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Conserved domains on  [gi|1958763444|ref|XP_038961577|]
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deoxyuridine 5'-triphosphate nucleotidohydrolase isoform X12 [Rattus norvegicus]

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 ...
 18-110 3.15e-49

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 PLN02547:

Pssm-ID: 444938  Cd Length: 157  Bit Score: 153.80  E-value: 3.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  18 PAGPRALQATTCT-----------APRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIL 86
Cdd:PLN02547   50 PARGKALVPTDLSiaipegtyariAPRSGLAWKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIV 129

                          90       100
                  ....*....|....*....|....
gi 1958763444  87 YPDLEEVQTLDNTERGSGGFGSTG 110
Cdd:PLN02547  130 TPEVVEVEDLDATVRGAGGFGSTG 153
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 18-110 3.15e-49

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 153.80  E-value: 3.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  18 PAGPRALQATTCT-----------APRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIL 86
Cdd:PLN02547   50 PARGKALVPTDLSiaipegtyariAPRSGLAWKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIV 129

                          90       100
                  ....*....|....*....|....
gi 1958763444  87 YPDLEEVQTLDNTERGSGGFGSTG 110
Cdd:PLN02547  130 TPEVVEVEDLDATVRGAGGFGSTG 153
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 31-111 4.33e-45

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: 142.76  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  31 APRSGLAVKHF--IDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILY-PDLEEVQTLDNTERGSGGFG 107
Cdd:TIGR00576  59 APRSGLALKHGvtIDNSPGVIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFG 138


                  ....
gi 1958763444 108 STGK 111
Cdd:TIGR00576 139 STGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 31-110 3.09e-40

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 129.72  E-value: 3.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  31 APRSGLAVKHFIDVGaGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGSTG 110
Cdd:pfam00692  51 FPRSGLAAKGLIVVP-GVIDSDYRGEVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 32-111 3.23e-39

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: 127.83  E-value: 3.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  32 PRSGLAVKHFIDVG--AGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGST 109
Cdd:COG0756    62 PRSGLALKHGITLLnsPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGST 141


                  ..
gi 1958763444 110 GK 111
Cdd:COG0756   142 GR 143
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 32-81 5.95e-18

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: 72.14  E-value: 5.95e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958763444  32 PRSGLAvKHFIDVG-AGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLI 81
Cdd:cd07557    42 PRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPVVIKKGDRIAQLV 91
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 18-110 3.15e-49

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 153.80  E-value: 3.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  18 PAGPRALQATTCT-----------APRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIL 86
Cdd:PLN02547   50 PARGKALVPTDLSiaipegtyariAPRSGLAWKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIV 129

                          90       100
                  ....*....|....*....|....
gi 1958763444  87 YPDLEEVQTLDNTERGSGGFGSTG 110
Cdd:PLN02547  130 TPEVVEVEDLDATVRGAGGFGSTG 153
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 31-110 4.95e-49

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 153.60  E-value: 4.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  31 APRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGSTG 110
Cdd:PHA02703   71 APRSGLAVKHFIDVGAGVIDADYRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTG 150
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 31-111 4.33e-45

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: 142.76  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  31 APRSGLAVKHF--IDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILY-PDLEEVQTLDNTERGSGGFG 107
Cdd:TIGR00576  59 APRSGLALKHGvtIDNSPGVIDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFG 138


                  ....
gi 1958763444 108 STGK 111
Cdd:TIGR00576 139 STGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 31-110 3.09e-40

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 129.72  E-value: 3.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  31 APRSGLAVKHFIDVGaGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGSTG 110
Cdd:pfam00692  51 FPRSGLAAKGLIVVP-GVIDSDYRGEVKVVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 32-111 3.23e-39

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: 127.83  E-value: 3.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  32 PRSGLAVKHFIDVG--AGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGST 109
Cdd:COG0756    62 PRSGLALKHGITLLnsPGTIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGST 141


                  ..
gi 1958763444 110 GK 111
Cdd:COG0756   142 GR 143
PHA03094 PHA03094
dUTPase; Provisional
 31-112 2.48e-38

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 125.65  E-value: 2.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  31 APRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGSTG 110
Cdd:PHA03094   63 APRSGLSLNYGIDIGGGVIDEDYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142


                  ..
gi 1958763444 111 KN 112
Cdd:PHA03094  143 LR 144
dut PRK00601
dUTP diphosphatase;
32-112 4.67e-35

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 117.57  E-value: 4.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  32 PRSGLAVKHFIDVG--AGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVQTLDNTERGSGGFGST 109
Cdd:PRK00601   68 PRSGLAHKHGIVLGnlPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGST 147


                  ...
gi 1958763444 110 GKN 112
Cdd:PRK00601  148 GRH 150
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 32-81 5.95e-18

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: 72.14  E-value: 5.95e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958763444  32 PRSGLAvKHFIDVG-AGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLI 81
Cdd:cd07557    42 PRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPVVIKKGDRIAQLV 91
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 47-112 4.53e-15

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 66.30  E-value: 4.53e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958763444  47 GVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLIC---ERILYpdlEEVQTLDNTERGSGGFGSTGKN 112
Cdd:PTZ00143   90 GLIDAGYRGELIAAVDNIKDEPYTIKKGDRLVQLVSfdgEPITF---ELVDELDETTRGEGGFGSTGRL 155
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 33-88 5.44e-05

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: 39.99  E-value: 5.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958763444  33 RSGLAVKH-FIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERILYP 88
Cdd:TIGR02274 100 RSSLARLGlFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFERLSSP 156
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 33-81 9.87e-05

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 39.42  E-value: 9.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958763444  33 RSGLavkhFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLI 81
Cdd:COG0717   104 RLGL----FVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQLV 148
dut PRK13956
dUTP diphosphatase;
47-111 5.05e-04

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 37.08  E-value: 5.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958763444  47 GVIDEDYRGNVG------VVLFNFGKEKFEVKKGDRIAQLICERILYPDLEEVqtldnTERGSGGFGSTGK 111
Cdd:PRK13956   82 GVIDGDYYGNPAneghifAQMKNITDQEVVLEVGERIVQGVFMPFLIADGDQA-----DGERTGGFGSTGK 147
PHA03124 PHA03124
dUTPase; Provisional
 33-111 2.67e-03

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 35.69  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763444  33 RSGLAVKHFIDVGAGVIDEDYrgnVGVVLFNFGKEKFEVKKGDRIAQLICE---------------RILYPDLEEVQTLd 97
Cdd:PHA03124  330 RSSMNLKGLLVDPEHVQDDDW---ISFNITNIRDAAAFFHAGDRIAQLIALedkleflgepdalpwKIVNSVQDEKKNL- 405

                          90
                  ....*....|....
gi 1958763444  98 nTERGSGGFGSTGK 111
Cdd:PHA03124  406 -SSRGDGGFGSSGK 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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