NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|190341012|ref|YP_001974474|]
View 

control protein E4orf1 [Human mastadenovirus D]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 36-119 7.46e-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: 45.17  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341012  36 IPPHGVVLLHLKVSVLVPTGYQGRF-----MALNDYhardILTQSDVIFAGRRQELTVLLFNHTDRFLYVRKGHPVGTLL 110
Cdd:PLN02547  49 VPARGKALVPTDLSIAIPEGTYARIaprsgLAWKHS----IDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLI 124


                 ....*....
gi 190341012 111 LERVIFPSV 119
Cdd:PLN02547 125 LEKIVTPEV 133
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 36-119 7.46e-07

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 45.17  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341012  36 IPPHGVVLLHLKVSVLVPTGYQGRF-----MALNDYhardILTQSDVIFAGRRQELTVLLFNHTDRFLYVRKGHPVGTLL 110
Cdd:PLN02547  49 VPARGKALVPTDLSIAIPEGTYARIaprsgLAWKHS----IDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLI 124


                 ....*....
gi 190341012 111 LERVIFPSV 119
Cdd:PLN02547 125 LEKIVTPEV 133
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 32-111 1.47e-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: 35.16  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341012  32 ESFHIPPHGVVLLHLKVSVLVPTGYQGRF-----MALNDYhardILTQSDVIFAGRRQELTVLLFNHTDRFLYVRKGHPV 106
Cdd:cd07557   12 EGIVLPPGETVLVPTGEAIELPEGYVGLVfprssLARKGI----TVHNAGVIDPGYRGEITLELYNLGPEPVVIKKGDRI 87


                 ....*
gi 190341012 107 GTLLL 111
Cdd:cd07557   88 AQLVF 92
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 36-119 7.46e-07

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 45.17  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341012  36 IPPHGVVLLHLKVSVLVPTGYQGRF-----MALNDYhardILTQSDVIFAGRRQELTVLLFNHTDRFLYVRKGHPVGTLL 110
Cdd:PLN02547  49 VPARGKALVPTDLSIAIPEGTYARIaprsgLAWKHS----IDVGAGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLI 124


                 ....*....
gi 190341012 111 LERVIFPSV 119
Cdd:PLN02547 125 LEKIVTPEV 133
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 32-111 1.47e-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: 35.16  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341012  32 ESFHIPPHGVVLLHLKVSVLVPTGYQGRF-----MALNDYhardILTQSDVIFAGRRQELTVLLFNHTDRFLYVRKGHPV 106
Cdd:cd07557   12 EGIVLPPGETVLVPTGEAIELPEGYVGLVfprssLARKGI----TVHNAGVIDPGYRGEITLELYNLGPEPVVIKKGDRI 87


                 ....*
gi 190341012 107 GTLLL 111
Cdd:cd07557   88 AQLVF 92
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 36-120 1.61e-03

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 36.50  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341012  36 IPPHGVVLLHLKVSVLVPTGYQGRFM---ALNDYHARDIltQSDVIFAGRRQELTVLLFNHTDRFLYVRKGHPVGTLLLE 112
Cdd:PHA02703  46 VPAGCRCVVFTDLLIKLPDGCYGRIAprsGLAVKHFIDV--GAGVIDADYRGNVGVVLFNFGHNDFEVKKGDRIAQLICE 123


                 ....*...
gi 190341012 113 RVIFPSVK 120
Cdd:PHA02703 124 RAAFPAVE 131
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH