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Conserved domains on  [gi|300681235|sp|Q0DC89|]
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RecName: Full=Peptide methionine sulfoxide reductase B1, chloroplastic; Short=OsMSRB1; AltName: Full=Peptide-methionine (R)-S-oxide reductase; Flags: Precursor

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, ...
 83-212 1.50e-88

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


:

Pssm-ID: 439999  Cd Length: 133  Bit Score: 256.55  E-value: 1.50e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235  83 PNYSTSLTDEEWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPI-GDNV 161
Cdd:COG0229    1 MTYKVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIdPGAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300681235 162 KCKLDMSiIFMPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLKLKK 212
Cdd:COG0229   81 EEKEDRS-HGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIP 130
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 83-212 1.50e-88

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 256.55  E-value: 1.50e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235  83 PNYSTSLTDEEWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPI-GDNV 161
Cdd:COG0229    1 MTYKVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIdPGAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300681235 162 KCKLDMSiIFMPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLKLKK 212
Cdd:COG0229   81 EEKEDRS-HGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIP 130
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 93-212 2.51e-84

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: 245.34  E-value: 2.51e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235   93 EWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPI-GDNVKCKLDMSiIF 171
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIpGDAVKEKEDTS-HG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 300681235  172 MPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLKLKK 212
Cdd:pfam01641  80 MVRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 89-209 5.15e-69

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: 207.31  E-value: 5.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235   89 LTDEEWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPIG-DNVKCKLDM 167
Cdd:TIGR00357   2 PSDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISeEVVAYERDE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 300681235  168 SiIFMPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLK 209
Cdd:TIGR00357  82 S-HGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALK 122
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 95-211 9.75e-52

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 168.15  E-value: 9.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235  95 RKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPIGDNVKCKLDMSIIfmpR 174
Cdd:PRK05550   4 MKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADGR---R 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 300681235 175 TEVLCAVCDAHLGHVF-DDGPRPTGKRYCINSASLKLK 211
Cdd:PRK05550  81 TEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFV 118
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 83-212 1.50e-88

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 256.55  E-value: 1.50e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235  83 PNYSTSLTDEEWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPI-GDNV 161
Cdd:COG0229    1 MTYKVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIdPGAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300681235 162 KCKLDMSiIFMPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLKLKK 212
Cdd:COG0229   81 EEKEDRS-HGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIP 130
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 93-212 2.51e-84

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: 245.34  E-value: 2.51e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235   93 EWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPI-GDNVKCKLDMSiIF 171
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIpGDAVKEKEDTS-HG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 300681235  172 MPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLKLKK 212
Cdd:pfam01641  80 MVRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 89-209 5.15e-69

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: 207.31  E-value: 5.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235   89 LTDEEWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPIG-DNVKCKLDM 167
Cdd:TIGR00357   2 PSDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISeEVVAYERDE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 300681235  168 SiIFMPRTEVLCAVCDAHLGHVFDDGPRPTGKRYCINSASLK 209
Cdd:TIGR00357  82 S-HGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALK 122
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 95-211 9.75e-52

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 168.15  E-value: 9.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235  95 RKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPIGDNVKCKLDMSIIfmpR 174
Cdd:PRK05550   4 MKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADGR---R 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 300681235 175 TEVLCAVCDAHLGHVF-DDGPRPTGKRYCINSASLKLK 211
Cdd:PRK05550  81 TEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFV 118
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 90-209 7.77e-38

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: 137.31  E-value: 7.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235  90 TDEEWRKRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPIGDNVKCKLDMSI 169
Cdd:PRK14018 381 SDAELKRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDFS 460

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300681235 170 IFMPRTEVLCAVCDAHLGHVFDDGPRP-TGKRYCINSASLK 209
Cdd:PRK14018 461 YNMRRTEVRSRAADSHLGHVFPDGPRDkGGLRYCINGASLK 501
PRK05508 PRK05508
methionine-R-sulfoxide reductase;
96-213 6.53e-37

methionine-R-sulfoxide reductase;


Pssm-ID: 180121  Cd Length: 119  Bit Score: 125.21  E-value: 6.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300681235  96 KRLTKDQYYITRQKGTERAFTGEYWNTKTPGIYHCVCCDTPLFESSTKFDSGTGWPSYYQPIGDNVKCKLDMSIIfmpRT 175
Cdd:PRK05508   2 NELTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSFDDEIKGAVKRIPDADGR---RT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 300681235 176 EVLCAVCDAHLGHVFdDGPRPTGK--RYCINSASLKLKKT 213
Cdd:PRK05508  79 EIVCANCGGHLGHVF-EGEGFTPKntRHCVNSISLKFVPD 117
 
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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