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Conserved domains on  [gi|489189315|ref|WP_003098697|]
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MULTISPECIES: phosphonate C-P lyase system protein PhnG [Pseudomonas]

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 ...
6-151 4.38e-66

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


:

Pssm-ID: 442842  Cd Length: 150  Bit Score: 197.76  E-value: 4.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189315   6 SDPTIAARQRWMGVLARARREELDAHADAL-RDADYHLLRAAETGMTLVRGRMGGTGSPFNLGEMTVTRCVVRLGDGRTG 84
Cdd:COG3624    3 ESADTAARQRWMRVLARAPPAELEALWAALgALPEVEWLRAPETGLVMVRGRAGGTGAPFNLGEATVTRAAVRLADGTVG 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489189315  85 YSYVAGRDKRHAELAALADAHLQGADA-AAWQARLIEPLARTQAERRAAQEAEIATTKVEFFTLVRGE 151
Cdd:COG3624   83 HAYVLGRDKRHAELAAVLDALLQTPAHrAALEAALLAPLAAARAARRAARAAEAAATKVDFFTMVRGE 150
 
Name Accession Description Interval E-value
PhnG COG3624
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion ...
6-151 4.38e-66

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


Pssm-ID: 442842  Cd Length: 150  Bit Score: 197.76  E-value: 4.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189315   6 SDPTIAARQRWMGVLARARREELDAHADAL-RDADYHLLRAAETGMTLVRGRMGGTGSPFNLGEMTVTRCVVRLGDGRTG 84
Cdd:COG3624    3 ESADTAARQRWMRVLARAPPAELEALWAALgALPEVEWLRAPETGLVMVRGRAGGTGAPFNLGEATVTRAAVRLADGTVG 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489189315  85 YSYVAGRDKRHAELAALADAHLQGADA-AAWQARLIEPLARTQAERRAAQEAEIATTKVEFFTLVRGE 151
Cdd:COG3624   83 HAYVLGRDKRHAELAAVLDALLQTPAHrAALEAALLAPLAAARAARRAARAAEAAATKVDFFTMVRGE 150
PhnG pfam06754
Phosphonate metabolism protein PhnG; This family consists of several bacterial phosphonate ...
17-149 4.30e-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: 181.94  E-value: 4.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189315   17 MGVLARARREELDAHADALRDA-DYHLLRAAETGMTLVRGRMGGTGSPFNLGEMTVTRCVVRLGDGRTGYSYVAGRDKRH 95
Cdd:pfam06754   1 MRVLARAPAAELAALAAALGPLpEVTYLRAPETGLVMVRGRDGGTGAPFNLGEMTVTRAAVRLADGTVGHAYVLGRDKRH 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489189315   96 AELAALADAHLQGAD-AAAWQARLIEPLARTQAERRAAQEAEIATTKVEFFTLVR 149
Cdd:pfam06754  81 AELAALIDALLQDPLpGDELEEALIAPLEARLAARRAARAAEAAATRVDFFTMVR 135
PhnG_redo TIGR03293
phosphonate C-P lyase system protein PhnG; PhnH is a component of the C-P lyase system ...
11-151 8.09e-57

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: 173.99  E-value: 8.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189315   11 AARQRWMGVLARARREELDAHADALRDA-DYHLLRAAETGMTLVRGRMGGTGSPFNLGEMTVTRCVVRLGDGRTGYSYVA 89
Cdd:TIGR03293   2 MTRQRWLEILAHAPLEELEALANRVAPSpQYSVLRAPETGLVMLRGRDGGTGEPFNLGEITVTRAAVRLNDGTEGYAYVL 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489189315   90 GRDKRHAELAALADAHLQGADA-AAWQARLIEPLARTQAERRAAQEAEIATTKVEFFTLVRGE 151
Cdd:TIGR03293  82 GRDKRHAELLAVLDALLQAPLLhDELIADLIAPLAQRLAERRARRQAEAAATRVDFFTMVRGE 144
 
Name Accession Description Interval E-value
PhnG COG3624
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG [Inorganic ion ...
6-151 4.38e-66

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


Pssm-ID: 442842  Cd Length: 150  Bit Score: 197.76  E-value: 4.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189315   6 SDPTIAARQRWMGVLARARREELDAHADAL-RDADYHLLRAAETGMTLVRGRMGGTGSPFNLGEMTVTRCVVRLGDGRTG 84
Cdd:COG3624    3 ESADTAARQRWMRVLARAPPAELEALWAALgALPEVEWLRAPETGLVMVRGRAGGTGAPFNLGEATVTRAAVRLADGTVG 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489189315  85 YSYVAGRDKRHAELAALADAHLQGADA-AAWQARLIEPLARTQAERRAAQEAEIATTKVEFFTLVRGE 151
Cdd:COG3624   83 HAYVLGRDKRHAELAAVLDALLQTPAHrAALEAALLAPLAAARAARRAARAAEAAATKVDFFTMVRGE 150
PhnG pfam06754
Phosphonate metabolism protein PhnG; This family consists of several bacterial phosphonate ...
17-149 4.30e-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: 181.94  E-value: 4.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189315   17 MGVLARARREELDAHADALRDA-DYHLLRAAETGMTLVRGRMGGTGSPFNLGEMTVTRCVVRLGDGRTGYSYVAGRDKRH 95
Cdd:pfam06754   1 MRVLARAPAAELAALAAALGPLpEVTYLRAPETGLVMVRGRDGGTGAPFNLGEMTVTRAAVRLADGTVGHAYVLGRDKRH 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489189315   96 AELAALADAHLQGAD-AAAWQARLIEPLARTQAERRAAQEAEIATTKVEFFTLVR 149
Cdd:pfam06754  81 AELAALIDALLQDPLpGDELEEALIAPLEARLAARRAARAAEAAATRVDFFTMVR 135
PhnG_redo TIGR03293
phosphonate C-P lyase system protein PhnG; PhnH is a component of the C-P lyase system ...
11-151 8.09e-57

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: 173.99  E-value: 8.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489189315   11 AARQRWMGVLARARREELDAHADALRDA-DYHLLRAAETGMTLVRGRMGGTGSPFNLGEMTVTRCVVRLGDGRTGYSYVA 89
Cdd:TIGR03293   2 MTRQRWLEILAHAPLEELEALANRVAPSpQYSVLRAPETGLVMLRGRDGGTGEPFNLGEITVTRAAVRLNDGTEGYAYVL 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489189315   90 GRDKRHAELAALADAHLQGADA-AAWQARLIEPLARTQAERRAAQEAEIATTKVEFFTLVRGE 151
Cdd:TIGR03293  82 GRDKRHAELLAVLDALLQAPLLhDELIADLIAPLAQRLAERRARRQAEAAATRVDFFTMVRGE 144
 
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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