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Conserved domains on  [gi|21313208|ref|NP_083895|]
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methionine-R-sulfoxide reductase B2, mitochondrial precursor [Mus musculus]

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, ...
 39-174 5.09e-77

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


:

Pssm-ID: 439999  Cd Length: 133  Bit Score: 225.73  E-value: 5.09e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208  39 KRSLSEADWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYgskgsDES 118
Cdd:COG0229   4 KVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPI-----DPG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21313208 119 HtgILRRLDTSLGCPRMEVVCKQCEAHLGHVFPDGPKPTGQRFCINSVALKFKPSK 174
Cdd:COG0229  79 A--VEEKEDRSHGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKE 132
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 39-174 5.09e-77

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 225.73  E-value: 5.09e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208  39 KRSLSEADWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYgskgsDES 118
Cdd:COG0229   4 KVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPI-----DPG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21313208 119 HtgILRRLDTSLGCPRMEVVCKQCEAHLGHVFPDGPKPTGQRFCINSVALKFKPSK 174
Cdd:COG0229  79 A--VEEKEDRSHGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKE 132
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 46-172 1.30e-73

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: 216.84  E-value: 1.30e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208    46 DWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYgskgsDESHtgILRR 125
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPI-----PGDA--VKEK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 21313208   126 LDTSLGCPRMEVVCKQCEAHLGHVFPDGPKPTGQRFCINSVALKFKP 172
Cdd:pfam01641  74 EDTSHGMVRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 42-172 5.21e-59

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: 180.35  E-value: 5.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208    42 LSEADWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYgskgsdeSHTG 121
Cdd:TIGR00357   2 PSDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPI-------SEEV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21313208   122 ILRRLDTSLGCPRMEVVCKQCEAHLGHVFPDGPKPTGQRFCINSVALKFKP 172
Cdd:TIGR00357  75 VAYERDESHGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIP 125
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 49-172 2.56e-47

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 155.44  E-value: 2.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208   49 KKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFS-EAYGSkgsdeshtgiLRRLD 127
Cdd:PRK05550   5 KSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDdEIPGA----------VKRLP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 21313208  128 TSLGcPRMEVVCKQCEAHLGHVF-PDGPKPTGQRFCINSVALKFKP 172
Cdd:PRK05550  75 DADG-RRTEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFVP 119
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 39-174 5.09e-77

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 225.73  E-value: 5.09e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208  39 KRSLSEADWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYgskgsDES 118
Cdd:COG0229   4 KVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPI-----DPG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21313208 119 HtgILRRLDTSLGCPRMEVVCKQCEAHLGHVFPDGPKPTGQRFCINSVALKFKPSK 174
Cdd:COG0229  79 A--VEEKEDRSHGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKE 132
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 46-172 1.30e-73

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: 216.84  E-value: 1.30e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208    46 DWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYgskgsDESHtgILRR 125
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPI-----PGDA--VKEK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 21313208   126 LDTSLGCPRMEVVCKQCEAHLGHVFPDGPKPTGQRFCINSVALKFKP 172
Cdd:pfam01641  74 EDTSHGMVRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 42-172 5.21e-59

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: 180.35  E-value: 5.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208    42 LSEADWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYgskgsdeSHTG 121
Cdd:TIGR00357   2 PSDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPI-------SEEV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21313208   122 ILRRLDTSLGCPRMEVVCKQCEAHLGHVFPDGPKPTGQRFCINSVALKFKP 172
Cdd:TIGR00357  75 VAYERDESHGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIP 125
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 49-172 2.56e-47

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 155.44  E-value: 2.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208   49 KKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFS-EAYGSkgsdeshtgiLRRLD 127
Cdd:PRK05550   5 KSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDdEIPGA----------VKRLP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 21313208  128 TSLGcPRMEVVCKQCEAHLGHVF-PDGPKPTGQRFCINSVALKFKP 172
Cdd:PRK05550  75 DADG-RRTEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFVP 119
PRK05508 PRK05508
methionine-R-sulfoxide reductase;
49-174 6.21e-37

methionine-R-sulfoxide reductase;


Pssm-ID: 180121  Cd Length: 119  Bit Score: 123.67  E-value: 6.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208   49 KKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFseaygskgsDESHTGILRRLDT 128
Cdd:PRK05508   2 NELTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSF---------DDEIKGAVKRIPD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 21313208  129 SLGcPRMEVVCKQCEAHLGHVFP-DGPKPTGQRFCINSVALKFKPSK 174
Cdd:PRK05508  73 ADG-RRTEIVCANCGGHLGHVFEgEGFTPKNTRHCVNSISLKFVPDK 118
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 43-172 9.92e-31

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: 116.13  E-value: 9.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313208   43 SEADWQKKLTPEQFYVTREKGTEAPFSGMYLNNKETGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAYGSKGSDEsHTgi 122
Cdd:PRK14018 381 SDAELKRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTE-HD-- 457

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21313208  123 lrrlDTSLGCPRMEVVCKQCEAHLGHVFPDGPKP-TGQRFCINSVALKFKP 172
Cdd:PRK14018 458 ----DFSYNMRRTEVRSRAADSHLGHVFPDGPRDkGGLRYCINGASLKFIP 504
 
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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