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Conserved domains on  [gi|446836061|ref|WP_000913317|]
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MULTISPECIES: peptide-methionine (R)-S-oxide reductase MsrB [Staphylococcus]

Protein Classification

peptide-methionine (R)-S-oxide reductase( domain architecture ID 10000743)

peptide-methionine (R)-S-oxide reductase catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins

CATH:  2.170.150.20
EC:  1.8.4.12
Gene Symbol:  msrB
Gene Ontology:  GO:0033743|GO:0008270
PubMed:  32943184|36084791
SCOP:  4002166

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 6-127 6.35e-74

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


:

Pssm-ID: 439999  Cd Length: 133  Bit Score: 216.49  E-value: 6.35e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061   6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:COG0229   13 RARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSHGMVR 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446836061  86 TEVRSEESNSHLGHVFNDGPKESgGLRYCINSAAIQFIPYEK 127
Cdd:COG0229   93 TEVRCARCGAHLGHVFDDGPPPT-GLRYCINSAALRFIPKEE 133
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 6-127 6.35e-74

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 216.49  E-value: 6.35e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061   6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:COG0229   13 RARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSHGMVR 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446836061  86 TEVRSEESNSHLGHVFNDGPKESgGLRYCINSAAIQFIPYEK 127
Cdd:COG0229   93 TEVRCARCGAHLGHVFDDGPPPT-GLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 6-124 1.03e-71

SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.


Pssm-ID: 460278  Cd Length: 120  Bit Score: 210.29  E-value: 1.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061    6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:pfam01641   3 RKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGMVR 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446836061   86 TEVRSEESNSHLGHVFNDGPKESgGLRYCINSAAIQFIP 124
Cdd:pfam01641  83 TEVRCARCGGHLGHVFDDGPPPT-GLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 6-133 1.24e-66

methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein important for pilin expression, N-terminal to a domain coextensive to with the known peptide methionine sulfoxide reductase (MsrA), a protein repair enzyme, of E. coli. Among the early completed genomes, this module is found if and only if MsrA is also found, whether N-terminal to MsrA (as for Helicobacter pylori), C-terminal (as for Treponema pallidum), or in a separate polypeptide. Although the function of this region is not clear, an auxiliary function to MsrA is suggested. [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 129454  Cd Length: 134  Bit Score: 198.07  E-value: 1.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061    6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:TIGR00357   8 KKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDESHGMIR 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446836061   86 TEVRSEESNSHLGHVFNDGPkESGGLRYCINSAAIQFIPYEKLEELGY 133
Cdd:TIGR00357  88 TEVRCRNCDAHLGHVFDDGP-EPTGLRYCINSAALKFIPLEEMEEEGY 134
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 6-138 1.74e-58

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


Pssm-ID: 184456 [Multi-domain]  Cd Length: 521  Bit Score: 188.93  E-value: 1.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061   6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:PRK14018 386 KRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDFSYNMRR 465

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446836061  86 TEVRSEESNSHLGHVFNDGPKESGGLRYCINSAAIQFIPYEKLEELGYGDLIS 138
Cdd:PRK14018 466 TEVRSRAADSHLGHVFPDGPRDKGGLRYCINGASLKFIPLEQMDAAGYGALKK 518
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 6-127 6.35e-74

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 216.49  E-value: 6.35e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061   6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:COG0229   13 RARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSHGMVR 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446836061  86 TEVRSEESNSHLGHVFNDGPKESgGLRYCINSAAIQFIPYEK 127
Cdd:COG0229   93 TEVRCARCGAHLGHVFDDGPPPT-GLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 6-124 1.03e-71

SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.


Pssm-ID: 460278  Cd Length: 120  Bit Score: 210.29  E-value: 1.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061    6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:pfam01641   3 RKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGMVR 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446836061   86 TEVRSEESNSHLGHVFNDGPKESgGLRYCINSAAIQFIP 124
Cdd:pfam01641  83 TEVRCARCGGHLGHVFDDGPPPT-GLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 6-133 1.24e-66

methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein important for pilin expression, N-terminal to a domain coextensive to with the known peptide methionine sulfoxide reductase (MsrA), a protein repair enzyme, of E. coli. Among the early completed genomes, this module is found if and only if MsrA is also found, whether N-terminal to MsrA (as for Helicobacter pylori), C-terminal (as for Treponema pallidum), or in a separate polypeptide. Although the function of this region is not clear, an auxiliary function to MsrA is suggested. [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 129454  Cd Length: 134  Bit Score: 198.07  E-value: 1.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061    6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:TIGR00357   8 KKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDESHGMIR 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446836061   86 TEVRSEESNSHLGHVFNDGPkESGGLRYCINSAAIQFIPYEKLEELGY 133
Cdd:TIGR00357  88 TEVRCRNCDAHLGHVFDDGP-EPTGLRYCINSAALKFIPLEEMEEEGY 134
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 6-138 1.74e-58

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


Pssm-ID: 184456 [Multi-domain]  Cd Length: 521  Bit Score: 188.93  E-value: 1.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061   6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFSKALDDDEIIELVDKSFGMVR 85
Cdd:PRK14018 386 KRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDFSYNMRR 465

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446836061  86 TEVRSEESNSHLGHVFNDGPKESGGLRYCINSAAIQFIPYEKLEELGYGDLIS 138
Cdd:PRK14018 466 TEVRSRAADSHLGHVFPDGPRDKGGLRYCINGASLKFIPLEQMDAAGYGALKK 518
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 6-127 4.08e-49

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 158.52  E-value: 4.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061   6 KSELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFskaldDDEI----IELVDKSf 81
Cdd:PRK05550   4 MKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSF-----DDEIpgavKRLPDAD- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446836061  82 GMvRTEVRSEESNSHLGHVFNDGPKESGGLRYCINSAAIQFIPYEK 127
Cdd:PRK05550  78 GR-RTEIVCANCGAHLGHVFEGEGLTPKNTRHCVNSASLDFVPAEE 122
PRK05508 PRK05508
methionine-R-sulfoxide reductase;
8-127 8.71e-31

methionine-R-sulfoxide reductase;


Pssm-ID: 180121  Cd Length: 119  Bit Score: 106.72  E-value: 8.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446836061   8 ELTDIEYIVTQENGTEPPFMNEYWNHFAKGIYVDKISGKPLFTSEEKFHSECGWPSFskaldDDEI---IELVDKSFGMv 84
Cdd:PRK05508   3 ELTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSF-----DDEIkgaVKRIPDADGR- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446836061  85 RTEVRSEESNSHLGHVFNDGPKESGGLRYCINSAAIQFIPYEK 127
Cdd:PRK05508  77 RTEIVCANCGGHLGHVFEGEGFTPKNTRHCVNSISLKFVPDKG 119
 
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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