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Conserved domains on  [gi|522047167|ref|WP_020558376|]
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dUTP diphosphatase [Thiofilum flexile]

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;
3-152 7.57e-100

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 283.21  E-value: 7.57e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   3 PNLEYKILDPRIGETIPLPAYATDGSAGMDLRACLDQALTLKPGDTVLIPTGLAIHIGDpSLAAVILPRSGLGHKHGIVL 82
Cdd:PRK00601   2 KKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  83 GNLVGLIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSGRH 152
Cdd:PRK00601  81 GNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
3-152 7.57e-100

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 283.21  E-value: 7.57e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   3 PNLEYKILDPRIGETIPLPAYATDGSAGMDLRACLDQALTLKPGDTVLIPTGLAIHIGDpSLAAVILPRSGLGHKHGIVL 82
Cdd:PRK00601   2 KKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  83 GNLVGLIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSGRH 152
Cdd:PRK00601  81 GNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-151 6.90e-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: 6.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   4 NLEYKILDPrigeTIPLPAYATDGSAGMDLRACLDQALTLKPGDTVLIPTGLAIHIGdPSLAAVILPRSGLGHKHGIVLG 83
Cdd:COG0756    1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522047167  84 NLVGLIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSGR 151
Cdd:COG0756   76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-151 7.78e-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: 184.36  E-value: 7.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167    8 KILDPRIGETIPLPAYATDGSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIGDpSLAAVILPRSGLGHKHGIVLGNLVG 87
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522047167   88 LIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQ-VELKAVTEFTQSERGAGGFGHSGR 151
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-150 1.43e-46

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 147.44  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   16 ETIPLPAYATDGSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIgDPSLAAVILPRSGLGHKHGIVLGnlvGLIDSDYQG 95
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYD--LTVKPGGTVLVPTDISIPL-PDGTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 522047167   96 QLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSG 150
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 29-122 5.51e-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: 101.80  E-value: 5.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  29 AGMDLRACLD-QALTLKPGDTVLIPTGLAIHIgDPSLAAVILPRSGLGhKHGIVLGNlVGLIDSDYQGQLMISCWNRGQS 107
Cdd:cd07557    1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 522047167 108 EFTIEVGERIAQLVI 122
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
3-152 7.57e-100

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 283.21  E-value: 7.57e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   3 PNLEYKILDPRIGETIPLPAYATDGSAGMDLRACLDQALTLKPGDTVLIPTGLAIHIGDpSLAAVILPRSGLGHKHGIVL 82
Cdd:PRK00601   2 KKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIVL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  83 GNLVGLIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSGRH 152
Cdd:PRK00601  81 GNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-151 6.90e-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: 6.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   4 NLEYKILDPrigeTIPLPAYATDGSAGMDLRACLDQALTLKPGDTVLIPTGLAIHIGdPSLAAVILPRSGLGHKHGIVLG 83
Cdd:COG0756    1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522047167  84 NLVGLIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSGR 151
Cdd:COG0756   76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-151 7.78e-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: 184.36  E-value: 7.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167    8 KILDPRIGETIPLPAYATDGSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIGDpSLAAVILPRSGLGHKHGIVLGNLVG 87
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522047167   88 LIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQ-VELKAVTEFTQSERGAGGFGHSGR 151
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-150 1.43e-46

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 147.44  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   16 ETIPLPAYATDGSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIgDPSLAAVILPRSGLGHKHGIVLGnlvGLIDSDYQG 95
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYD--LTVKPGGTVLVPTDISIPL-PDGTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 522047167   96 QLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSG 150
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
PLN02547 PLN02547
dUTP pyrophosphatase
 3-150 5.22e-29

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 103.72  E-value: 5.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   3 PNLEYKILDPRIGETIPLPAYATDGSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIgDPSLAAVILPRSGLGHKHGIVL 82
Cdd:PLN02547  11 QKPSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYD--TVVPARGKALVPTDLSIAI-PEGTYARIAPRSGLAWKHSIDV 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522047167  83 GnlVGLIDSDYQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSG 150
Cdd:PLN02547  88 G--AGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 29-122 5.51e-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: 101.80  E-value: 5.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  29 AGMDLRACLD-QALTLKPGDTVLIPTGLAIHIgDPSLAAVILPRSGLGhKHGIVLGNlVGLIDSDYQGQLMISCWNRGQS 107
Cdd:cd07557    1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                         90
                 ....*....|....*
gi 522047167 108 EFTIEVGERIAQLVI 122
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
PHA03094 PHA03094
dUTPase; Provisional
 13-150 3.37e-25

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 93.68  E-value: 3.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  13 RIGETIPLPAYATDGSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIGDPSLAAvILPRSGLGHKHGIVLGNlvGLIDSD 92
Cdd:PHA03094  10 KLSNFAKIPTRSSPKSAGYDLYSAYD--YTVPPKERILVKTDISLSIPKFCYGR-IAPRSGLSLNYGIDIGG--GVIDED 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 522047167  93 YQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSG 150
Cdd:PHA03094  85 YRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 13-150 3.96e-20

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 81.18  E-value: 3.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  13 RIGETIPLPAYATDGSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIgDPSLAAVILPRSGLGHKHGIVLGnlVGLIDSD 92
Cdd:PHA02703  18 RLSPNATIPTRGSPGAAGLDLCSACD--CIVPAGCRCVVFTDLLIKL-PDGCYGRIAPRSGLAVKHFIDVG--AGVIDAD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 522047167  93 YQGQLMISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSG 150
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTG 150
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 26-151 3.45e-18

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 75.93  E-value: 3.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  26 DGSAGMDLRACLDQalTLKPGDTVLIPTGLAI-----HIGDPSLAAV---ILPRSGLGhKHGIVLGNLVGLIDSDYQGQL 97
Cdd:PTZ00143  24 EGDSGLDLFIVKDQ--TIKPGETAFIKLGIKAaafqkDEDGSDGKNVswlLFPRSSIS-KTPLRLANSIGLIDAGYRGEL 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 522047167  98 MISCWNRGQSEFTIEVGERIAQLVIVPVVQVELKAVTEFTQSERGAGGFGHSGR 151
Cdd:PTZ00143 101 IAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTGR 154
dut PRK13956
dUTP diphosphatase;
20-151 1.42e-15

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 69.05  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  20 LPAYATDGSAGMDLRACldQALTLKPGDTVLIPTGLAIHIgDPSLAAVILPRSGLGHKHGIVLGNLVGLIDSDY------ 93
Cdd:PRK13956  18 LPKRETAHAAGYDLKVA--ERTVIAPGEIKLVPTGVKAYM-QPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnpan 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 522047167  94 QGQLMISCWNRGQSEFTIEVGERIAQLVIVPVvqveLKAVTEFTQSERgAGGFGHSGR 151
Cdd:PRK13956  95 EGHIFAQMKNITDQEVVLEVGERIVQGVFMPF----LIADGDQADGER-TGGFGSTGK 147
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 38-121 1.17e-06

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 45.59  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  38 DQALTLKPGDTVLIPTGLAIHIGDpSLAAVILPRSGLGhKHGIVLGNLVGLIDSDYQGQ--LMIScwNRGQSEFTIEVGE 115
Cdd:COG0717   67 GDGFILPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRitLELS--NTGPLPIKLYPGM 142


                 ....*.
gi 522047167 116 RIAQLV 121
Cdd:COG0717  143 RIAQLV 148
PHA03131 PHA03131
dUTPase; Provisional
 8-123 5.66e-06

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 44.60  E-value: 5.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   8 KILDPRIgetIPLPAYATDgsAGMDLraCLDQALTLKPGDTVLIPTGLAIHIGDPSLAAVILPRSGLGHKhGIvlgnlvg 87
Cdd:PHA03131 117 ILTDDSL---LNPPQYPDD--AGFDV--SLPQDLVIFPTTTFTFTLSLCCPPISPHFVPVIFGRSGLASK-GL------- 181

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 522047167  88 LIDSD--YQGQLMISCWNRGQSEFTIEVGERIAQLVIV 123
Cdd:PHA03131 182 TVKPTkwRRSGLQLKLYNYTDETIFLPAGSRICQVVFM 219
PHA03124 PHA03124
dUTPase; Provisional
 27-151 5.76e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 41.85  E-value: 5.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167  27 GSAGMDLRACLDqaLTLKPGDTVLIPTGLAIHIGdPSLAAVILPRSGLGHKHgiVLGNLVGLIDSDYqgqLMISCWNRGQ 106
Cdd:PHA03124 289 EDAGYDIRAPED--CTILPGGSTRIILPQKLACG-KFRAAFILGRSSMNLKG--LLVDPEHVQDDDW---ISFNITNIRD 360

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522047167 107 SEFTIEVGERIAQLV------------------IVPVVQVELKavtefTQSERGAGGFGHSGR 151
Cdd:PHA03124 361 AAAFFHAGDRIAQLIaledkleflgepdalpwkIVNSVQDEKK-----NLSSRGDGGFGSSGK 418
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 38-125 7.09e-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: 40.76  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522047167   38 DQALTLKPGDTVLIPTGLAIHIGDpSLAAVILPRSGLGHKhGIVLGNLVGLIDSDYQGQLMISCWNRGQSEFTIEVGERI 117
Cdd:TIGR02274  68 GEEFVIPPGEFALATTLEYVKLPD-DVVGFLEGRSSLARL-GLFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRI 145


                  ....*...
gi 522047167  118 AQLVIVPV 125
Cdd:TIGR02274 146 AQLVFERL 153
 
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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