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Conserved domains on  [gi|1491308471|gb|RLI72198|]
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MAG: deoxyuridine 5'-triphosphate nucleotidohydrolase [Candidatus Gerdarchaeota archaeon]

Protein Classification

dCTP deaminase/dUTPase family protein( domain architecture ID 272)

dCTP deaminase/dUTPase family protein similar to archaeal deoxycytidine triphosphate (dCTP) deaminase that catalyzes the deamination of dCTP to dUTP, and to Yarrowia lipolytica deoxyuridine 5'-triphosphate (dUTP) nucleotidohydrolase that catalyzes the hydrolysis of dUTP to form dUMP

CATH:  2.70.40.10
Gene Ontology:  GO:0009165
SCOP:  3001957

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
trimeric_dUTPase super family cl00493
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 30-168 7.07e-60

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.


The actual alignment was detected with superfamily member PRK02253:

Pssm-ID: 444938  Cd Length: 167  Bit Score: 183.23  E-value: 7.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  30 DKQVQVNGFDLTVKEVFLLKGEGVIDFDNskRILPEYEPVPLIDNDYWSLPAGSYVIRYNEIVSVPLDALGIIQPRSTLL 109
Cdd:PRK02253   27 DDQVQPNGVDLTLGEVEEQEGPGRIDFDN--RKLPEREPLEFDDDGWIRLEPGIYKVRYNEVVNIPEDHVGFAYPRSSLL 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308471 110 RMGGTIVGAWWDAGYSGRGQGLMILTRP--VKIYKNARVAQIVFLRTKKVTKGYQGTYQNE 168
Cdd:PRK02253  105 RNGCTLETAVWDAGYEGRGEGLLVVHNPhgIRLERGARIAQLVFATLDHETEGYSGSYQGE 165
 
Name Accession Description Interval E-value
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 30-168 7.07e-60

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 183.23  E-value: 7.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  30 DKQVQVNGFDLTVKEVFLLKGEGVIDFDNskRILPEYEPVPLIDNDYWSLPAGSYVIRYNEIVSVPLDALGIIQPRSTLL 109
Cdd:PRK02253   27 DDQVQPNGVDLTLGEVEEQEGPGRIDFDN--RKLPEREPLEFDDDGWIRLEPGIYKVRYNEVVNIPEDHVGFAYPRSSLL 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308471 110 RMGGTIVGAWWDAGYSGRGQGLMILTRP--VKIYKNARVAQIVFLRTKKVTKGYQGTYQNE 168
Cdd:PRK02253  105 RNGCTLETAVWDAGYEGRGEGLLVVHNPhgIRLERGARIAQLVFATLDHETEGYSGSYQGE 165
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 20-168 3.02e-33

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 116.08  E-value: 3.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  20 KTIIRDAVDfDKQVQVNGFDLTVKEVFLLKGE---GVIDFDnsKRILPEYEPVPliDNDYWSLPAGSYVI-RYNEIVSVP 95
Cdd:COG0717    15 GRIVIEPFD-EEQVQPNSYDLRLGNEFRVFENhnsGVIDPK--KRDLTEEIEIE--PGDGFILPPGEFYLaRTLEYVRLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  96 LDALGIIQPRSTLLRMGGTIV--GAWWDAGYSGRGQGLMI--LTRPVKIYKNARVAQIVFLRTK-KVTKGY--QGTYQNE 168
Cdd:COG0717    90 DDLVAFLEGRSSLARLGLFVHttAGVIDPGFEGRITLELSntGPLPIKLYPGMRIAQLVFFRLSgPAERPYgrGGKYQGQ 169
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 73-151 1.64e-15

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: 67.90  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  73 DNDYWSLPAGS-YVIRYNEIVSVPLDALGIIQPRSTLLRMGGTI-VGAWWDAGYSGRGQGLMILTR--PVKIYKNARVAQ 148
Cdd:cd07557    10 DFEGIVLPPGEtVLVPTGEAIELPEGYVGLVFPRSSLARKGITVhNAGVIDPGYRGEITLELYNLGpePVVIKKGDRIAQ 89


                  ...
gi 1491308471 149 IVF 151
Cdd:cd07557    90 LVF 92
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 32-167 1.27e-13

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: 65.03  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  32 QVQVNGFDLTVKEVFLL---KGEGVIDFDNSKRILPEYEPVPliDNDYWSLPAGSYV-IRYNEIVSVPLDALGIIQPRST 107
Cdd:TIGR02274  25 QLQPAGVDLRLGNEFRVfrnHTGAVIDPENPKEAVSYLFEVE--EGEEFVIPPGEFAlATTLEYVKLPDDVVGFLEGRSS 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491308471 108 LLRMGGTI--VGAWWDAGYSGRgQGLMIL---TRPVKIYKNARVAQIVFLRT----KKVTKGYQGTYQN 167
Cdd:TIGR02274 103 LARLGLFIhvTAGRIDPGFEGN-ITLELFnagKLPVKLRPGMRIAQLVFERLsspaERPYNGRSGKYQG 170
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 79-155 3.22e-09

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 52.29  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  79 LPAGSYVIRYNEI-VSVPLDALGIIQPRSTLLRMGGTIVGAWWDAGYSGRGQ-GLMILTR-PVKIYKNARVAQIVFLRTK 155
Cdd:pfam00692  26 VKPGGTVLVPTDIsIPLPDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKvVLFNLGKsDFTIKKGDRIAQLIFEPIL 105
 
Name Accession Description Interval E-value
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 30-168 7.07e-60

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 183.23  E-value: 7.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  30 DKQVQVNGFDLTVKEVFLLKGEGVIDFDNskRILPEYEPVPLIDNDYWSLPAGSYVIRYNEIVSVPLDALGIIQPRSTLL 109
Cdd:PRK02253   27 DDQVQPNGVDLTLGEVEEQEGPGRIDFDN--RKLPEREPLEFDDDGWIRLEPGIYKVRYNEVVNIPEDHVGFAYPRSSLL 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491308471 110 RMGGTIVGAWWDAGYSGRGQGLMILTRP--VKIYKNARVAQIVFLRTKKVTKGYQGTYQNE 168
Cdd:PRK02253  105 RNGCTLETAVWDAGYEGRGEGLLVVHNPhgIRLERGARIAQLVFATLDHETEGYSGSYQGE 165
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 20-168 3.02e-33

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 116.08  E-value: 3.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  20 KTIIRDAVDfDKQVQVNGFDLTVKEVFLLKGE---GVIDFDnsKRILPEYEPVPliDNDYWSLPAGSYVI-RYNEIVSVP 95
Cdd:COG0717    15 GRIVIEPFD-EEQVQPNSYDLRLGNEFRVFENhnsGVIDPK--KRDLTEEIEIE--PGDGFILPPGEFYLaRTLEYVRLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  96 LDALGIIQPRSTLLRMGGTIV--GAWWDAGYSGRGQGLMI--LTRPVKIYKNARVAQIVFLRTK-KVTKGY--QGTYQNE 168
Cdd:COG0717    90 DDLVAFLEGRSSLARLGLFVHttAGVIDPGFEGRITLELSntGPLPIKLYPGMRIAQLVFFRLSgPAERPYgrGGKYQGQ 169
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 73-151 1.64e-15

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: 67.90  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  73 DNDYWSLPAGS-YVIRYNEIVSVPLDALGIIQPRSTLLRMGGTI-VGAWWDAGYSGRGQGLMILTR--PVKIYKNARVAQ 148
Cdd:cd07557    10 DFEGIVLPPGEtVLVPTGEAIELPEGYVGLVFPRSSLARKGITVhNAGVIDPGYRGEITLELYNLGpePVVIKKGDRIAQ 89


                  ...
gi 1491308471 149 IVF 151
Cdd:cd07557    90 LVF 92
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 32-167 1.27e-13

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: 65.03  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  32 QVQVNGFDLTVKEVFLL---KGEGVIDFDNSKRILPEYEPVPliDNDYWSLPAGSYV-IRYNEIVSVPLDALGIIQPRST 107
Cdd:TIGR02274  25 QLQPAGVDLRLGNEFRVfrnHTGAVIDPENPKEAVSYLFEVE--EGEEFVIPPGEFAlATTLEYVKLPDDVVGFLEGRSS 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491308471 108 LLRMGGTI--VGAWWDAGYSGRgQGLMIL---TRPVKIYKNARVAQIVFLRT----KKVTKGYQGTYQN 167
Cdd:TIGR02274 103 LARLGLFIhvTAGRIDPGFEGN-ITLELFnagKLPVKLRPGMRIAQLVFERLsspaERPYNGRSGKYQG 170
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 79-155 3.22e-09

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 52.29  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  79 LPAGSYVIRYNEI-VSVPLDALGIIQPRSTLLRMGGTIVGAWWDAGYSGRGQ-GLMILTR-PVKIYKNARVAQIVFLRTK 155
Cdd:pfam00692  26 VKPGGTVLVPTDIsIPLPDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKvVLFNLGKsDFTIKKGDRIAQLIFEPIL 105
dut PHA01707
2'-deoxyuridine 5'-triphosphatase
 33-168 1.03e-04

2'-deoxyuridine 5'-triphosphatase


Pssm-ID: 107053  Cd Length: 158  Bit Score: 40.69  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491308471  33 VQVNGFDLTV-KEVFLLKGEGVIDFDNSKRILPeYEPVPLIDNDYwslpagsyviryneiVSVPLDALGIIQPRSTLLRM 111
Cdd:PHA01707   27 IRENGVDLKIgNEIVRIKENMEKEVGDEFIIYP-HEHVLLTTKEY---------------IKLPNDIIAFCNLRSTFARK 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1491308471 112 GGTIVGAWWDAGYSGRGQGLMILTR-PVKIYKNARVAQIVFLRT-KKVTKGYQGTYQNE 168
Cdd:PHA01707   91 GLLIPPTIVDAGFEGQLTIELVGSSiPVKLKSGERFLHLIFARTlTPVEKPYNGKYQKQ 149
 
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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