NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15240796|ref|NP_196364|]
View 

peptidemethionine sulfoxide reductase 3 [Arabidopsis thaliana]

Protein Classification

peptide-methionine (S)-S-oxide reductase( domain architecture ID 10000723)

peptide-methionine (S)-S-oxide reductase catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MsrA COG0225
Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, ...
32-180 5.02e-83

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


:

Pssm-ID: 439995  Cd Length: 177  Bit Score: 243.85  E-value: 5.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796  32 APGNQFAQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRH 111
Cdd:COG0225   1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCSGRTGHAEAVQVTYDPAVISYEELLEVFFEIH 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240796 112 DPTTLNRQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQMERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:COG0225  81 DPTQLNRQGNDRGTQYRSAIFYHDEEQKEIAEASIAALQASLDGPIVTEIEPAKTFYPAEDYHQDYLAK 149
 
Name Accession Description Interval E-value
MsrA COG0225
Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, ...
32-180 5.02e-83

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


Pssm-ID: 439995  Cd Length: 177  Bit Score: 243.85  E-value: 5.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796  32 APGNQFAQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRH 111
Cdd:COG0225   1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCSGRTGHAEAVQVTYDPAVISYEELLEVFFEIH 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240796 112 DPTTLNRQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQMERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:COG0225  81 DPTQLNRQGNDRGTQYRSAIFYHDEEQKEIAEASIAALQASLDGPIVTEIEPAKTFYPAEDYHQDYLAK 149
PMSR pfam01625
Peptide methionine sulfoxide reductase; This enzyme repairs damaged proteins. Methionine ...
40-180 1.24e-82

Peptide methionine sulfoxide reductase; This enzyme repairs damaged proteins. Methionine sulfoxide in proteins is reduced to methionine.


Pssm-ID: 460270  Cd Length: 153  Bit Score: 241.91  E-value: 1.24e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796    40 FGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRHDPTTLNRQ 119
Cdd:pfam01625   4 FAGGCFWGVEALFERLPGVISTEVGYAGGHTENPTYEEVCSGTTGHAEAVQVVYDPEVISYEELLELFFEIHDPTTLNRQ 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240796   120 GNDVGTQYRSGIYFYTPEQEKLARESLERHQQQM--ERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:pfam01625  84 GNDVGTQYRSAIFYHDEEQKEIAEASIAELQASGryGKPIVTEIEPAGNFYPAEDYHQDYLEK 146
msrA TIGR00401
methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase ...
38-180 4.08e-71

methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase (MsrA), a repair enzyme for proteins that have been inactivated by oxidation. The enzyme from E. coli is coextensive with this model and has enzymatic activity. However, in all completed genomes in which this module is present, a second protein module, described in TIGR00357, is also found, and in several cases as part of the same polypeptide chain: N-terminal to this module in Helicobacter pylori and Haemophilus influenzae (as in PilB of Neisseria gonorrhoeae) but C-terminal to it in Treponema pallidum. PilB, containing both domains, has been shown to be important for the expression of adhesins in certain pathogens. [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 129496  Cd Length: 149  Bit Score: 212.69  E-value: 4.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796    38 AQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRHDPTTLN 117
Cdd:TIGR00401   3 ATFAGGCFWGTEKYFRLIPGVVSTAVGYTNGYTPNPTYEEVCSGDTGHAEAVQVTYDPKVISYEELLDVFWEIHDPTTGN 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240796   118 RQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQM--ERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:TIGR00401  83 RQGNDIGTQYRSGIYYHSDAQEKAAAASKERLQAAAnyGDPIVTEIEPAENFYYAEEYHQQYLKK 147
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
28-182 3.81e-70

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 214.76  E-value: 3.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796   28 DDTPAPGNQFAQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLF 107
Cdd:PRK05550 120 AEEGAYDTEEAIFAGGCFWGVEYYFKKLPGVLSVESGYTGGDTKNPTYEQVCSGTTGHAEAVRVEFDPAKISYETLLKVF 199
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240796  108 WSRHDPTTLNRQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQmERKIMTEILPAKKFYRAEEHHQQYLSKGG 182
Cdd:PRK05550 200 FEIHDPTQLNRQGPDIGTQYRSAIFYHDDEQKQIAEKLIAELTKK-GYPVVTEVEAAGPFYPAEDYHQDYYEKHG 273
 
Name Accession Description Interval E-value
MsrA COG0225
Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, ...
32-180 5.02e-83

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


Pssm-ID: 439995  Cd Length: 177  Bit Score: 243.85  E-value: 5.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796  32 APGNQFAQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRH 111
Cdd:COG0225   1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCSGRTGHAEAVQVTYDPAVISYEELLEVFFEIH 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240796 112 DPTTLNRQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQMERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:COG0225  81 DPTQLNRQGNDRGTQYRSAIFYHDEEQKEIAEASIAALQASLDGPIVTEIEPAKTFYPAEDYHQDYLAK 149
PMSR pfam01625
Peptide methionine sulfoxide reductase; This enzyme repairs damaged proteins. Methionine ...
40-180 1.24e-82

Peptide methionine sulfoxide reductase; This enzyme repairs damaged proteins. Methionine sulfoxide in proteins is reduced to methionine.


Pssm-ID: 460270  Cd Length: 153  Bit Score: 241.91  E-value: 1.24e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796    40 FGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRHDPTTLNRQ 119
Cdd:pfam01625   4 FAGGCFWGVEALFERLPGVISTEVGYAGGHTENPTYEEVCSGTTGHAEAVQVVYDPEVISYEELLELFFEIHDPTTLNRQ 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240796   120 GNDVGTQYRSGIYFYTPEQEKLARESLERHQQQM--ERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:pfam01625  84 GNDVGTQYRSAIFYHDEEQKEIAEASIAELQASGryGKPIVTEIEPAGNFYPAEDYHQDYLEK 146
msrA TIGR00401
methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase ...
38-180 4.08e-71

methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase (MsrA), a repair enzyme for proteins that have been inactivated by oxidation. The enzyme from E. coli is coextensive with this model and has enzymatic activity. However, in all completed genomes in which this module is present, a second protein module, described in TIGR00357, is also found, and in several cases as part of the same polypeptide chain: N-terminal to this module in Helicobacter pylori and Haemophilus influenzae (as in PilB of Neisseria gonorrhoeae) but C-terminal to it in Treponema pallidum. PilB, containing both domains, has been shown to be important for the expression of adhesins in certain pathogens. [Protein fate, Protein modification and repair, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 129496  Cd Length: 149  Bit Score: 212.69  E-value: 4.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796    38 AQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRHDPTTLN 117
Cdd:TIGR00401   3 ATFAGGCFWGTEKYFRLIPGVVSTAVGYTNGYTPNPTYEEVCSGDTGHAEAVQVTYDPKVISYEELLDVFWEIHDPTTGN 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240796   118 RQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQM--ERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:TIGR00401  83 RQGNDIGTQYRSGIYYHSDAQEKAAAASKERLQAAAnyGDPIVTEIEPAENFYYAEEYHQQYLKK 147
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
28-182 3.81e-70

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 214.76  E-value: 3.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796   28 DDTPAPGNQFAQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLF 107
Cdd:PRK05550 120 AEEGAYDTEEAIFAGGCFWGVEYYFKKLPGVLSVESGYTGGDTKNPTYEQVCSGTTGHAEAVRVEFDPAKISYETLLKVF 199
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240796  108 WSRHDPTTLNRQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQmERKIMTEILPAKKFYRAEEHHQQYLSKGG 182
Cdd:PRK05550 200 FEIHDPTQLNRQGPDIGTQYRSAIFYHDDEQKQIAEKLIAELTKK-GYPVVTEVEAAGPFYPAEDYHQDYYEKHG 273
PRK13014 PRK13014
methionine sulfoxide reductase A; Provisional
29-180 3.72e-68

methionine sulfoxide reductase A; Provisional


Pssm-ID: 237269  Cd Length: 186  Bit Score: 206.40  E-value: 3.72e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796   29 DTPAPGNQFAQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFW 108
Cdd:PRK13014   2 DAAADGMETATFAGGCFWGVEGVFQHVPGVVSVVSGYSGGHVDNPTYEQVCTGTTGHAEAVQITYDPKQVSYENLLQIFF 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240796  109 SRHDPTTLNRQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQM--ERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:PRK13014  82 STHDPTQLNRQGPDRGEQYRSAIFYHDEEQKKVAEAYIAQLDEAGifKKPIVTPIKPYKNFYPAEDYHQDYLKK 155
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
43-180 6.59e-47

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: 161.20  E-value: 6.59e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796   43 GCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTtGHSEVVRVQYDLNDCTYESLLDLFWSRHDPTTLNRQGND 122
Cdd:PRK14018 206 GCFWGLEAYFQRIDGVVDAVSGYANGNTKNPSYEDVYRHS-GHAETVKVTYDADKLSLDTILQYYFRVVDPTSLNKQGND 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15240796  123 VGTQYRSGIYFYTPEQEKLARESLERHQQQMERKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:PRK14018 285 TGTQYRSGVYYTDPADKAVIAAALKREQQKYQLPLVVENEPLKNFYDAEEYHQDYLIK 342
PRK05528 PRK05528
peptide-methionine (S)-S-oxide reductase;
40-180 6.67e-30

peptide-methionine (S)-S-oxide reductase;


Pssm-ID: 235497  Cd Length: 156  Bit Score: 107.79  E-value: 6.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240796   40 FGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSygdvcSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRHDPTTLNRQ 119
Cdd:PRK05528   6 FAGGCLWGVQAFFKTLPGVIHTEAGRANGRTSTLD-----GPYDGYAECVKTHFDPRMVSITDLMGYLFEIIDPYSVNKQ 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240796  120 GNDVGTQYRSGIYFYTPEQEKLARESLERHQQQmeRKIMTEILPAKKFYRAEEHHQQYLSK 180
Cdd:PRK05528  81 GNDVGEKYRTGIYSEVDDHLIEARQFIERREDA--DKIAVEVLPLTNYVKSAEEHQDRLEK 139
 
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