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Conserved domains on  [gi|2053333316|gb|QWR80069|]
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dUTP diphosphatase [Cronobacter sakazakii]

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;
2-152 7.70e-108

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 303.24  E-value: 7.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   2 MKKIDVKILDPRVGEQFPLPTYATSGSAGLDLRACLDESVELAPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKHGVV 81
Cdd:PRK00601    1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2053333316  82 LGNLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSGRK 152
Cdd:PRK00601   80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
2-152 7.70e-108

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 303.24  E-value: 7.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   2 MKKIDVKILDPRVGEQFPLPTYATSGSAGLDLRACLDESVELAPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKHGVV 81
Cdd:PRK00601    1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2053333316  82 LGNLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSGRK 152
Cdd:PRK00601   80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-151 6.79e-89

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: 254.94  E-value: 6.79e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   4 KIDVKILDPrvgeQFPLPTYATSGSAGLDLRACLDESVELAPGATTLLPTGLAIHIAdPSLAAVILPRSGLGHKHGVVLG 83
Cdd:COG0756     1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2053333316  84 NLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSGR 151
Cdd:COG0756    76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-151 1.66e-64

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: 193.60  E-value: 1.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   8 KILDPRVGEQFPLPTYATSGSAGLDLRACLDesVELAPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKHGVVLGNLVG 87
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053333316  88 LIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQ-AEFNLVEDFTATDRGEGGFGHSGR 151
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-150 1.83e-53

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 165.15  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  16 EQFPLPTYATSGSAGLDLRACLDESVElaPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKHGVVLGnlvGLIDSDYQG 95
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVK--PGGTVLVPTDISIPLPD-GTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2053333316  96 QLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSG 150
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 29-122 1.54e-30

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: 105.65  E-value: 1.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  29 AGLDLRACLD-ESVELAPGATTLLPTGLAIHIaDPSLAAVILPRSGLGhKHGVVLGNlVGLIDSDYQGQLMVSVWNRGQQ 107
Cdd:cd07557     1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                          90
                  ....*....|....*
gi 2053333316 108 SFTIEPGERIAQMVF 122
Cdd:cd07557    78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
2-152 7.70e-108

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 303.24  E-value: 7.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   2 MKKIDVKILDPRVGEQFPLPTYATSGSAGLDLRACLDESVELAPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKHGVV 81
Cdd:PRK00601    1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2053333316  82 LGNLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSGRK 152
Cdd:PRK00601   80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-151 6.79e-89

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: 254.94  E-value: 6.79e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   4 KIDVKILDPrvgeQFPLPTYATSGSAGLDLRACLDESVELAPGATTLLPTGLAIHIAdPSLAAVILPRSGLGHKHGVVLG 83
Cdd:COG0756     1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2053333316  84 NLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSGR 151
Cdd:COG0756    76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-151 1.66e-64

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: 193.60  E-value: 1.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   8 KILDPRVGEQFPLPTYATSGSAGLDLRACLDesVELAPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKHGVVLGNLVG 87
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053333316  88 LIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQ-AEFNLVEDFTATDRGEGGFGHSGR 151
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-150 1.83e-53

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 165.15  E-value: 1.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  16 EQFPLPTYATSGSAGLDLRACLDESVElaPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKHGVVLGnlvGLIDSDYQG 95
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVK--PGGTVLVPTDISIPLPD-GTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2053333316  96 QLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSG 150
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 29-122 1.54e-30

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: 105.65  E-value: 1.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  29 AGLDLRACLD-ESVELAPGATTLLPTGLAIHIaDPSLAAVILPRSGLGhKHGVVLGNlVGLIDSDYQGQLMVSVWNRGQQ 107
Cdd:cd07557     1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                          90
                  ....*....|....*
gi 2053333316 108 SFTIEPGERIAQMVF 122
Cdd:cd07557    78 PVVIKKGDRIAQLVF 92
PLN02547 PLN02547
dUTP pyrophosphatase
 2-150 4.04e-28

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 101.79  E-value: 4.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   2 MKKIDVKILDPRVGEQFPLPTYATSGSAGLDLRACLDESVelAPGATTLLPTGLAIHIAdPSLAAVILPRSGLGHKHGVV 81
Cdd:PLN02547   10 IQKPSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVV--PARGKALVPTDLSIAIP-EGTYARIAPRSGLAWKHSID 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2053333316  82 LGnlVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSG 150
Cdd:PLN02547   87 VG--AGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
PHA03094 PHA03094
dUTPase; Provisional
 2-150 8.49e-23

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 87.51  E-value: 8.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   2 MKKIDVKILdpRVGEQFPLPTYATSGSAGLDLRACLDESVElaPGATTLLPTGLAIHIADPSLAAvILPRSGLGHKHGVV 81
Cdd:PHA03094    1 MSNSPVRCV--KLSNFAKIPTRSSPKSAGYDLYSAYDYTVP--PKERILVKTDISLSIPKFCYGR-IAPRSGLSLNYGID 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2053333316  82 LGNlvGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSG 150
Cdd:PHA03094   76 IGG--GVIDEDYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 13-150 3.37e-20

