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Conserved domains on  [gi|61602118|ref|YP_213995|]
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E4 ORF1 [simian adenovirus 1]

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 ...
 27-120 1.00e-08

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: 50.56  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61602118   27 YVLFSPEDFVIAPRGIVLLSLQLSLDIPAGYLGRFF---------------SVADMNVRGvllcaqeiqpstwwEVSVVL 91
Cdd:PLN02547  39 YDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAprsglawkhsidvgaGVIDADYRG--------------PVGVIL 104

                         90       100
                 ....*....|....*....|....*....
gi 61602118   92 FNHSDEFYRGSRGQPVACLLLERVIYPTV 120
Cdd:PLN02547 105 FNHSDVDFEVKVGDRIAQLILEKIVTPEV 133
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 27-120 1.00e-08

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 50.56  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61602118   27 YVLFSPEDFVIAPRGIVLLSLQLSLDIPAGYLGRFF---------------SVADMNVRGvllcaqeiqpstwwEVSVVL 91
Cdd:PLN02547  39 YDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAprsglawkhsidvgaGVIDADYRG--------------PVGVIL 104

                         90       100
                 ....*....|....*....|....*....
gi 61602118   92 FNHSDEFYRGSRGQPVACLLLERVIYPTV 120
Cdd:PLN02547 105 FNHSDVDFEVKVGDRIAQLILEKIVTPEV 133
 
Name Accession Description Interval E-value
PLN02547 PLN02547
dUTP pyrophosphatase
 27-120 1.00e-08

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 50.56  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61602118   27 YVLFSPEDFVIAPRGIVLLSLQLSLDIPAGYLGRFF---------------SVADMNVRGvllcaqeiqpstwwEVSVVL 91
Cdd:PLN02547  39 YDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAprsglawkhsidvgaGVIDADYRG--------------PVGVIL 104

                         90       100
                 ....*....|....*....|....*....
gi 61602118   92 FNHSDEFYRGSRGQPVACLLLERVIYPTV 120
Cdd:PLN02547 105 FNHSDVDFEVKVGDRIAQLILEKIVTPEV 133
 
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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