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Conserved domains on  [gi|2082267807|ref|XP_001692126|]
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dUTP pyrophosphatase [Chlamydomonas reinhardtii]

Protein Classification

dUTP diphosphatase( domain architecture ID 10791399)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 16-174 5.45e-94

dUTP pyrophosphatase


:

Pssm-ID: 215302  Cd Length: 157  Bit Score: 269.74  E-value: 5.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  16 MSAEKPPAKLARvdFEEKLLVKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSG 95
Cdd:PLN02547    1 PAVQEPPPKIQK--PSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082267807  96 LAVKNFIDTGAGVVDEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGVAKA 174
Cdd:PLN02547   79 LAWKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTGVALS 157
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 16-174 5.45e-94

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 269.74  E-value: 5.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  16 MSAEKPPAKLARvdFEEKLLVKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSG 95
Cdd:PLN02547    1 PAVQEPPPKIQK--PSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082267807  96 LAVKNFIDTGAGVVDEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGVAKA 174
Cdd:PLN02547   79 LAWKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTGVALS 157
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 33-171 6.85e-68

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: 202.85  E-value: 6.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  33 KLLVKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNF--IDTGAGVVD 110
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082267807 111 EDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIAT-PDVEEVEELDATDRGANGYGSTGV 171
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 41-170 1.20e-56

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 174.01  E-value: 1.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  41 DKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTGaGVVDEDYRGEVGVV 120
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2082267807 121 LFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTG 170
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 33-171 4.13e-55

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: 170.58  E-value: 4.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  33 KLLVKKLNDKATLPKRGSAGAAGYDLASA--EDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIdT---GAG 107
Cdd:COG0756     1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGI-TllnSPG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082267807 108 VVDEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGV 171
Cdd:COG0756    80 TIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 54-142 2.28e-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: 108.74  E-value: 2.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  54 AGYDLASAED---TVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTGAGVVDEDYRGEVGVVLFNHSDVDFV 130
Cdd:cd07557     1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARKGITVHNAGVIDPGYRGEITLELYNLGPEPVV 80

                          90
                  ....*....|..
gi 2082267807 131 VKVGDRVAQLVL 142
Cdd:cd07557    81 IKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 16-174 5.45e-94

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 269.74  E-value: 5.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  16 MSAEKPPAKLARvdFEEKLLVKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSG 95
Cdd:PLN02547    1 PAVQEPPPKIQK--PSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082267807  96 LAVKNFIDTGAGVVDEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGVAKA 174
Cdd:PLN02547   79 LAWKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTGVALS 157
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 33-171 6.85e-68

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: 202.85  E-value: 6.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  33 KLLVKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNF--IDTGAGVVD 110
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082267807 111 EDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIAT-PDVEEVEELDATDRGANGYGSTGV 171
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 32-171 1.27e-65

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 198.28  E-value: 1.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  32 EKLLVKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTGAGVVDE 111
Cdd:PHA02703   12 DALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDA 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807 112 DYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGV 171
Cdd:PHA02703   92 DYRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGS 151
PHA03094 PHA03094
dUTPase; Provisional
 36-171 3.18e-57

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 176.11  E-value: 3.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  36 VKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTGAGVVDEDYRG 115
Cdd:PHA03094    8 CVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVIDEDYRG 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2082267807 116 EVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGV 171
Cdd:PHA03094   88 NIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSGL 143
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 41-170 1.20e-56

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 174.01  E-value: 1.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  41 DKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTGaGVVDEDYRGEVGVV 120
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2082267807 121 LFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTG 170
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 33-171 4.13e-55

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: 170.58  E-value: 4.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  33 KLLVKKLNDKATLPKRGSAGAAGYDLASA--EDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIdT---GAG 107
Cdd:COG0756     1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGI-TllnSPG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082267807 108 VVDEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGV 171
Cdd:COG0756    80 TIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut PRK00601
dUTP diphosphatase;
33-171 2.87e-48

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 153.40  E-value: 2.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  33 KLLVKKLNDKATLPKRGSAGAAGYDLASAEDT--VIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTG--AGV 108
Cdd:PRK00601    7 KILDPRLGKEFPLPAYATEGSAGLDLRACLDEpvTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGnlPGT 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2082267807 109 VDEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEVEELDATDRGANGYGSTGV 171
Cdd:PRK00601   87 IDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGR 149
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 54-142 2.28e-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: 108.74  E-value: 2.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  54 AGYDLASAED---TVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTGAGVVDEDYRGEVGVVLFNHSDVDFV 130
Cdd:cd07557     1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARKGITVHNAGVIDPGYRGEITLELYNLGPEPVV 80

                          90
                  ....*....|..
gi 2082267807 131 VKVGDRVAQLVL 142
Cdd:cd07557    81 IKKGDRIAQLVF 92
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 51-171 7.35e-15

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 67.84  E-value: 7.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  51 AGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGR---------VAPRSGLA-----VKNFIdtgaGVVDEDYRGE 116
Cdd:PTZ00143   24 EGDSGLDLFIVKDQTIKPGETAFIKLGIKAAAFQKDEDGsdgknvswlLFPRSSISktplrLANSI----GLIDAGYRGE 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2082267807 117 VGVVLFNHSDVDFVVKVGDRVAQLVL---ERIAtpdVEEVEELDATDRGANGYGSTGV 171
Cdd:PTZ00143  100 LIAAVDNIKDEPYTIKKGDRLVQLVSfdgEPIT---FELVDELDETTRGEGGFGSTGR 154
dut PRK13956
dUTP diphosphatase;
35-171 1.28e-11

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 59.04  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  35 LVKKLNDKATLPKRGSAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGT----YGRVA-PR-SGLAVKNFIdtgaGV 108
Cdd:PRK13956    8 LVSSFTNENLLPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEvlylYDRSSnPRkKGLVLINSV----GV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082267807 109 VDEDY------RGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPDVEEveeldATDRGANGYGSTGV 171
Cdd:PRK13956   84 IDGDYygnpanEGHIFAQMKNITDQEVVLEVGERIVQGVFMPFLIADGDQ-----ADGERTGGFGSTGK 147
PHA03124 PHA03124
dUTPase; Provisional
 46-171 2.28e-08

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 52.25  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  46 PKRgsAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKNFIDTGAGVVDEDYrgeVGVVLFNHS 125
Cdd:PHA03124  285 PKE--AEDAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLKGLLVDPEHVQDDDW---ISFNITNIR 359

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2082267807 126 DVDFVVKVGDRVAQLV-----LERIATPD------VEEV--EELDATDRGANGYGSTGV 171
Cdd:PHA03124  360 DAAAFFHAGDRIAQLIaledkLEFLGEPDalpwkiVNSVqdEKKNLSSRGDGGFGSSGK 418
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 80-148 9.60e-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: 43.66  E-value: 9.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082267807  80 IRCPKGTYGRVAPRS-----GLavknFIDTGAGVVDEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATP 148
Cdd:COG0717    86 VRLPDDLVAFLEGRSslarlGL----FVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQLVFFRLSGP 155
PHA03131 PHA03131
dUTPase; Provisional
 54-141 1.50e-03

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 38.05  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  54 AGYDLASAEDTVIPAKGKGIVKtgLSIRCPkGTYGRVAP----RSGLAVKnfidtGAGV-VDEDYRGEVGVVLFNHSDVD 128
Cdd:PHA03131  133 AGFDVSLPQDLVIFPTTTFTFT--LSLCCP-PISPHFVPvifgRSGLASK-----GLTVkPTKWRRSGLQLKLYNYTDET 204

                          90
                  ....*....|...
gi 2082267807 129 FVVKVGDRVAQLV 141
Cdd:PHA03131  205 IFLPAGSRICQVV 217
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 32-171 4.92e-03

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: 36.14  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082267807  32 EKLLVKKLNDKATLPKRG-SAGAAGYDLASAEDTVIPAKGKGIVKTGLSIRCPKGTYGRVAPRSGLAVKN-FIDTGAGVV 109
Cdd:TIGR02274  38 EFRVFRNHTGAVIDPENPkEAVSYLFEVEEGEEFVIPPGEFALATTLEYVKLPDDVVGFLEGRSSLARLGlFIHVTAGRI 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082267807 110 DEDYRGEVGVVLFNHSDVDFVVKVGDRVAQLVLERIATPdveevEELDATDRGANGYGSTGV 171
Cdd:TIGR02274 118 DPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFERLSSP-----AERPYNGRSGKYQGQRGV 174
 
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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