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Conserved domains on  [gi|492047718|ref|WP_005731629|]
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MULTISPECIES: dUTP diphosphatase [Pseudomonas]

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 3.64e-100

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 283.98  E-value: 3.64e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718   1 MHALQAKILDPRIGNEFPLPAYATVGSAGLDLRAMLKEDTVLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492047718  81 LGNLVGLIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSGSH 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-151 3.64e-100

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 283.98  E-value: 3.64e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718   1 MHALQAKILDPRIGNEFPLPAYATVGSAGLDLRAMLKEDTVLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492047718  81 LGNLVGLIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSGSH 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-149 1.74e-83

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: 241.46  E-value: 1.74e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718   4 LQAKILDPrignEFPLPAYATVGSAGLDLRAMLKEDTVLEPGQTLLIPTGLSIYIGdPGLAALILPRSGLGHKHGIVLGN 83
Cdd:COG0756    2 VKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLLN 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492047718  84 LVGLIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSG 149
Cdd:COG0756   77 SPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 7-150 4.48e-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: 184.75  E-value: 4.48e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718    7 KILDPRIGNEFPLPAYATVGSAGLDLRAMlkEDTVLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLGHKHGIVLGNLVG 86
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492047718   87 LIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAH-FELVEAFDESQRGAGGFGHSGS 150
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVeFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 15-149 1.00e-47

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 150.52  E-value: 1.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718   15 NEFPLPAYATVGSAGLDLRAmlKEDTVLEPGQTLLIPTGLSIYIgDPGLAALILPRSGLGHKHGIVLGnlvGLIDSDYQG 94
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYA--PYDLTVKPGGTVLVPTDISIPL-PDGTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 492047718   95 ELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSG 149
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 28-121 4.60e-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: 99.49  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  28 AGLDLRAMLKEDT-VLEPGQTLLIPTGLSIYIgDPGLAALILPRSGLGhKHGIVLGNlVGLIDSDYQGELMVSCWNRGQT 106
Cdd:cd07557    1 AGYDLRLGEDFEGiVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 492047718 107 AFNIAVGERIAQLVL 121
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-151 3.64e-100

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 283.98  E-value: 3.64e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718   1 MHALQAKILDPRIGNEFPLPAYATVGSAGLDLRAMLKEDTVLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492047718  81 LGNLVGLIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSGSH 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-149 1.74e-83

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: 241.46  E-value: 1.74e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718   4 LQAKILDPrignEFPLPAYATVGSAGLDLRAMLKEDTVLEPGQTLLIPTGLSIYIGdPGLAALILPRSGLGHKHGIVLGN 83
Cdd:COG0756    2 VKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLLN 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492047718  84 LVGLIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSG 149
Cdd:COG0756   77 SPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 7-150 4.48e-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: 184.75  E-value: 4.48e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718    7 KILDPRIGNEFPLPAYATVGSAGLDLRAMlkEDTVLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLGHKHGIVLGNLVG 86
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492047718   87 LIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAH-FELVEAFDESQRGAGGFGHSGS 150
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVeFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 15-149 1.00e-47

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 150.52  E-value: 1.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718   15 NEFPLPAYATVGSAGLDLRAmlKEDTVLEPGQTLLIPTGLSIYIgDPGLAALILPRSGLGHKHGIVLGnlvGLIDSDYQG 94
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYA--PYDLTVKPGGTVLVPTDISIPL-PDGTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 492047718   95 ELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSG 149
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
PLN02547 PLN02547
dUTP pyrophosphatase
 19-149 1.99e-29

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 104.88  E-value: 1.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  19 LPAYATVGSAGLDLRAmlKEDTVLEPGQTLLIPTGLSIYIgDPGLAALILPRSGLGHKHGIVLGnlVGLIDSDYQGELMV 98
Cdd:PLN02547  28 LPSRGSALAAGYDLSS--AYDTVVPARGKALVPTDLSIAI-PEGTYARIAPRSGLAWKHSIDVG--AGVIDADYRGPVGV 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492047718  99 SCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSG 149
Cdd:PLN02547 103 ILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 28-121 4.60e-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: 99.49  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  28 AGLDLRAMLKEDT-VLEPGQTLLIPTGLSIYIgDPGLAALILPRSGLGhKHGIVLGNlVGLIDSDYQGELMVSCWNRGQT 106
Cdd:cd07557    1 AGYDLRLGEDFEGiVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 492047718 107 AFNIAVGERIAQLVL 121
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
PHA03094 PHA03094
dUTPase; Provisional
 19-149 3.45e-22

