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Conserved domains on  [gi|495621839|ref|WP_008346418|]
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MULTISPECIES: peptide-methionine (R)-S-oxide reductase MsrB [Bacillus]

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, ...
 5-129 1.53e-88

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


:

Pssm-ID: 439999  Cd Length: 133  Bit Score: 253.46  E-value: 1.53e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839   5 KEQRIKELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSH 84
Cdd:COG0229    9 DAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSH 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495621839  85 GMVRTEVRSKTADSHLGHVFPDGPGPKGLRYCINSAALKFIPKDD 129
Cdd:COG0229   89 GMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 5-129 1.53e-88

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 253.46  E-value: 1.53e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839   5 KEQRIKELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSH 84
Cdd:COG0229    9 DAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSH 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495621839  85 GMVRTEVRSKTADSHLGHVFPDGPGPKGLRYCINSAALKFIPKDD 129
Cdd:COG0229   89 GMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 10-126 1.75e-83

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: 240.34  E-value: 1.75e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839   10 KELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSHGMVRT 89
Cdd:pfam01641   4 KRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGMVRT 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 495621839   90 EVRSKTADSHLGHVFPDGPGPKGLRYCINSAALKFIP 126
Cdd:pfam01641  84 EVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 5-135 3.98e-81

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: 235.05  E-value: 3.98e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839    5 KEQRIKELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSH 84
Cdd:TIGR00357   4 DEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDESH 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495621839   85 GMVRTEVRSKTADSHLGHVFPDGPGPKGLRYCINSAALKFIPKDDLEKEGY 135
Cdd:TIGR00357  84 GMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIPLEEMEEEGY 134
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 12-139 4.10e-64

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: 203.57  E-value: 4.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839  12 LNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSHGMVRTEV 91
Cdd:PRK14018 389 LTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDFSYNMRRTEV 468

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495621839  92 RSKTADSHLGHVFPDGPGPK-GLRYCINSAALKFIPKDDLEKEGYGHLK 139
Cdd:PRK14018 469 RSRAADSHLGHVFPDGPRDKgGLRYCINGASLKFIPLEQMDAAGYGALK 517
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 5-129 1.53e-88

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 253.46  E-value: 1.53e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839   5 KEQRIKELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSH 84
Cdd:COG0229    9 DAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSH 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495621839  85 GMVRTEVRSKTADSHLGHVFPDGPGPKGLRYCINSAALKFIPKDD 129
Cdd:COG0229   89 GMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 10-126 1.75e-83

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: 240.34  E-value: 1.75e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839   10 KELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSHGMVRT 89
Cdd:pfam01641   4 KRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGMVRT 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 495621839   90 EVRSKTADSHLGHVFPDGPGPKGLRYCINSAALKFIP 126
Cdd:pfam01641  84 EVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 5-135 3.98e-81

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: 235.05  E-value: 3.98e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839    5 KEQRIKELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSH 84
Cdd:TIGR00357   4 DEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDESH 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495621839   85 GMVRTEVRSKTADSHLGHVFPDGPGPKGLRYCINSAALKFIPKDDLEKEGY 135
Cdd:TIGR00357  84 GMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIPLEEMEEEGY 134
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 12-139 4.10e-64

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: 203.57  E-value: 4.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839  12 LNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSHGMVRTEV 91
Cdd:PRK14018 389 LTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDFSYNMRRTEV 468

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495621839  92 RSKTADSHLGHVFPDGPGPK-GLRYCINSAALKFIPKDDLEKEGYGHLK 139
Cdd:PRK14018 469 RSRAADSHLGHVFPDGPRDKgGLRYCINGASLKFIPLEQMDAAGYGALK 517
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 6-129 2.01e-54

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 172.39  E-value: 2.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839   6 EQRIKELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQEVEEKVDTSHg 85
Cdd:PRK05550   1 MDKMKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADGR- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495621839  86 mvRTEVRSKTADSHLGHVF-PDGPGPKGLRYCINSAALKFIPKDD 129
Cdd:PRK05550  80 --RTEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFVPAEE 122
PRK05508 PRK05508
methionine-R-sulfoxide reductase;
10-129 4.96e-31

methionine-R-sulfoxide reductase;


Pssm-ID: 180121  Cd Length: 119  Bit Score: 107.50  E-value: 4.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621839  10 KELNRMQYEVTQNNGTEPPFQNEFWDHKEEGIYVDIISGKPLFSSLDKFDAHCGWPSFTKPIEDQeVEEKVDtSHGMvRT 89
Cdd:PRK05508   2 NELTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSFDDEIKGA-VKRIPD-ADGR-RT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495621839  90 EVRSKTADSHLGHVFpDGPG--PKGLRYCINSAALKFIPKDD 129
Cdd:PRK05508  79 EIVCANCGGHLGHVF-EGEGftPKNTRHCVNSISLKFVPDKG 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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