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Conserved domains on  [gi|254675452|gb|ACT76710|]
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deoxyuridine 5'-triphosphate nucleotidohydrolase, partial [Fusobacterium nucleatum]

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 ...
 1-91 7.40e-55

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 PRK00601:

Pssm-ID: 444938 [Multi-domain]  Cd Length: 150  Bit Score: 166.49  E-value: 7.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   1 MKKIQVKVIRE---KGVELPKYETEGSAGMDVRANIKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITM 77
Cdd:PRK00601   1 MKKIDVKILDPrlgKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80

                         90
                 ....*....|....
gi 254675452  78 LNTPGTVDSDYRGE 91
Cdd:PRK00601  81 GNLPGTIDSDYRGE 94
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-91 7.40e-55

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 166.49  E-value: 7.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   1 MKKIQVKVIRE---KGVELPKYETEGSAGMDVRANIKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITM 77
Cdd:PRK00601   1 MKKIDVKILDPrlgKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80

                         90
                 ....*....|....
gi 254675452  78 LNTPGTVDSDYRGE 91
Cdd:PRK00601  81 GNLPGTIDSDYRGE 94
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 3-91 7.82e-53

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: 161.34  E-value: 7.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   3 KIQVKVIREkGVELPKYETEGSAGMDVRANIKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMLNTPG 82
Cdd:COG0756    1 KVKIKRLDE-DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPG 79


                 ....*....
gi 254675452  83 TVDSDYRGE 91
Cdd:COG0756   80 TIDSDYRGE 88
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 3-91 2.83e-35

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: 116.95  E-value: 2.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452    3 KIQVKVIREKGVeLPKYETEGSAGMDVRANikEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMLNTPG 82
Cdd:TIGR00576   1 KLKFVKLSPNAP-LPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPG 77


                  ....*....
gi 254675452   83 TVDSDYRGE 91
Cdd:TIGR00576  78 VIDADYRGE 86
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 25-91 7.01e-21

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: 78.69  E-value: 7.01e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675452 25 AGMDVRA-NIKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAiKHGITMLNtPGTVDSDYRGE 91
Cdd:cd07557   1 AGYDLRLgEDFEGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGE 66
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 15-91 8.38e-16

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 66.93  E-value: 8.38e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675452   15 ELPKYETEGSAGMDVRAniKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITmlnTPGTVDSDYRGE 91
Cdd:pfam00692   4 EIPTPGSPGDAGYDLYA--PYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIV---VPGVIDSDYRGE 75
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-91 7.40e-55

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 166.49  E-value: 7.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   1 MKKIQVKVIRE---KGVELPKYETEGSAGMDVRANIKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITM 77
Cdd:PRK00601   1 MKKIDVKILDPrlgKEFPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80

                         90
                 ....*....|....
gi 254675452  78 LNTPGTVDSDYRGE 91
Cdd:PRK00601  81 GNLPGTIDSDYRGE 94
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 3-91 7.82e-53

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: 161.34  E-value: 7.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   3 KIQVKVIREkGVELPKYETEGSAGMDVRANIKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMLNTPG 82
Cdd:COG0756    1 KVKIKRLDE-DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPG 79


                 ....*....
gi 254675452  83 TVDSDYRGE 91
Cdd:COG0756   80 TIDSDYRGE 88
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 3-91 2.83e-35

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: 116.95  E-value: 2.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452    3 KIQVKVIREKGVeLPKYETEGSAGMDVRANikEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMLNTPG 82
Cdd:TIGR00576   1 KLKFVKLSPNAP-LPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPG 77


                  ....*....
gi 254675452   83 TVDSDYRGE 91
Cdd:TIGR00576  78 VIDADYRGE 86
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 25-91 7.01e-21

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: 78.69  E-value: 7.01e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675452 25 AGMDVRA-NIKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAiKHGITMLNtPGTVDSDYRGE 91
Cdd:cd07557   1 AGYDLRLgEDFEGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGE 66
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 15-91 8.38e-16

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 66.93  E-value: 8.38e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675452   15 ELPKYETEGSAGMDVRAniKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITmlnTPGTVDSDYRGE 91
Cdd:pfam00692   4 EIPTPGSPGDAGYDLYA--PYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIV---VPGVIDSDYRGE 75
PLN02547 PLN02547
dUTP pyrophosphatase
 3-91 7.33e-15

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 65.20  E-value: 7.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   3 KIQVKVIREKGVeLPKYETEGSAGMDVRAniKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMlnTPG 82
Cdd:PLN02547  16 LLRVKKLSEKAT-LPSRGSALAAGYDLSS--AYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDV--GAG 90


                 ....*....
gi 254675452  83 TVDSDYRGE 91
Cdd:PLN02547  91 VIDADYRGP 99
PHA03094 PHA03094
dUTPase; Provisional
 1-91 1.92e-11

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 55.93  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   1 MKKIQVKVIREKG-VELPKYETEGSAGMDVRANIKepITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMln 79
Cdd:PHA03094   1 MSNSPVRCVKLSNfAKIPTRSSPKSAGYDLYSAYD--YTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDI-- 76

                         90
                 ....*....|..
gi 254675452  80 TPGTVDSDYRGE 91
Cdd:PHA03094  77 GGGVIDEDYRGN 88
dut PRK13956
dUTP diphosphatase;
16-90 1.50e-08

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 48.64  E-value: 1.50e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675452  16 LPKYETEGSAGMDVRAniKEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMLNTPGTVDSDYRG 90
Cdd:PRK13956  18 LPKRETAHAAGYDLKV--AERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYYG 90
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 6-90 1.28e-07

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 46.52  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675452   6 VKVIR-EKGVELPKYETEGSAGMDVRANIKepITLKSLERILVPTGLKVAIPEGYEIQVRPRSGLAIKHGITMlnTPGTV 84
Cdd:PHA02703  14 LRVVRlSPNATIPTRGSPGAAGLDLCSACD--CIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDV--GAGVI 89


                 ....*.
gi 254675452  85 DSDYRG 90
Cdd:PHA02703  90 DADYRG 95
PHA03127 PHA03127
dUTPase; Provisional
 34-91 1.04e-04

dUTPase; Provisional


Pssm-ID: 222993 [Multi-domain]  Cd Length: 322  Bit Score: 38.82  E-value: 1.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254675452  34 KEPITLKSLERILVPTGLKVAIPEGYEIQVRPRSGlAIKHGITMLNTPGTVDSDYRGE 91
Cdd:PHA03127  53 REAPNGDILYSRLVNLGLRAAAPGGYAILMSQMCS-GQTPSRPPAVAVGIVDSGYRGI 109
 
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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