPFTIAVGERIAQLVLV 122
Cdd:PHA03131 190 RSgLQLKLYNYTDETIFLPAGSRICQVVFM 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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