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Conserved domains on  [gi|261278720|pdb|3HCI|A]
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Chain A, Peptide methionine sulfoxide reductase

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, ...
 21-138 9.81e-77

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


:

Pssm-ID: 439999  Cd Length: 133  Bit Score: 224.19  E-value: 9.81e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A       21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSYGMVRTEI 100
Cdd:COG0229  16 LTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSHGMVRTEV 95

                        90       100       110
                ....*....|....*....|....*....|....*...
3HCI_A      101 VCARCDSHLGHVFPDGPPPTGERHSLNSVSLAFTEDGQ 138
Cdd:COG0229  96 RCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 21-138 9.81e-77

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 224.19  E-value: 9.81e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A       21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSYGMVRTEI 100
Cdd:COG0229  16 LTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSHGMVRTEV 95

                        90       100       110
                ....*....|....*....|....*....|....*...
3HCI_A      101 VCARCDSHLGHVFPDGPPPTGERHSLNSVSLAFTEDGQ 138
Cdd:COG0229  96 RCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 21-133 7.80e-74

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: 216.45  E-value: 7.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A         21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSYGMVRTEI 100
Cdd:pfam01641   6 LTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGMVRTEV 85

                          90       100       110
                  ....*....|....*....|....*....|...
3HCI_A        101 VCARCDSHLGHVFPDGPPPTGERHSLNSVSLAF 133
Cdd:pfam01641  86 RCARCGGHLGHVFDDGPPPTGLRYCINSASLKF 118
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 15-134 9.88e-54

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: 166.10  E-value: 9.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A         15 DALIAGLSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSYG 94
Cdd:TIGR00357   5 EELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDESHG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
3HCI_A         95 MVRTEIVCARCDSHLGHVFPDGPPPTGERHSLNSVSLAFT 134
Cdd:TIGR00357  85 MIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFI 124
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 21-143 1.13e-49

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 160.45  E-value: 1.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A        21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSygmVRTEI 100
Cdd:PRK05550   7 LTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADG---RRTEI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
3HCI_A       101 VCARCDSHLGHVFPDGPP-PTGERHSLNSVSLAFTEDGQPLPNP 143
Cdd:PRK05550  84 VCANCGAHLGHVFEGEGLtPKNTRHCVNSASLDFVPAEEGAYDT 127
 
Name Accession Description Interval E-value
MsrB COG0229
Peptide methionine sulfoxide reductase MsrB [Posttranslational modification, protein turnover, ...
 21-138 9.81e-77

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


Pssm-ID: 439999  Cd Length: 133  Bit Score: 224.19  E-value: 9.81e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A       21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSYGMVRTEI 100
Cdd:COG0229  16 LTPEQYRVLREKGTERPFSGEYWDNKEEGIYVCAGCGAPLFSSDTKFDSGTGWPSFTKPIDPGAVEEKEDRSHGMVRTEV 95

                        90       100       110
                ....*....|....*....|....*....|....*...
3HCI_A      101 VCARCDSHLGHVFPDGPPPTGERHSLNSVSLAFTEDGQ 138
Cdd:COG0229  96 RCARCGAHLGHVFDDGPPPTGLRYCINSAALRFIPKEE 133
SelR pfam01641
SelR domain; Methionine sulfoxide reduction is an important process, by which cells regulate ...
 21-133 7.80e-74

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: 216.45  E-value: 7.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A         21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSYGMVRTEI 100
Cdd:pfam01641   6 LTPEQYRVLREKGTERPFTGEYWDNKEPGIYVCAGCGTPLFSSDTKFDSGCGWPSFYDPIPGDAVKEKEDTSHGMVRTEV 85

                          90       100       110
                  ....*....|....*....|....*....|...
3HCI_A        101 VCARCDSHLGHVFPDGPPPTGERHSLNSVSLAF 133
Cdd:pfam01641  86 RCARCGGHLGHVFDDGPPPTGLRYCINSASLKF 118
TIGR00357 TIGR00357
methionine-R-sulfoxide reductase; This model describes a domain found in PilB, a protein ...
 15-134 9.88e-54

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: 166.10  E-value: 9.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A         15 DALIAGLSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSYG 94
Cdd:TIGR00357   5 EELKKKLTPLQYEVTQNAGTEPPFTNEYWDNKEEGIYVDITCGEPLFSSEDKFDSGCGWPSFYKPISEEVVAYERDESHG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
3HCI_A         95 MVRTEIVCARCDSHLGHVFPDGPPPTGERHSLNSVSLAFT 134
Cdd:TIGR00357  85 MIRTEVRCRNCDAHLGHVFDDGPEPTGLRYCINSAALKFI 124
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 21-143 1.13e-49

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 160.45  E-value: 1.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A        21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSygmVRTEI 100
Cdd:PRK05550   7 LTPFEYRVIEDKGTERPFSGEYYDHDEKGVYLCRRCGAPLFRSEDKFNSGCGWPSFDDEIPGAVKRLPDADG---RRTEI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
3HCI_A       101 VCARCDSHLGHVFPDGPP-PTGERHSLNSVSLAFTEDGQPLPNP 143
Cdd:PRK05550  84 VCANCGAHLGHVFEGEGLtPKNTRHCVNSASLDFVPAEEGAYDT 127
PRK05508 PRK05508
methionine-R-sulfoxide reductase;
21-137 9.53e-40

methionine-R-sulfoxide reductase;


Pssm-ID: 180121  Cd Length: 119  Bit Score: 130.22  E-value: 9.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A        21 LSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFfapyD---PAHVREIRDTSyGMvR 97
Cdd:PRK05508   4 LTPEEEAVILRKGTEPPFSGEYNDFFEKGTYVCKQCGAPLYRSEDKFKSGCGWPSF----DdeiKGAVKRIPDAD-GR-R 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
3HCI_A        98 TEIVCARCDSHLGHVFP-DGPPPTGERHSLNSVSLAFTEDG 137
Cdd:PRK05508  78 TEIVCANCGGHLGHVFEgEGFTPKNTRHCVNSISLKFVPDK 118
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 14-133 2.58e-29

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: 111.51  E-value: 2.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HCI_A        14 RDALIAGLSDEEQRVLLHHGTEAPFCGVFLDNKLDGVYTCRLCGLPLFRSNAKFDSGTGWPSFFAPYDPAHVREIRDTSY 93
Cdd:PRK14018 382 DAELKRTLTEEQYQITQNAATERAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKVVTEHDDFSY 461

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
3HCI_A        94 GMVRTEIVCARCDSHLGHVFPDGPPP-TGERHSLNSVSLAF 133
Cdd:PRK14018 462 NMRRTEVRSRAADSHLGHVFPDGPRDkGGLRYCINGASLKF 502
 
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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