methionine-R-sulfoxide reductase B1 isoform 2 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SelR super family | cl15841 | SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ... |
7-59 | 9.46e-15 | ||
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. The actual alignment was detected with superfamily member pfam01641: Pssm-ID: 472838 Cd Length: 120 Bit Score: 63.91 E-value: 9.46e-15
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| Name | Accession | Description | Interval | E-value | ||
| SelR | pfam01641 | SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ... |
7-59 | 9.46e-15 | ||
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: 63.91 E-value: 9.46e-15
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| MsrB | COG0229 | Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ... |
14-59 | 1.28e-14 | ||
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 439999 Cd Length: 133 Bit Score: 63.95 E-value: 1.28e-14
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| TIGR00357 | TIGR00357 | methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ... |
7-59 | 2.24e-11 | ||
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: 55.93 E-value: 2.24e-11
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| PRK05550 | PRK05550 | bifunctional methionine sulfoxide reductase B/A protein; Provisional |
7-50 | 2.95e-10 | ||
bifunctional methionine sulfoxide reductase B/A protein; Provisional Pssm-ID: 235499 [Multi-domain] Cd Length: 283 Bit Score: 54.52 E-value: 2.95e-10
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| Name | Accession | Description | Interval | E-value | ||
| SelR | pfam01641 | SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ... |
7-59 | 9.46e-15 | ||
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: 63.91 E-value: 9.46e-15
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| MsrB | COG0229 | Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ... |
14-59 | 1.28e-14 | ||
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 439999 Cd Length: 133 Bit Score: 63.95 E-value: 1.28e-14
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| TIGR00357 | TIGR00357 | methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ... |
7-59 | 2.24e-11 | ||
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: 55.93 E-value: 2.24e-11
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| PRK05550 | PRK05550 | bifunctional methionine sulfoxide reductase B/A protein; Provisional |
7-50 | 2.95e-10 | ||
bifunctional methionine sulfoxide reductase B/A protein; Provisional Pssm-ID: 235499 [Multi-domain] Cd Length: 283 Bit Score: 54.52 E-value: 2.95e-10
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| PRK05508 | PRK05508 | methionine-R-sulfoxide reductase; |
7-50 | 7.35e-10 | ||
methionine-R-sulfoxide reductase; Pssm-ID: 180121 Cd Length: 119 Bit Score: 51.64 E-value: 7.35e-10
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| PRK14018 | PRK14018 | bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ... |
12-55 | 7.02e-07 | ||
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: 45.25 E-value: 7.02e-07
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| Blast search parameters | ||||
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