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Conserved domains on  [gi|90265363|emb|CAJ77045|]
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Rifampin ADP-ribosylating transferase [Acinetobacter baumannii]

Protein Classification

NAD(+)--rifampin ADP-ribosyltransferase( domain architecture ID 10572757)

NAD(+)--rifampin ADP-ribosyltransferase modifies and inactivates rifamycin antibiotics such as rifampin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arr-ms pfam12120
Rifampin ADP-ribosyl transferase; This protein is found in bacteria. Proteins in this family ...
 33-135 4.77e-61

Rifampin ADP-ribosyl transferase; This protein is found in bacteria. Proteins in this family are typically between 136 to 150 amino acids in length. The opportunistic pathogen Mycobacterium smegmatis is resistant to rifampin because of the presence of a chromosomally encoded rifampin ADP-ribosyltransferase (Arr-ms). Arr-ms is a small enzyme whose activity thus renders rifamycin antibiotics ineffective.


:

Pssm-ID: 432344  Cd Length: 99  Bit Score: 183.59  E-value: 4.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90265363    33 FYHGTKANLAIGDLLTTGFISHFEDGRILKHIYFSALMEPAVWGAELAMSlsglEGRGYIYIVEPTGPFEDDPNLTNKKF 112
Cdd:pfam12120   1 FYHGTKADLQVGDLLTPGRSSNYGPGRVMNHVYFTATLDAAIWGAELAAG----DGRGRIYIVEPTGPFEDDPNVTDKKF 76

                          90       100
                  ....*....|....*....|...
gi 90265363   113 PGNPTQSYRTCEPLRIVGVVEDW 135
Cdd:pfam12120  77 PGNPTRSYRSREPLRVVGEVTDW 99
 
Name Accession Description Interval E-value
Arr-ms pfam12120
Rifampin ADP-ribosyl transferase; This protein is found in bacteria. Proteins in this family ...
 33-135 4.77e-61

Rifampin ADP-ribosyl transferase; This protein is found in bacteria. Proteins in this family are typically between 136 to 150 amino acids in length. The opportunistic pathogen Mycobacterium smegmatis is resistant to rifampin because of the presence of a chromosomally encoded rifampin ADP-ribosyltransferase (Arr-ms). Arr-ms is a small enzyme whose activity thus renders rifamycin antibiotics ineffective.


Pssm-ID: 432344  Cd Length: 99  Bit Score: 183.59  E-value: 4.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90265363    33 FYHGTKANLAIGDLLTTGFISHFEDGRILKHIYFSALMEPAVWGAELAMSlsglEGRGYIYIVEPTGPFEDDPNLTNKKF 112
Cdd:pfam12120   1 FYHGTKADLQVGDLLTPGRSSNYGPGRVMNHVYFTATLDAAIWGAELAAG----DGRGRIYIVEPTGPFEDDPNVTDKKF 76

                          90       100
                  ....*....|....*....|...
gi 90265363   113 PGNPTQSYRTCEPLRIVGVVEDW 135
Cdd:pfam12120  77 PGNPTRSYRSREPLRVVGEVTDW 99
 
Name Accession Description Interval E-value
Arr-ms pfam12120
Rifampin ADP-ribosyl transferase; This protein is found in bacteria. Proteins in this family ...
 33-135 4.77e-61

Rifampin ADP-ribosyl transferase; This protein is found in bacteria. Proteins in this family are typically between 136 to 150 amino acids in length. The opportunistic pathogen Mycobacterium smegmatis is resistant to rifampin because of the presence of a chromosomally encoded rifampin ADP-ribosyltransferase (Arr-ms). Arr-ms is a small enzyme whose activity thus renders rifamycin antibiotics ineffective.


Pssm-ID: 432344  Cd Length: 99  Bit Score: 183.59  E-value: 4.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90265363    33 FYHGTKANLAIGDLLTTGFISHFEDGRILKHIYFSALMEPAVWGAELAMSlsglEGRGYIYIVEPTGPFEDDPNLTNKKF 112
Cdd:pfam12120   1 FYHGTKADLQVGDLLTPGRSSNYGPGRVMNHVYFTATLDAAIWGAELAAG----DGRGRIYIVEPTGPFEDDPNVTDKKF 76

                          90       100
                  ....*....|....*....|...
gi 90265363   113 PGNPTQSYRTCEPLRIVGVVEDW 135
Cdd:pfam12120  77 PGNPTRSYRSREPLRVVGEVTDW 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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