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Conserved domains on  [gi|446464938|ref|WP_000542792|]
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phosphonate C-P lyase system protein PhnG [Escherichia coli]

Protein Classification

phosphonate C-P lyase system protein PhnG( domain architecture ID 10007620)

phosphonate C-P lyase system protein PhnG may be responsible for the uptake and breakdown of phosphonates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PhnG COG3624
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion ...
2-148 3.99e-70

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion transport and metabolism];


:

Pssm-ID: 442842  Cd Length: 150  Bit Score: 207.77  E-value: 3.99e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464938   2 HADTATRQHWMSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGY 81
Cdd:COG3624    4 SADTAARQRWMRVLARAPPAELEALWAALGALPEVEWLRAPETGLVMVRGRAGGTGAPFNLGEATVTRAAVRLADGTVGH 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446464938  82 SWVQGRDKRHAERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVRGD 148
Cdd:COG3624   84 AYVLGRDKRHAELAAVLDALLQTPAHRAALEAALLAPLAAARAARRAARAAEAAATKVDFFTMVRGE 150
 
Name Accession Description Interval E-value
PhnG COG3624
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion ...
2-148 3.99e-70

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion transport and metabolism];


Pssm-ID: 442842  Cd Length: 150  Bit Score: 207.77  E-value: 3.99e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464938   2 HADTATRQHWMSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGY 81
Cdd:COG3624    4 SADTAARQRWMRVLARAPPAELEALWAALGALPEVEWLRAPETGLVMVRGRAGGTGAPFNLGEATVTRAAVRLADGTVGH 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446464938  82 SWVQGRDKRHAERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVRGD 148
Cdd:COG3624   84 AYVLGRDKRHAELAAVLDALLQTPAHRAALEAALLAPLAAARAARRAARAAEAAATKVDFFTMVRGE 150
PhnG_redo TIGR03293
phosphonate C-P lyase system protein PhnG; PhnH is a component of the C-P lyase system ...
5-148 9.53e-63

phosphonate C-P lyase system protein PhnG; PhnH is a component of the C-P lyase system (GenProp0232) for the catabolism of phosphonate compounds. The specific function of this component is unknown. This model is based on pfam06754.2, and has been broadened to include sequences missed by that model which are clearly true positive hits based on genome context.


Pssm-ID: 274505  Cd Length: 144  Bit Score: 189.01  E-value: 9.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464938    5 TATRQHWMSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGYSWV 84
Cdd:TIGR03293   1 TMTRQRWLEILAHAPLEELEALANRVAPSPQYSVLRAPETGLVMLRGRDGGTGEPFNLGEITVTRAAVRLNDGTEGYAYV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446464938   85 QGRDKRHAERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVRGD 148
Cdd:TIGR03293  81 LGRDKRHAELLAVLDALLQAPLLHDELIADLIAPLAQRLAERRARRQAEAAATRVDFFTMVRGE 144
PhnG pfam06754
Phosphonate metabolism protein PhnG; This family consists of several bacterial phosphonate ...
12-146 2.23e-60

Phosphonate metabolism protein PhnG; This family consists of several bacterial phosphonate metabolism protein PhnG sequences. In Escherichia coli, the phn operon encodes proteins responsible for the uptake and breakdown of phosphonates. The exact function of PhnG is unknown, however it is thought likely that along with six other proteins PhnG makes up the the C-P (carbon-phosphorus) lyase.


Pssm-ID: 429102  Cd Length: 135  Bit Score: 182.71  E-value: 2.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464938   12 MSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGYSWVQGRDKRH 91
Cdd:pfam06754   1 MRVLARAPAAELAALAAALGPLPEVTYLRAPETGLVMVRGRDGGTGAPFNLGEMTVTRAAVRLADGTVGHAYVLGRDKRH 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446464938   92 AERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVR 146
Cdd:pfam06754  81 AELAALIDALLQDPLPGDELEEALIAPLEARLAARRAARAAEAAATRVDFFTMVR 135
 
Name Accession Description Interval E-value
PhnG COG3624
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion ...
2-148 3.99e-70

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion transport and metabolism];


Pssm-ID: 442842  Cd Length: 150  Bit Score: 207.77  E-value: 3.99e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464938   2 HADTATRQHWMSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGY 81
Cdd:COG3624    4 SADTAARQRWMRVLARAPPAELEALWAALGALPEVEWLRAPETGLVMVRGRAGGTGAPFNLGEATVTRAAVRLADGTVGH 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446464938  82 SWVQGRDKRHAERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVRGD 148
Cdd:COG3624   84 AYVLGRDKRHAELAAVLDALLQTPAHRAALEAALLAPLAAARAARRAARAAEAAATKVDFFTMVRGE 150
PhnG_redo TIGR03293
phosphonate C-P lyase system protein PhnG; PhnH is a component of the C-P lyase system ...
5-148 9.53e-63

phosphonate C-P lyase system protein PhnG; PhnH is a component of the C-P lyase system (GenProp0232) for the catabolism of phosphonate compounds. The specific function of this component is unknown. This model is based on pfam06754.2, and has been broadened to include sequences missed by that model which are clearly true positive hits based on genome context.


Pssm-ID: 274505  Cd Length: 144  Bit Score: 189.01  E-value: 9.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464938    5 TATRQHWMSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGYSWV 84
Cdd:TIGR03293   1 TMTRQRWLEILAHAPLEELEALANRVAPSPQYSVLRAPETGLVMLRGRDGGTGEPFNLGEITVTRAAVRLNDGTEGYAYV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446464938   85 QGRDKRHAERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVRGD 148
Cdd:TIGR03293  81 LGRDKRHAELLAVLDALLQAPLLHDELIADLIAPLAQRLAERRARRQAEAAATRVDFFTMVRGE 144
PhnG pfam06754
Phosphonate metabolism protein PhnG; This family consists of several bacterial phosphonate ...
12-146 2.23e-60

Phosphonate metabolism protein PhnG; This family consists of several bacterial phosphonate metabolism protein PhnG sequences. In Escherichia coli, the phn operon encodes proteins responsible for the uptake and breakdown of phosphonates. The exact function of PhnG is unknown, however it is thought likely that along with six other proteins PhnG makes up the the C-P (carbon-phosphorus) lyase.


Pssm-ID: 429102  Cd Length: 135  Bit Score: 182.71  E-value: 2.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464938   12 MSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGYSWVQGRDKRH 91
Cdd:pfam06754   1 MRVLARAPAAELAALAAALGPLPEVTYLRAPETGLVMVRGRDGGTGAPFNLGEMTVTRAAVRLADGTVGHAYVLGRDKRH 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446464938   92 AERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVR 146
Cdd:pfam06754  81 AELAALIDALLQDPLPGDELEEALIAPLEARLAARRAARAAEAAATRVDFFTMVR 135
 
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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