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Conserved domains on  [gi|1447699799|ref|NP_312542|]
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deoxyuridinetriphosphatase [Escherichia coli O157:H7 str. Sakai]

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 1.44e-106

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 300.16  E-value: 1.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799   2 MKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKHGIV 81
Cdd:PRK00601    1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699799  82 LGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ 152
Cdd:PRK00601   80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
2-152 1.44e-106

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 300.16  E-value: 1.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799   2 MKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKHGIV 81
Cdd:PRK00601    1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699799  82 LGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ 152
Cdd:PRK00601   80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-151 9.03e-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: 9.03e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799   4 KIDVKILDPrvgkEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIAdPSLAAMMLPRSGLGHKHGIVLG 83
Cdd:COG0756     1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699799  84 NLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGR 151
Cdd:COG0756    76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-151 2.21e-66

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: 198.23  E-value: 2.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799   8 KILDPRVGKEFPLPTYATSGSAGLDLRACLDdaVELAPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKHGIVLGNLVG 87
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699799  88 LIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQ-AEFNLVEDFDATDRGEGGFGHSGR 151
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-150 2.33e-56

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 172.47  E-value: 2.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  16 KEFPLPTYATSGSAGLDLRACLDDAVElaPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKHGIVLGnlvGLIDSDYQG 95
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVK--PGGTVLVPTDISIPLPD-GTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1447699799  96 QLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSG 150
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 29-122 3.87e-31

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: 107.19  E-value: 3.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  29 AGLDLRACLD-DAVELAPGDTTLVPTGLAIHIaDPSLAAMMLPRSGLGhKHGIVLGNlVGLIDSDYQGQLMISVWNRGQD 107
Cdd:cd07557     1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                          90
                  ....*....|....*
gi 1447699799 108 SFTIQPGERIAQMIF 122
Cdd:cd07557    78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
2-152 1.44e-106

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 300.16  E-value: 1.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799   2 MKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKHGIV 81
Cdd:PRK00601    1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699799  82 LGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ 152
Cdd:PRK00601   80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 4-151 9.03e-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: 9.03e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799   4 KIDVKILDPrvgkEFPLPTYATSGSAGLDLRACLDDAVELAPGDTTLVPTGLAIHIAdPSLAAMMLPRSGLGHKHGIVLG 83
Cdd:COG0756     1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699799  84 NLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGR 151
Cdd:COG0756    76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 8-151 2.21e-66

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: 198.23  E-value: 2.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799   8 KILDPRVGKEFPLPTYATSGSAGLDLRACLDdaVELAPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKHGIVLGNLVG 87
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699799  88 LIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQ-AEFNLVEDFDATDRGEGGFGHSGR 151
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-150 2.33e-56

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 172.47  E-value: 2.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  16 KEFPLPTYATSGSAGLDLRACLDDAVElaPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKHGIVLGnlvGLIDSDYQG 95
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVK--PGGTVLVPTDISIPLPD-GTYGRIFPRSGLAAKGLIVVP---GVIDSDYRG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1447699799  96 QLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSG 150
Cdd:pfam00692  75 EVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 29-122 3.87e-31

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: 107.19  E-value: 3.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  29 AGLDLRACLD-DAVELAPGDTTLVPTGLAIHIaDPSLAAMMLPRSGLGhKHGIVLGNlVGLIDSDYQGQLMISVWNRGQD 107
Cdd:cd07557     1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                          90
                  ....*....|....*
gi 1447699799 108 SFTIQPGERIAQMIF 122
Cdd:cd07557    78 PVVIKKGDRIAQLVF 92
PLN02547 PLN02547
dUTP pyrophosphatase
 20-150 2.29e-29

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 104.88  E-value: 2.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  20 LPTYATSGSAGLDLRACLDDAVelAPGDTTLVPTGLAIHIAdPSLAAMMLPRSGLGHKHGIVLGnlVGLIDSDYQGQLMI 99
Cdd:PLN02547   28 LPSRGSALAAGYDLSSAYDTVV--PARGKALVPTDLSIAIP-EGTYARIAPRSGLAWKHSIDVG--AGVIDADYRGPVGV 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1447699799 100 SVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSG 150
Cdd:PLN02547  103 ILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
PHA03094 PHA03094
dUTPase; Provisional
 20-150 7.26e-25

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 92.91  E-value: 7.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  20 LPTYATSGSAGLDLRACLDDAVElaPGDTTLVPTGLAIHIADPSLAAMMlPRSGLGHKHGIVLGNlvGLIDSDYQGQLMI 99
Cdd:PHA03094   17 IPTRSSPKSAGYDLYSAYDYTVP--PKERILVKTDISLSIPKFCYGRIA-PRSGLSLNYGIDIGG--GVIDEDYRGNIGV 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1447699799 100 SVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSG 150
Cdd:PHA03094   92 IFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 13-150 1.59e-21

