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Conserved domains on  [gi|1836287305|gb|QJI05929|]
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13.5 kDa protein [Human adenovirus E4]

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 ...
 15-118 1.40e-07

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: 47.10  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836287305  15 ALLPeQKGS----NYIFYAPANFVLYPHGVALLELRLSIVVPRGFIGRFF---SLTDANVPGVYASsqIIHAGHREGLSV 87
Cdd:PLN02547   26 ATLP-SRGSalaaGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAprsGLAWKHSIDVGAG--VIDADYRGPVGV 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1836287305  88 MLFNHNVSFYSGRAGDPVACLVLEKVIYPPV 118
Cdd:PLN02547  103 ILFNHSDVDFEVKVGDRIAQLILEKIVTPEV 133
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 15-118 1.40e-07

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 47.10  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836287305  15 ALLPeQKGS----NYIFYAPANFVLYPHGVALLELRLSIVVPRGFIGRFF---SLTDANVPGVYASsqIIHAGHREGLSV 87
Cdd:PLN02547   26 ATLP-SRGSalaaGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAprsGLAWKHSIDVGAG--VIDADYRGPVGV 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1836287305  88 MLFNHNVSFYSGRAGDPVACLVLEKVIYPPV 118
Cdd:PLN02547  103 ILFNHSDVDFEVKVGDRIAQLILEKIVTPEV 133
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 28-118 9.90e-07

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 44.59  E-value: 9.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836287305  28 YAPANFVLYPHGVALLELRLSIVVPRGFIGRFFSLTDANVPGVYASSQIIHAGHREGLSVMLFNHNVSFYSGRAGDPVAC 107
Cdd:pfam00692  19 YAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKVVLFNLGKSDFTIKKGDRIAQ 98

                          90
                  ....*....|.
gi 1836287305 108 LVLEKVIYPPV 118
Cdd:pfam00692  99 LIFEPILHPEL 109
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 33-110 3.94e-03

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: 34.01  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836287305  33 FVLYPHGVALLELRLSIVVPRGFIGRFF---SLT----DANVPGVyassqiIHAGHREGLSVMLFNHNVSFYSGRAGDPV 105
Cdd:cd07557    14 IVLPPGETVLVPTGEAIELPEGYVGLVFprsSLArkgiTVHNAGV------IDPGYRGEITLELYNLGPEPVVIKKGDRI 87


                  ....*
gi 1836287305 106 ACLVL 110
Cdd:cd07557    88 AQLVF 92
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 15-118 1.40e-07

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 47.10  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836287305  15 ALLPeQKGS----NYIFYAPANFVLYPHGVALLELRLSIVVPRGFIGRFF---SLTDANVPGVYASsqIIHAGHREGLSV 87
Cdd:PLN02547   26 ATLP-SRGSalaaGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAprsGLAWKHSIDVGAG--VIDADYRGPVGV 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1836287305  88 MLFNHNVSFYSGRAGDPVACLVLEKVIYPPV 118
Cdd:PLN02547  103 ILFNHSDVDFEVKVGDRIAQLILEKIVTPEV 133
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 28-118 9.90e-07

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 44.59  E-value: 9.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836287305  28 YAPANFVLYPHGVALLELRLSIVVPRGFIGRFFSLTDANVPGVYASSQIIHAGHREGLSVMLFNHNVSFYSGRAGDPVAC 107
Cdd:pfam00692  19 YAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKVVLFNLGKSDFTIKKGDRIAQ 98

                          90
                  ....*....|.
gi 1836287305 108 LVLEKVIYPPV 118
Cdd:pfam00692  99 LIFEPILHPEL 109
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 33-110 3.94e-03

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: 34.01  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836287305  33 FVLYPHGVALLELRLSIVVPRGFIGRFF---SLT----DANVPGVyassqiIHAGHREGLSVMLFNHNVSFYSGRAGDPV 105
Cdd:cd07557    14 IVLPPGETVLVPTGEAIELPEGYVGLVFprsSLArkgiTVHNAGV------IDPGYRGEITLELYNLGPEPVVIKKGDRI 87


                  ....*
gi 1836287305 106 ACLVL 110
Cdd:cd07557    88 AQLVF 92
 
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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