Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370512392  62 PEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCS 110
Cdd:COG0225     1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCS 49

Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370512392  62 PEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCS 110
Cdd:COG0225     1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCS 49

methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase (MsrA), a repair enzyme for proteins that have been inactivated by oxidation. The enzyme from E. coli is coextensive with this model and has enzymatic activity. However, in all completed genomes in which this module is present, a second protein module, described in TIGR00357, is also found, and in several cases as part of the same polypeptide chain: N-terminal to this module in Helicobacter pylori and Haemophilus influenzae (as in PilB of Neisseria gonorrhoeae) but C-terminal to it in Treponema pallidum. PilB, containing both domains, has been shown to be important for the expression of adhesins in certain pathogens. [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370512392  66 QMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCS 110
Cdd:TIGR00401   1 EIATFAGGCFWGTEKYFRLIPGVVSTAVGYTNGYTPNPTYEEVCS 45

Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370512392  62 PEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCS 110
Cdd:COG0225     1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCS 49

methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase (MsrA), a repair enzyme for proteins that have been inactivated by oxidation. The enzyme from E. coli is coextensive with this model and has enzymatic activity. However, in all completed genomes in which this module is present, a second protein module, described in TIGR00357, is also found, and in several cases as part of the same polypeptide chain: N-terminal to this module in Helicobacter pylori and Haemophilus influenzae (as in PilB of Neisseria gonorrhoeae) but C-terminal to it in Treponema pallidum. PilB, containing both domains, has been shown to be important for the expression of adhesins in certain pathogens. [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370512392  66 QMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCS 110
Cdd:TIGR00401   1 EIATFAGGCFWGTEKYFRLIPGVVSTAVGYTNGYTPNPTYEEVCS 45

bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB;

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1370512392  73 GCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVC 109
Cdd:PRK14018  206 GCFWGLEAYFQRIDGVVDAVSGYANGNTKNPSYEDVY 242