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 81.57  E-value: 3.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  13 RVGEQFPLPTYATSGSAGLDLRACLDESVelAPGATTLLPTGLAIHIAdPSLAAVILPRSGLGHKHGVVLGnlVGLIDSD 92
Cdd:PHA02703   18 RLSPNATIPTRGSPGAAGLDLCSACDCIV--PAGCRCVVFTDLLIKLP-DGCYGRIAPRSGLAVKHFIDVG--AGVIDAD 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053333316  93 YQGQLMVSVWNRGQQSFTIEPGERIAQMV----FVPVVQaEFNLVEDftaTDRGEGGFGHSG 150
Cdd:PHA02703   93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLIceraAFPAVE-EVACLDD---TDRGAGGFGSTG 150
dut PRK13956
dUTP diphosphatase;
20-151 1.71e-19

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 79.07  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  20 LPTYATSGSAGLDLRACldESVELAPGATTLLPTGLAIHIaDPSLAAVILPRSGLGHKHGVVLGNLVGLIDSDY------ 93
Cdd:PRK13956   18 LPKRETAHAAGYDLKVA--ERTVIAPGEIKLVPTGVKAYM-QPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnpan 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2053333316  94 QGQLMVSVWNRGQQSFTIEPGERIAQMVFVPvvqaeFNLVEDFTATDRGEGGFGHSGR 151
Cdd:PRK13956   95 EGHIFAQMKNITDQEVVLEVGERIVQGVFMP-----FLIADGDQADGERTGGFGSTGK 147
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 5-152 2.16e-19

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 79.01  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316   5 IDVKILDPRVGEQFPLPTYATSGSAGLDLRACLDEsvELAPGATTLLPTGLAIHIADP--------SLAAVILPRSGLGh 76
Cdd:PTZ00143    3 LKILPLNDEVRELYKNHKTFHEGDSGLDLFIVKDQ--TIKPGETAFIKLGIKAAAFQKdedgsdgkNVSWLLFPRSSIS- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2053333316  77 KHGVVLGNLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPVVQAEFNLVEDFTATDRGEGGFGHSGRK 152
Cdd:PTZ00143   80 KTPLRLANSIGLIDAGYRGELIAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTGRL 155
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 10-125 3.25e-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: 50.01  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  10 LDPRVGEQFPLPTYATSG---------SAGLDLRACLDESVELAPGATTLLPTGLAIHIADpSLAAVILPRSGLGHKhGV 80
Cdd:TIGR02274  31 VDLRLGNEFRVFRNHTGAvidpenpkeAVSYLFEVEEGEEFVIPPGEFALATTLEYVKLPD-DVVGFLEGRSSLARL-GL 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2053333316  81 VLGNLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERIAQMVFVPV 125
Cdd:TIGR02274 109 FIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFERL 153
PHA03131 PHA03131
dUTPase; Provisional
 20-123 2.09e-06

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 45.75  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  20 LPTYatSGSAGLDLraCLDESVELAPGATTLLPTGLAIHIADPSLAAVILPRSGLGHKhGVvlgnlvgLIDSD--YQGQL 97
Cdd:PHA03131  126 PPQY--PDDAGFDV--SLPQDLVIFPTTTFTFTLSLCCPPISPHFVPVIFGRSGLASK-GL-------TVKPTkwRRSGL 193

                          90       100
                  ....*....|....*....|....*.
gi 2053333316  98 MVSVWNRGQQSFTIEPGERIAQMVFV 123
Cdd:PHA03131  194 QLKLYNYTDETIFLPAGSRICQVVFM 219
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 38-122 4.53e-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: 44.04  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  38 DESVELAPGATTLLPTGLAIHIADpSLAAVILPRSGLGhKHGVVLGNLVGLIDSDYQGQLMVSVWNRGQQSFTIEPGERI 117
Cdd:COG0717    67 GDGFILPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRI 144


                  ....*
gi 2053333316 118 AQMVF 122
Cdd:COG0717   145 AQLVF 149
PHA03124 PHA03124
dUTPase; Provisional
 26-151 3.01e-04

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 39.54  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053333316  26 SGSAGLDLRAclDESVELAPGATT--LLPTGLAIhiaDPSLAAVILPRSGLGHKHgvVLGNLVGLIDSDYqgqLMVSVWN 103
Cdd:PHA03124  288 AEDAGYDIRA--PEDCTILPGGSTriILPQKLAC---GKFRAAFILGRSSMNLKG--LLVDPEHVQDDDW---ISFNITN 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2053333316 104 RGQQSFTIEPGERIAQMV------------------FVPVVQAEFNlvedfTATDRGEGGFGHSGR 151
Cdd:PHA03124  358 IRDAAAFFHAGDRIAQLIaledkleflgepdalpwkIVNSVQDEKK-----NLSSRGDGGFGSSGK 418
PHA03131 PHA03131
dUTPase; Provisional
 45-115 1.10e-03

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 38.05  E-value: 1.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053333316  45 PGATTLLPTGLaiHIADPSLAAVIL----PRSGLGHkhgvvlgnlVGLIDSDYQGQLMVSVWNRGQQSFTIEPGE 115
Cdd:PHA03131   40 PGEPTVVPLGL--YIRRPPGFAFILwgstSKNVTCH---------TGLIDPGYRGELKLILLNKTKYNVTLRPGE 103
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 62-122 6.28e-03

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 35.31  E-value: 6.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053333316  62 PSLAAVILPRSGLgHKHGVVLGNLVGliDSDYQG--QLMVSVWNrgQQSFTIEPGERIAQMVF 122
Cdd:PRK02253   91 EDHVGFAYPRSSL-LRNGCTLETAVW--DAGYEGrgEGLLVVHN--PHGIRLERGARIAQLVF 148
 
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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