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Conserved domains on  [gi|1860589441|ref|WP_175630784|]
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dUTP diphosphatase [Bacteroides acidifaciens]

Protein Classification

dUTP diphosphatase( domain architecture ID 10786453)

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|GO:0006226|GO:0046081
SCOP:  4002970

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 9-143 3.03e-92

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: 263.03  E-value: 3.03e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441   9 SKHPLPAYATELSAGMDIRANLSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNSPGTIDADYRGE 88
Cdd:COG0756     9 EDAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGTIDSDYRGE 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1860589441  89 ICIILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTGV 143
Cdd:COG0756    89 IKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 9-143 3.03e-92

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: 263.03  E-value: 3.03e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441   9 SKHPLPAYATELSAGMDIRANLSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNSPGTIDADYRGE 88
Cdd:COG0756     9 EDAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGTIDSDYRGE 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1860589441  89 ICIILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTGV 143
Cdd:COG0756    89 IKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut PRK00601
dUTP diphosphatase;
1-143 9.82e-92

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 262.02  E-value: 9.82e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441   1 MNIQVINK---SKHPLPAYATELSAGMDIRANLSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNS 77
Cdd:PRK00601    4 IDVKILDPrlgKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860589441  78 PGTIDADYRGEICIILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTGV 143
Cdd:PRK00601   84 PGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGR 149
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 12-143 5.31e-67

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: 199.38  E-value: 5.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  12 PLPAYATELSAGMDIRAnlSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNSPGTIDADYRGEICI 91
Cdd:TIGR00576  12 PLPTYATEGAAGYDLRA--AEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGVIDADYRGEIKV 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1860589441  92 ILINLSSETFVIEDGERIAQMVIAKHEQ-PSWQEVEVLDETERGAGGFGHTGV 143
Cdd:TIGR00576  90 ILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 12-142 2.10e-41

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 134.34  E-value: 2.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  12 PLPAYATELSAGMDIRAnlSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVlnsPGTIDADYRGEICI 91
Cdd:pfam00692   4 EIPTPGSPGDAGYDLYA--PYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVV---PGVIDSDYRGEVKV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1860589441  92 ILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTG 142
Cdd:pfam00692  79 VLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 22-114 1.05e-35

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: 118.37  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  22 AGMDIRA-NLSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAiKKGISVLNsPGTIDADYRGEICIILINLSSET 100
Cdd:cd07557     1 AGYDLRLgEDFEGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPEP 78

                          90
                  ....*....|....
gi 1860589441 101 FVIEDGERIAQMVI 114
Cdd:cd07557    79 VVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 9-143 3.03e-92

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: 263.03  E-value: 3.03e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441   9 SKHPLPAYATELSAGMDIRANLSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNSPGTIDADYRGE 88
Cdd:COG0756     9 EDAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGTIDSDYRGE 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1860589441  89 ICIILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTGV 143
Cdd:COG0756    89 IKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut PRK00601
dUTP diphosphatase;
1-143 9.82e-92

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 262.02  E-value: 9.82e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441   1 MNIQVINK---SKHPLPAYATELSAGMDIRANLSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNS 77
Cdd:PRK00601    4 IDVKILDPrlgKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860589441  78 PGTIDADYRGEICIILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTGV 143
Cdd:PRK00601   84 PGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGR 149
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 12-143 5.31e-67

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: 199.38  E-value: 5.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  12 PLPAYATELSAGMDIRAnlSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNSPGTIDADYRGEICI 91
Cdd:TIGR00576  12 PLPTYATEGAAGYDLRA--AEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGVIDADYRGEIKV 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1860589441  92 ILINLSSETFVIEDGERIAQMVIAKHEQ-PSWQEVEVLDETERGAGGFGHTGV 143
Cdd:TIGR00576  90 ILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 12-142 2.10e-41

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 134.34  E-value: 2.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  12 PLPAYATELSAGMDIRAnlSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVlnsPGTIDADYRGEICI 91
Cdd:pfam00692   4 EIPTPGSPGDAGYDLYA--PYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVV---PGVIDSDYRGEVKV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1860589441  92 ILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTG 142
Cdd:pfam00692  79 VLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
PLN02547 PLN02547
dUTP pyrophosphatase
 13-143 4.87e-40

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 131.84  E-value: 4.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  13 LPAYATELSAGMDIRAnlSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVlnSPGTIDADYRGEICII 92
Cdd:PLN02547   28 LPSRGSALAAGYDLSS--AYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDV--GAGVIDADYRGPVGVI 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1860589441  93 LINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTGV 143
Cdd:PLN02547  104 LFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTGV 154
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 22-114 1.05e-35

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: 118.37  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  22 AGMDIRA-NLSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAiKKGISVLNsPGTIDADYRGEICIILINLSSET 100
Cdd:cd07557     1 AGYDLRLgEDFEGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPEP 78

                          90
                  ....*....|....
gi 1860589441 101 FVIEDGERIAQMVI 114
Cdd:cd07557    79 VVIKKGDRIAQLVF 92
PHA03094 PHA03094
dUTPase; Provisional
 13-143 2.71e-31

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 109.08  E-value: 2.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  13 LPAYATELSAGMDIRANLSepVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVlnSPGTIDADYRGEICII 92
Cdd:PHA03094   17 IPTRSSPKSAGYDLYSAYD--YTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDI--GGGVIDEDYRGNIGVI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1860589441  93 LINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHTGV 143
Cdd:PHA03094   93 FINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSGL 143
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 41-143 3.30e-30

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 106.99  E-value: 3.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  41 RCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVlnSPGTIDADYRGEICIILINLSSETFVIEDGERIAQMVIAKHEQP 120
Cdd:PHA02703   51 RCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDV--GAGVIDADYRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFP 128

                          90       100
                  ....*....|....*....|...
gi 1860589441 121 SWQEVEVLDETERGAGGFGHTGV 143
Cdd:PHA02703  129 AVEEVACLDDTDRGAGGFGSTGS 151
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 62-143 4.16e-19

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 77.85  E-value: 4.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  62 PRSGLAiKKGISVLNSPGTIDADYRGEICIILINLSSETFVIEDGERIAQMVIAKHEQPSWQEVEVLDETERGAGGFGHT 141
Cdd:PTZ00143   74 PRSSIS-KTPLRLANSIGLIDAGYRGELIAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGST 152


                  ..
gi 1860589441 142 GV 143
Cdd:PTZ00143  153 GR 154
dut PRK13956
dUTP diphosphatase;
13-143 3.17e-15

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 67.90  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  13 LPAYATELSAGMDIRAnlSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKKGISVLNSPGTIDADY------R 86
Cdd:PRK13956   18 LPKRETAHAAGYDLKV--AERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnpanE 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860589441  87 GEICIILINLSSETFVIEDGERIAQMV-----IAKHEQpswqevevldETERGAGGFGHTGV 143
Cdd:PRK13956   96 GHIFAQMKNITDQEVVLEVGERIVQGVfmpflIADGDQ----------ADGERTGGFGSTGK 147
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 32-116 1.46e-09

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 53.29  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  32 EPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAiKKGISVLNSPGTIDADYRGEICIILINLSSETFVIEDGERIAQ 111
Cdd:COG0717    68 DGFILPPGEFYLARTLEYVRLPDDLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQ 146


                  ....*
gi 1860589441 112 MVIAK 116
Cdd:COG0717   147 LVFFR 151
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 32-121 3.31e-08

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: 49.62  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  32 EPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAiKKGISVLNSPGTIDADYRGEICIILINLSSETFVIEDGERIAQ 111
Cdd:TIGR02274  69 EEFVIPPGEFALATTLEYVKLPDDVVGFLEGRSSLA-RLGLFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQ 147

                          90
                  ....*....|
gi 1860589441 112 MVIAKHEQPS 121
Cdd:TIGR02274 148 LVFERLSSPA 157
PHA03131 PHA03131
dUTPase; Provisional
 33-107 4.35e-07

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 47.29  E-value: 4.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860589441  33 PVTLEPLQRCLVPTGLYIALPKGFeAQIrprsgLAIKKGISVLNSPGTIDADYRGEICIILINLSSETFVIEDGE 107
Cdd:PHA03131   35 PILVRPGEPTVVPLGLYIRRPPGF-AFI-----LWGSTSKNVTCHTGLIDPGYRGELKLILLNKTKYNVTLRPGE 103
PHA03131 PHA03131
dUTPase; Provisional
 13-121 6.31e-06

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 44.21  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  13 LPAYatELSAGMDIRanLSEPVTLEPLQRclVPTGLYIALP---KGFEAQIRPRSGLAIKkGISVLNSPGTidadyRGEI 89
Cdd:PHA03131  126 PPQY--PDDAGFDVS--LPQDLVIFPTTT--FTFTLSLCCPpisPHFVPVIFGRSGLASK-GLTVKPTKWR-----RSGL 193

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1860589441  90 CIILINLSSETFVIEDGERIAQMV-IAKHEQPS 121
Cdd:PHA03131  194 QLKLYNYTDETIFLPAGSRICQVVfMHKDHLPS 226
PHA03124 PHA03124
dUTPase; Provisional
 22-143 8.05e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 41.08  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  22 AGMDIRAnlSEPVTLEPLQRCLVPTGLYIALPKGFEAQIRPRSGLAIKkgiSVLNSP-GTIDADYrgeICIILINLSSET 100
Cdd:PHA03124  291 AGYDIRA--PEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLK---GLLVDPeHVQDDDW---ISFNITNIRDAA 362

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1860589441 101 FVIEDGERIAQMVIAKHEQP--------SWQEVE-VLDE----TERGAGGFGHTGV 143
Cdd:PHA03124  363 AFFHAGDRIAQLIALEDKLEflgepdalPWKIVNsVQDEkknlSSRGDGGFGSSGK 418
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 32-119 4.30e-04

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 38.39  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860589441  32 EPVTLEPLQRCLVPTGLY-------IALPKGFEAQIRPRSGLaIKKGISVLNSpgTIDADY--RGEICIILINlsSETFV 102
Cdd:PRK02253   62 EPLEFDDDGWIRLEPGIYkvrynevVNIPEDHVGFAYPRSSL-LRNGCTLETA--VWDAGYegRGEGLLVVHN--PHGIR 136

                          90
                  ....*....|....*....
gi 1860589441 103 IEDGERIAQMVIAK--HEQ 119
Cdd:PRK02253  137 LERGARIAQLVFATldHET 155
 
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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