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 85.04  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  13 RVGKEFPLPTYATSGSAGLDLRACLDDAVelAPGDTTLVPTGLAIHIAdPSLAAMMLPRSGLGHKHGIVLGnlVGLIDSD 92
Cdd:PHA02703   18 RLSPNATIPTRGSPGAAGLDLCSACDCIV--PAGCRCVVFTDLLIKLP-DGCYGRIAPRSGLAVKHFIDVG--AGVIDAD 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699799  93 YQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSG 150
Cdd:PHA02703   93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTG 150
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 27-151 3.86e-21

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 83.63  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  27 GSAGLDLrACLDDAVeLAPGDTTLVPTGLAIHIADP--------SLAAMMLPRSGLGhKHGIVLGNLVGLIDSDYQGQLM 98
Cdd:PTZ00143   25 GDSGLDL-FIVKDQT-IKPGETAFIKLGIKAAAFQKdedgsdgkNVSWLLFPRSSIS-KTPLRLANSIGLIDAGYRGELI 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1447699799  99 ISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGR 151
Cdd:PTZ00143  102 AAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTGR 154
dut PRK13956
dUTP diphosphatase;
20-151 2.01e-18

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 76.37  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  20 LPTYATSGSAGLDLRACldDAVELAPGDTTLVPTGLAIHIaDPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDY------ 93
Cdd:PRK13956   18 LPKRETAHAAGYDLKVA--ERTVIAPGEIKLVPTGVKAYM-QPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnpan 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699799  94 QGQLMISVWNRGQDSFTIQPGERIAQMIFVPvvqaeFNLVEDFDATDRGEGGFGHSGR 151
Cdd:PRK13956   95 EGHIFAQMKNITDQEVVLEVGERIVQGVFMP-----FLIADGDQADGERTGGFGSTGK 147
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 10-125 1.14e-10

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: 56.55  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  10 LDPRVGKEFPLPTYATSG---------SAGLDLRACLDDAVELAPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGHKhGI 80
Cdd:TIGR02274  31 VDLRLGNEFRVFRNHTGAvidpenpkeAVSYLFEVEEGEEFVIPPGEFALATTLEYVKLPD-DVVGFLEGRSSLARL-GL 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1447699799  81 VLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPV 125
Cdd:TIGR02274 109 FIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFERL 153
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 38-122 1.87e-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: 47.90  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  38 DDAVELAPGDTTLVPTGLAIHIADpSLAAMMLPRSGLGhKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERI 117
Cdd:COG0717    67 GDGFILPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRI 144


                  ....*
gi 1447699799 118 AQMIF 122
Cdd:COG0717   145 AQLVF 149
PHA03131 PHA03131
dUTPase; Provisional
 20-123 4.56e-05

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 41.90  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  20 LPTYatSGSAGLDLraCLDDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKhGIvlgnlvgLIDSD--YQGQL 97
Cdd:PHA03131  126 PPQY--PDDAGFDV--SLPQDLVIFPTTTFTFTLSLCCPPISPHFVPVIFGRSGLASK-GL-------TVKPTkwRRSGL 193

                          90       100
                  ....*....|....*....|....*.
gi 1447699799  98 MISVWNRGQDSFTIQPGERIAQMIFV 123
Cdd:PHA03131  194 QLKLYNYTDETIFLPAGSRICQVVFM 219
PHA03131 PHA03131
dUTPase; Provisional
 45-115 9.79e-05

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 40.75  E-value: 9.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699799  45 PGDTTLVPTGLaiHIADPSLAAMML----PRSGLGHkhgivlgnlVGLIDSDYQGQLMISVWNRGQDSFTIQPGE 115
Cdd:PHA03131   40 PGEPTVVPLGL--YIRRPPGFAFILwgstSKNVTCH---------TGLIDPGYRGELKLILLNKTKYNVTLRPGE 103
PHA03124 PHA03124
dUTPase; Provisional
 26-151 2.68e-03

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 36.84  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699799  26 SGSAGLDLRACLDdaVELAPGDTTLVPTGLAIHIAdPSLAAMMLPRSGLGHKHgiVLGNLVGLIDSDYqgqLMISVWNRG 105
Cdd:PHA03124  288 AEDAGYDIRAPED--CTILPGGSTRIILPQKLACG-KFRAAFILGRSSMNLKG--LLVDPEHVQDDDW---ISFNITNIR 359

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699799 106 QDSFTIQPGERIAQMIfvpVVQAEFNLVEDFDA----------------TDRGEGGFGHSGR 151
Cdd:PHA03124  360 DAAAFFHAGDRIAQLI---ALEDKLEFLGEPDAlpwkivnsvqdekknlSSRGDGGFGSSGK 418
 
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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