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Conserved domains on  [gi|16767016|ref|NP_462631|]
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deoxyuridinetriphosphatase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

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 1.20e-106

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 300.16  E-value: 1.20e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016    1 MKKIDVKILDPRVGQQFPLPTYATSGSAGLDLRACLDDAVELAPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16767016   81 LGNLVGLIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSGRK 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-151 1.20e-106

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 300.16  E-value: 1.20e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016    1 MKKIDVKILDPRVGQQFPLPTYATSGSAGLDLRACLDDAVELAPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16767016   81 LGNLVGLIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSGRK 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 3-150 2.38e-88

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: 253.79  E-value: 2.38e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   3 KIDVKILDPrvgqQFPLPTYATSGSAGLDLRACLDDAVELAPGATTLVPTGLAIHIAdPSLAAVMLPRSGLGHKHGIVLG 82
Cdd:COG0756   1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16767016  83 NLVGLIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSGR 150
Cdd:COG0756  76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 7-150 1.46e-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: 1.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016     7 KILDPRVGQQFPLPTYATSGSAGLDLRACLDdaVELAPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKHGIVLGNLVG 86
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16767016    87 LIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQ-AEFNLVEAFDATERGEGGFGHSGR 150
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 17-149 4.56e-55

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 169.01  E-value: 4.56e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016    17 FPLPTYATSGSAGLDLRACLDDAVElaPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKHGIVLGnlvGLIDSDYQGQL 96
Cdd:pfam00692   3 AEIPTPGSPGDAGYDLYAPYDLTVK--PGGTVLVPTDISIPLPD-GTYGRIFPRSGLAAKGLIVVP---GVIDSDYRGEV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16767016    97 MVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSG 149
Cdd:pfam00692  77 KVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 28-121 5.60e-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: 106.81  E-value: 5.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016  28 AGLDLRACLD-DAVELAPGATTLVPTGLAIHIaDPSLAAVMLPRSGLGhKHGIVLGNlVGLIDSDYQGQLMVSIWNRGQD 106
Cdd:cd07557   1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                        90
                ....*....|....*
gi 16767016 107 SFTIEPGERIAQMVF 121
Cdd:cd07557  78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-151 1.20e-106

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 300.16  E-value: 1.20e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016    1 MKKIDVKILDPRVGQQFPLPTYATSGSAGLDLRACLDDAVELAPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKHGIV 80
Cdd:PRK00601   1 MKKIDVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPD-GYEAQILPRSGLAHKHGIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16767016   81 LGNLVGLIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSGRK 151
Cdd:PRK00601  80 LGNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 3-150 2.38e-88

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: 253.79  E-value: 2.38e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   3 KIDVKILDPrvgqQFPLPTYATSGSAGLDLRACLDDAVELAPGATTLVPTGLAIHIAdPSLAAVMLPRSGLGHKHGIVLG 82
Cdd:COG0756   1 KVKIKRLDE----DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALP-PGYEAQVRPRSGLALKHGITLL 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16767016  83 NLVGLIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSGR 150
Cdd:COG0756  76 NSPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 7-150 1.46e-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: 1.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016     7 KILDPRVGQQFPLPTYATSGSAGLDLRACLDdaVELAPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKHGIVLGNLVG 86
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAED--VTIPPGERALVPTGIAIELPD-GYYGRVAPRSGLALKHGVTIDNSPG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16767016    87 LIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQ-AEFNLVEAFDATERGEGGFGHSGR 150
Cdd:TIGR00576  78 VIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 17-149 4.56e-55

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 169.01  E-value: 4.56e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016    17 FPLPTYATSGSAGLDLRACLDDAVElaPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKHGIVLGnlvGLIDSDYQGQL 96
Cdd:pfam00692   3 AEIPTPGSPGDAGYDLYAPYDLTVK--PGGTVLVPTDISIPLPD-GTYGRIFPRSGLAAKGLIVVP---GVIDSDYRGEV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16767016    97 MVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSG 149
Cdd:pfam00692  77 KVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 28-121 5.60e-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: 106.81  E-value: 5.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016  28 AGLDLRACLD-DAVELAPGATTLVPTGLAIHIaDPSLAAVMLPRSGLGhKHGIVLGNlVGLIDSDYQGQLMVSIWNRGQD 106
Cdd:cd07557   1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIEL-PEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPE 77

                        90
                ....*....|....*
gi 16767016 107 SFTIEPGERIAQMVF 121
Cdd:cd07557  78 PVVIKKGDRIAQLVF 92
PLN02547 PLN02547
dUTP pyrophosphatase
 19-149 3.28e-28

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 101.79  E-value: 3.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   19 LPTYATSGSAGLDLRACLDDAVelAPGATTLVPTGLAIHIADPSLAAVMlPRSGLGHKHGIVLGnlVGLIDSDYQGQLMV 98
Cdd:PLN02547  28 LPSRGSALAAGYDLSSAYDTVV--PARGKALVPTDLSIAIPEGTYARIA-PRSGLAWKHSIDVG--AGVIDADYRGPVGV 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16767016   99 SIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSG 149
Cdd:PLN02547 103 ILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
PHA03094 PHA03094
dUTPase; Provisional
 19-149 5.48e-24

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 90.59  E-value: 5.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   19 LPTYATSGSAGLDLRACLDDAVElaPGATTLVPTGLAIHIADPSLAAVMlPRSGLGHKHGIVLGNlvGLIDSDYQGQLMV 98
Cdd:PHA03094  17 IPTRSSPKSAGYDLYSAYDYTVP--PKERILVKTDISLSIPKFCYGRIA-PRSGLSLNYGIDIGG--GVIDEDYRGNIGV 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16767016   99 SIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSG 149
Cdd:PHA03094  92 IFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 12-149 8.12e-23

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 88.12  E-value: 8.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   12 RVGQQFPLPTYATSGSAGLDLRACLDDAVelAPGATTLVPTGLAIHIADPSLAAVMlPRSGLGHKHGIVLGnlVGLIDSD 91
Cdd:PHA02703  18 RLSPNATIPTRGSPGAAGLDLCSACDCIV--PAGCRCVVFTDLLIKLPDGCYGRIA-PRSGLAVKHFIDVG--AGVIDAD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16767016   92 YQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSG 149
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTG 150
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 26-151 6.83e-21

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 82.86  E-value: 6.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   26 GSAGLDLrACLDDAVeLAPGATTLVPTGLAIHIADP--------SLAAVMLPRSGLGhKHGIVLGNLVGLIDSDYQGQLM 97
Cdd:PTZ00143  25 GDSGLDL-FIVKDQT-IKPGETAFIKLGIKAAAFQKdedgsdgkNVSWLLFPRSSIS-KTPLRLANSIGLIDAGYRGELI 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16767016   98 VSIWNRGQDSFTIEPGERIAQMVFVPVVQAEFNLVEAFDATERGEGGFGHSGRK 151
Cdd:PTZ00143 102 AAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTGRL 155
dut PRK13956
dUTP diphosphatase;
19-150 1.57e-19

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 79.07  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   19 LPTYATSGSAGLDLRACldDAVELAPGATTLVPTGLAIHIaDPSLAAVMLPRSGLGHKHGIVLGNLVGLIDSDY------ 92
Cdd:PRK13956  18 LPKRETAHAAGYDLKVA--ERTVIAPGEIKLVPTGVKAYM-QPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnpan 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16767016   93 QGQLMVSIWNRGQDSFTIEPGERIAQMVFVPvvqaeFNLVEAFDATERGEGGFGHSGR 150
Cdd:PRK13956  95 EGHIFAQMKNITDQEVVLEVGERIVQGVFMP-----FLIADGDQADGERTGGFGSTGK 147
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 9-124 3.04e-09

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: 52.70  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016     9 LDPRVGQQFPLPTYATSG---------SAGLDLRACLDDAVELAPGATTLVPTGLAIHIADpSLAAVMLPRSGLGHKhGI 79
Cdd:TIGR02274  31 VDLRLGNEFRVFRNHTGAvidpenpkeAVSYLFEVEEGEEFVIPPGEFALATTLEYVKLPD-DVVGFLEGRSSLARL-GL 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 16767016    80 VLGNLVGLIDSDYQGQLMVSIWNRGQDSFTIEPGERIAQMVFVPV 124
Cdd:TIGR02274 109 FIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFERL 153
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 37-121 1.83e-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: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016  37 DDAVELAPGATTLVPTGLAIHIADpSLAAVMLPRSGLGhKHGIVLGNLVGLIDSDYQGQLMVSIWNRGQDSFTIEPGERI 116
Cdd:COG0717  67 GDGFILPPGEFYLARTLEYVRLPD-DLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRI 144


                ....*
gi 16767016 117 AQMVF 121
Cdd:COG0717 145 AQLVF 149
PHA03131 PHA03131
dUTPase; Provisional
 19-122 9.67e-06

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 43.83  E-value: 9.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   19 LPTYatSGSAGLDLraCLDDAVELAPGATTLVPTGLAIHIADPSLAAVMLPRSGLGHKhGIvlgnlvgLIDSD--YQGQL 96
Cdd:PHA03131 126 PPQY--PDDAGFDV--SLPQDLVIFPTTTFTFTLSLCCPPISPHFVPVIFGRSGLASK-GL-------TVKPTkwRRSGL 193

                         90       100
                 ....*....|....*....|....*.
gi 16767016   97 MVSIWNRGQDSFTIEPGERIAQMVFV 122
Cdd:PHA03131 194 QLKLYNYTDETIFLPAGSRICQVVFM 219
PHA03131 PHA03131
dUTPase; Provisional
 44-114 9.16e-04

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 38.05  E-value: 9.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16767016   44 PGATTLVPTGLaiHIADPSLAAVML----PRSGLGHkhgivlgnlVGLIDSDYQGQLMVSIWNRGQDSFTIEPGE 114
Cdd:PHA03131  40 PGEPTVVPLGL--YIRRPPGFAFILwgstSKNVTCH---------TGLIDPGYRGELKLILLNKTKYNVTLRPGE 103
PHA03124 PHA03124
dUTPase; Provisional
 25-150 1.94e-03

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 37.23  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767016   25 SGSAGLDLRACLDdaVELAPGATTLVPTGLAIHIAdPSLAAVMLPRSGLGHKHgiVLGNLVGLIDSDYqgqLMVSIWNRG 104
Cdd:PHA03124 288 AEDAGYDIRAPED--CTILPGGSTRIILPQKLACG-KFRAAFILGRSSMNLKG--LLVDPEHVQDDDW---ISFNITNIR 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16767016  105 QDSFTIEPGERIAQMVfvpVVQAEFNLVEAFDA----------------TERGEGGFGHSGR 150
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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