NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|301336164|ref|NP_001180390|]
View 

methionine-R-sulfoxide reductase B3 isoform 2 precursor [Homo sapiens]

Protein Classification

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

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

EC:  1.8.4.12
Gene Symbol:  msrB
Gene Ontology:  GO:0008270|GO:0033743
PubMed:  32943184|36084791

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 35-163 1.12e-84

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


:

Pssm-ID: 439999  Cd Length: 133  Bit Score: 245.38  E-value: 1.12e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164  35 KVVFSQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFT 114
Cdd:COG0229    4 KVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEK 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 301336164 115 DDFSYGMHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTPAD 163
Cdd:COG0229   84 EDRSHGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKE 132
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 35-163 1.12e-84

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 245.38  E-value: 1.12e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164  35 KVVFSQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFT 114
Cdd:COG0229    4 KVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEK 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 301336164 115 DDFSYGMHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTPAD 163
Cdd:COG0229   84 EDRSHGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKE 132
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 42-161 1.89e-80

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: 234.56  E-value: 1.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164   42 ELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFSYGM 121
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 301336164  122 HRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTP 161
Cdd:pfam01641  81 VRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 39-163 5.27e-68

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: 203.46  E-value: 5.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164   39 SQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFS 118
Cdd:TIGR00357   3 SDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDES 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 301336164  119 YGMHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTPAD 163
Cdd:TIGR00357  83 HGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIPLE 127
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 42-163 4.18e-55

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 175.86  E-value: 4.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164  42 ELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFSygm 121
Cdd:PRK05550   2 DKMKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADG--- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 301336164 122 HRVETSCSQCGAHLGHIF-DDGPRPTGKRYCINSAALSFTPAD 163
Cdd:PRK05550  79 RRTEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFVPAE 121
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 35-163 1.12e-84

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 245.38  E-value: 1.12e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164  35 KVVFSQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFT 114
Cdd:COG0229    4 KVKKSDAEWRARLTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEK 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 301336164 115 DDFSYGMHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTPAD 163
Cdd:COG0229   84 EDRSHGMVRTEVRCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKE 132
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 42-161 1.89e-80

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: 234.56  E-value: 1.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164   42 ELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFSYGM 121
Cdd:pfam01641   1 EWRKRLTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 301336164  122 HRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTP 161
Cdd:pfam01641  81 VRTEVRCARCGGHLGHVFDDGPPPTGLRYCINSASLKFIP 120
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 39-163 5.27e-68

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: 203.46  E-value: 5.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164   39 SQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFS 118
Cdd:TIGR00357   3 SDEELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDES 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 301336164  119 YGMHRVETSCSQCGAHLGHIFDDGPRPTGKRYCINSAALSFTPAD 163
Cdd:TIGR00357  83 HGMIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFIPLE 127
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 42-163 4.18e-55

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 175.86  E-value: 4.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164  42 ELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDFSygm 121
Cdd:PRK05550   2 DKMKSLTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADG--- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 301336164 122 HRVETSCSQCGAHLGHIF-DDGPRPTGKRYCINSAALSFTPAD 163
Cdd:PRK05550  79 RRTEIVCANCGAHLGHVFeGEGLTPKNTRHCVNSASLDFVPAE 121
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 38-163 5.96e-46

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: 157.73  E-value: 5.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164  38 FSQQELRKRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSEAITFTDDF 117
Cdd:PRK14018 380 PSDAELKRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDF 459

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 301336164 118 SYGMHRVETSCSQCGAHLGHIFDDGPRP-TGKRYCINSAALSFTPAD 163
Cdd:PRK14018 460 SYNMRRTEVRSRAADSHLGHVFPDGPRDkGGLRYCINGASLKFIPLE 506
PRK05508 PRK05508
methionine-R-sulfoxide reductase;
45-161 2.72e-36

methionine-R-sulfoxide reductase;


Pssm-ID: 180121  Cd Length: 119  Bit Score: 122.52  E-value: 2.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301336164  45 KRLTPLQYHVTQEKGTESAFEGEYTHHKDPGIYKCVVCGTPLFKSETKFDSGSGWPSFHDVINSeAITFTDDfSYGMhRV 124
Cdd:PRK05508   2 NELTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSFDDEIKG-AVKRIPD-ADGR-RT 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 301336164 125 ETSCSQCGAHLGHIFdDGPRPTGK--RYCINSAALSFTP 161
Cdd:PRK05508  79 EIVCANCGGHLGHVF-EGEGFTPKntRHCVNSISLKFVP 116
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH