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Conserved domains on  [gi|1129982904|gb|APU03168|]
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hypothetical protein phiAp1_27 [Ralstonia phage phiAp1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dGTP_diPhyd_N pfam18909
dATP/dGTP diphosphohydrolase, N-terminal; This entry represent the N-terminal region of ...
 88-187 4.02e-27

dATP/dGTP diphosphohydrolase, N-terminal; This entry represent the N-terminal region of SHab15497_00040, an Acinetobacter phage protein that catalyzes the hydrolysis of dGTP into dGMP, which is needed among others for the first step of biosynthesis of dZTP (2-amino-2'-deoxyadenosine-5'- triphosphate).


:

Pssm-ID: 465905  Cd Length: 99  Bit Score: 99.68  E-value: 4.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129982904  88 ANPKQAFGDKKPPVHLVHGIALLAESQALHAGRRKYGENNFIQTPvEAMTYVAGMKRHIDQWVAGEEFDPVELVSHLGAV 167
Cdd:pfam18909   1 SGPGGKKDTGKPRYDLLPPRALLEVAEVLTFGAKKYGPHNWRKGP-PWVRYLAAALRHLLAYWAGEDYDPESGLPHLAHA 79

                          90       100
                  ....*....|....*....|
gi 1129982904 168 RAGAGILLTAAACGMMIDNR 187
Cdd:pfam18909  80 AWNALFLLEAELRGKEIDDR 99
 
Name Accession Description Interval E-value
dGTP_diPhyd_N pfam18909
dATP/dGTP diphosphohydrolase, N-terminal; This entry represent the N-terminal region of ...
 88-187 4.02e-27

dATP/dGTP diphosphohydrolase, N-terminal; This entry represent the N-terminal region of SHab15497_00040, an Acinetobacter phage protein that catalyzes the hydrolysis of dGTP into dGMP, which is needed among others for the first step of biosynthesis of dZTP (2-amino-2'-deoxyadenosine-5'- triphosphate).


Pssm-ID: 465905  Cd Length: 99  Bit Score: 99.68  E-value: 4.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129982904  88 ANPKQAFGDKKPPVHLVHGIALLAESQALHAGRRKYGENNFIQTPvEAMTYVAGMKRHIDQWVAGEEFDPVELVSHLGAV 167
Cdd:pfam18909   1 SGPGGKKDTGKPRYDLLPPRALLEVAEVLTFGAKKYGPHNWRKGP-PWVRYLAAALRHLLAYWAGEDYDPESGLPHLAHA 79

                          90       100
                  ....*....|....*....|
gi 1129982904 168 RAGAGILLTAAACGMMIDNR 187
Cdd:pfam18909  80 AWNALFLLEAELRGKEIDDR 99
 
Name Accession Description Interval E-value
dGTP_diPhyd_N pfam18909
dATP/dGTP diphosphohydrolase, N-terminal; This entry represent the N-terminal region of ...
 88-187 4.02e-27

dATP/dGTP diphosphohydrolase, N-terminal; This entry represent the N-terminal region of SHab15497_00040, an Acinetobacter phage protein that catalyzes the hydrolysis of dGTP into dGMP, which is needed among others for the first step of biosynthesis of dZTP (2-amino-2'-deoxyadenosine-5'- triphosphate).


Pssm-ID: 465905  Cd Length: 99  Bit Score: 99.68  E-value: 4.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129982904  88 ANPKQAFGDKKPPVHLVHGIALLAESQALHAGRRKYGENNFIQTPvEAMTYVAGMKRHIDQWVAGEEFDPVELVSHLGAV 167
Cdd:pfam18909   1 SGPGGKKDTGKPRYDLLPPRALLEVAEVLTFGAKKYGPHNWRKGP-PWVRYLAAALRHLLAYWAGEDYDPESGLPHLAHA 79

                          90       100
                  ....*....|....*....|
gi 1129982904 168 RAGAGILLTAAACGMMIDNR 187
Cdd:pfam18909  80 AWNALFLLEAELRGKEIDDR 99
 
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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