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Conserved domains on  [gi|30695559|ref|NP_564640|]
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methionine sulfoxide reductase B 1 [Arabidopsis thaliana]

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, ...
 73-199 6.02e-86

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


:

Pssm-ID: 439999  Cd Length: 133  Bit Score: 249.61  E-value: 6.02e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559  73 LSENEWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPI-GNNVKTKLDL 151
Cdd:COG0229   7 KSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIdPGAVEEKEDR 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30695559 152 SiIFMPRQEVVCAVCNAHLGHVFDDGPRPTGKRYCLNSAALKLNALEK 199
Cdd:COG0229  87 S-HGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 73-199 6.02e-86

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 249.61  E-value: 6.02e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559  73 LSENEWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPI-GNNVKTKLDL 151
Cdd:COG0229   7 KSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIdPGAVEEKEDR 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30695559 152 SiIFMPRQEVVCAVCNAHLGHVFDDGPRPTGKRYCLNSAALKLNALEK 199
Cdd:COG0229  87 S-HGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 77-194 1.77e-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: 242.65  E-value: 1.77e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559    77 EWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPI-GNNVKTKLDLSiIF 155
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIpGDAVKEKEDTS-HG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 30695559   156 MPRQEVVCAVCNAHLGHVFDDGPRPTGKRYCLNSAALKL 194
Cdd:pfam01641  80 MVRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKF 118
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 73-199 1.17e-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: 200.77  E-value: 1.17e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559    73 LSENEWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPIG-NNVKTKLDL 151
Cdd:TIGR00357   2 PSDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISeEVVAYERDE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 30695559   152 SiIFMPRQEVVCAVCNAHLGHVFDDGPRPTGKRYCLNSAALKLNALEK 199
Cdd:TIGR00357  82 S-HGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIPLEE 128
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 79-200 7.61e-53

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 170.46  E-value: 7.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559   79 KKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPIGNNVKTKLDLSIIfmpR 158
Cdd:PRK05550   4 MKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADGR---R 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 30695559  159 QEVVCAVCNAHLGHVF-DDGPRPTGKRYCLNSAALKLNALEKT 200
Cdd:PRK05550  81 TEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFVPAEEG 123
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 73-199 6.02e-86

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 249.61  E-value: 6.02e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559  73 LSENEWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPI-GNNVKTKLDL 151
Cdd:COG0229   7 KSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIdPGAVEEKEDR 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30695559 152 SiIFMPRQEVVCAVCNAHLGHVFDDGPRPTGKRYCLNSAALKLNALEK 199
Cdd:COG0229  87 S-HGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 77-194 1.77e-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: 242.65  E-value: 1.77e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559    77 EWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPI-GNNVKTKLDLSiIF 155
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIpGDAVKEKEDTS-HG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 30695559   156 MPRQEVVCAVCNAHLGHVFDDGPRPTGKRYCLNSAALKL 194
Cdd:pfam01641  80 MVRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKF 118
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 73-199 1.17e-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: 200.77  E-value: 1.17e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559    73 LSENEWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPIG-NNVKTKLDL 151
Cdd:TIGR00357   2 PSDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISeEVVAYERDE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 30695559   152 SiIFMPRQEVVCAVCNAHLGHVFDDGPRPTGKRYCLNSAALKLNALEK 199
Cdd:TIGR00357  82 S-HGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIPLEE 128
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 79-200 7.61e-53

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 170.46  E-value: 7.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559   79 KKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPIGNNVKTKLDLSIIfmpR 158
Cdd:PRK05550   4 MKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADGR---R 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 30695559  159 QEVVCAVCNAHLGHVF-DDGPRPTGKRYCLNSAALKLNALEKT 200
Cdd:PRK05550  81 TEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFVPAEEG 123
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 58-199 1.76e-36

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: 133.08  E-value: 1.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559   58 KPDNVQEA-EKNEFASLSENEWKKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPS 136
Cdd:PRK14018 364 KTAPQGKGfDAATYKKPSDAELKRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPS 443

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695559  137 YYQPIGNNVKTKLDLSIIFMPRQEVVCAVCNAHLGHVFDDGPRP-TGKRYCLNSAALKLNALEK 199
Cdd:PRK14018 444 FTRPIDAKVVTEHDDFSYNMRRTEVRSRAADSHLGHVFPDGPRDkGGLRYCINGASLKFIPLEQ 507
PRK05508 PRK05508
methionine-R-sulfoxide reductase;
79-194 1.08e-35

methionine-R-sulfoxide reductase;


Pssm-ID: 180121  Cd Length: 119  Bit Score: 121.75  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559   79 KKRLTPEQYYITRQKGTERAFTGEYWNSKTPGVYNCVCCDTPLFDSSTKFDSGTGWPSYYQPIGNNVKTKLDLSIIfmpR 158
Cdd:PRK05508   1 YNELTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSFDDEIKGAVKRIPDADGR---R 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30695559  159 QEVVCAVCNAHLGHVFdDGPRPTGK--RYCLNSAALKL 194
Cdd:PRK05508  78 TEIVCANCGGHLGHVF-EGEGFTPKntRHCVNSISLKF 114
Yippee-Mis18 pfam03226
Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both ...
 111-192 7.45e-04

Yippee zinc-binding/DNA-binding /Mis18, centromere assembly; This family includes both Yippee-type proteins and Mis18 kinetochore proteins. Yippee are putative zinc-binding/DNA-binding proteins. Mis18 are proteins involved in the priming of centromeres for recruiting CENP-A. Mis18-alpha and beta form part of a small complex with Mis18-binding protein. Mis18-alpha is found to interact with DNA de-methylases through a Leu-rich region located at its carboxyl terminus. This entry also includes the CULT domain proteins such as Cereblon.


Pssm-ID: 427204  Cd Length: 99  Bit Score: 37.68  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695559   111 VYNCVCCDTPLFDSSTKFDSGTGWPSY-YQPIGNNVKTKLDLSIIFMPR-----QEVVCAVCNAHLGHVFDDGPRP-TGK 183
Cdd:pfam03226   2 VFQCKRCNTILGDSLALVSSGRELNTIvLKKVTRNVVVGKELVTSESGFddctySPLFCAGCGAVLGRKYRSTPEElDYK 81

                          90
                  ....*....|.
gi 30695559   184 R--YCLNSAAL 192
Cdd:pfam03226  82 RglFCLETDAI 92
 
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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