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 85.97  E-value: 3.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  19 LPAYATVGSAGLDLRAMLkeDTVLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLGHKHGIVLGNlvGLIDSDYQGELMV 98
Cdd:PHA03094  17 IPTRSSPKSAGYDLYSAY--DYTVPPKERILVKTDISLSIPK-FCYGRIAPRSGLSLNYGIDIGG--GVIDEDYRGNIGV 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492047718  99 SCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSG 149
Cdd:PHA03094  92 IFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 12-150 5.05e-22

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 86.19  E-value: 5.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  12 RIGNEFPLPAYATVGSAGLDLRAMLkeDTVLEPGQTLLIPTGLSIYIgDPGLAALILPRSGLGHKHGIVLGnlVGLIDSD 91
Cdd:PHA02703  18 RLSPNATIPTRGSPGAAGLDLCSAC--DCIVPAGCRCVVFTDLLIKL-PDGCYGRIAPRSGLAVKHFIDVG--AGVIDAD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492047718  92 YQGELMVSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSGS 150
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGS 151
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 26-149 3.73e-19

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 78.62  E-value: 3.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  26 GSAGLDLraMLKEDTVLEPGQTLLIPTGLSIYIGDP--------GLAALILPRSGLGhKHGIVLGNLVGLIDSDYQGELM 97
Cdd:PTZ00143  25 GDSGLDL--FIVKDQTIKPGETAFIKLGIKAAAFQKdedgsdgkNVSWLLFPRSSIS-KTPLRLANSIGLIDAGYRGELI 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492047718  98 VSCWNRGQTAFNIAVGERIAQLVLVPVVQAHFELVEAFDESQRGAGGFGHSG 149
Cdd:PTZ00143 102 AAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTG 153
dut PRK13956
dUTP diphosphatase;
15-149 1.83e-17

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 73.68  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  15 NEFPLPAYATVGSAGLDLRAmlKEDTVLEPGQTLLIPTGLSIYIgDPGLAALILPRSGLGHKHGIVLGNLVGLIDSDY-- 92
Cdd:PRK13956  14 NENLLPKRETAHAAGYDLKV--AERTVIAPGEIKLVPTGVKAYM-QPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYyg 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492047718  93 ----QGELMVSCWNRGQTAFNIAVGERIAQLVLVPvvqahFELVEAFDESQRGAGGFGHSG 149
Cdd:PRK13956  91 npanEGHIFAQMKNITDQEVVLEVGERIVQGVFMP-----FLIADGDQADGERTGGFGSTG 146
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 4-124 1.29e-06

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: 45.77  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718    4 LQAKILDPRIGNEFPLPAYATVG---------SAGLDLRAMLKEDTVLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLG 74
Cdd:TIGR02274  26 LQPAGVDLRLGNEFRVFRNHTGAvidpenpkeAVSYLFEVEEGEEFVIPPGEFALATTLEYVKLPD-DVVGFLEGRSSLA 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 492047718   75 HKhGIVLGNLVGLIDSDYQGELMVSCWNRGQTAFNIAVGERIAQLVLVPV 124
Cdd:TIGR02274 105 RL-GLFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFERL 153
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 41-121 5.16e-05

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 41.35  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  41 VLEPGQTLLIPTGLSIYIGDpGLAALILPRSGLGhKHGIVLGNLVGLIDSDYQG--ELMVScwNRGQTAFNIAVGERIAQ 118
Cdd:COG0717   71 ILPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGriTLELS--NTGPLPIKLYPGMRIAQ 146


                 ...
gi 492047718 119 LVL 121
Cdd:COG0717  147 LVF 149
PHA03124 PHA03124
dUTPase; Provisional
 26-149 8.99e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 41.08  E-value: 8.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492047718  26 GSAGLDLRAmlKEDTVLEPGQTLLIPTGLSIYIGdPGLAALILPRSGLGHKHgiVLGNLVGLIDSDYqgeLMVSCWNRGQ 105
Cdd:PHA03124 289 EDAGYDIRA--PEDCTILPGGSTRIILPQKLACG-KFRAAFILGRSSMNLKG--LLVDPEHVQDDDW---ISFNITNIRD 360

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492047718 106 TAFNIAVGERIAQLVLVP---------------VVQAHFElvEAFDESQRGAGGFGHSG 149
Cdd:PHA03124 361 AAAFFHAGDRIAQLIALEdkleflgepdalpwkIVNSVQD--EKKNLSSRGDGGFGSSG 417
PHA03131 PHA03131
dUTPase; Provisional
 41-114 6.32e-04

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 38.43  E-value: 6.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492047718  41 VLEPGQTLLIPTGLSIyIGDPGLAaLIL----PRSGLGHkhgivlgnlVGLIDSDYQGELMVSCWNRGQTAFNIAVGE 114
Cdd:PHA03131  37 LVRPGEPTVVPLGLYI-RRPPGFA-FILwgstSKNVTCH---------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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