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Conserved domains on  [gi|15234942|ref|NP_194243|]
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peptide met sulfoxide reductase 4 [Arabidopsis thaliana]

Protein Classification

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

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

EC:  1.8.4.11
Gene Ontology:  GO:0008113|GO:0036211|GO:0033744
PubMed:  11063566|36084791

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MsrA COG0225
Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, ...
 88-236 3.63e-90

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


:

Pssm-ID: 439995  Cd Length: 177  Bit Score: 264.26  E-value: 3.63e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942  88 SSGQQFAQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRH 167
Cdd:COG0225   1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCSGRTGHAEAVQVTYDPAVISYEELLEVFFEIH 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234942 168 DPTTLNRQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKILNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:COG0225  81 DPTQLNRQGNDRGTQYRSAIFYHDEEQKEIAEASIAALQASLDGPIVTEIEPAKTFYPAEDYHQDYLAK 149
 
Name Accession Description Interval E-value
MsrA COG0225
Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, ...
 88-236 3.63e-90

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


Pssm-ID: 439995  Cd Length: 177  Bit Score: 264.26  E-value: 3.63e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942  88 SSGQQFAQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRH 167
Cdd:COG0225   1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCSGRTGHAEAVQVTYDPAVISYEELLEVFFEIH 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234942 168 DPTTLNRQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKILNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:COG0225  81 DPTQLNRQGNDRGTQYRSAIFYHDEEQKEIAEASIAALQASLDGPIVTEIEPAKTFYPAEDYHQDYLAK 149
PMSR pfam01625
Peptide methionine sulfoxide reductase; This enzyme repairs damaged proteins. Methionine ...
 96-236 2.22e-89

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: 261.17  E-value: 2.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942    96 FGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRHDPTTLNRQ 175
Cdd:pfam01625   4 FAGGCFWGVEALFERLPGVISTEVGYAGGHTENPTYEEVCSGTTGHAEAVQVVYDPEVISYEELLELFFEIHDPTTLNRQ 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234942   176 GGDVGTQYRSGIYYYTDEQERIAREAVEKQQK--ILNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:pfam01625  84 GNDVGTQYRSAIFYHDEEQKEIAEASIAELQAsgRYGKPIVTEIEPAGNFYPAEDYHQDYLEK 146
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 82-238 1.14e-77

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 236.33  E-value: 1.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942   82 PDDDvPSSGQQFAQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLD 161
Cdd:PRK05550 119 PAEE-GAYDTEEAIFAGGCFWGVEYYFKKLPGVLSVESGYTGGDTKNPTYEQVCSGTTGHAEAVRVEFDPAKISYETLLK 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234942  162 VFWNRHDPTTLNRQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKIlNKRIVTEILPATKFYRAENYHQQYLAKGG 238
Cdd:PRK05550 198 VFFEIHDPTQLNRQGPDIGTQYRSAIFYHDDEQKQIAEKLIAELTKK-GYPVVTEVEAAGPFYPAEDYHQDYYEKHG 273
msrA TIGR00401
methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase ...
 94-236 3.90e-74

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: 222.70  E-value: 3.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942    94 AQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRHDPTTLN 173
Cdd:TIGR00401   3 ATFAGGCFWGTEKYFRLIPGVVSTAVGYTNGYTPNPTYEEVCSGDTGHAEAVQVTYDPKVISYEELLDVFWEIHDPTTGN 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234942   174 RQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKILN--KRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:TIGR00401  83 RQGNDIGTQYRSGIYYHSDAQEKAAAASKERLQAAANygDPIVTEIEPAENFYYAEEYHQQYLKK 147
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 163-181 4.90e-03

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212996  Cd Length: 62  Bit Score: 34.56  E-value: 4.90e-03
                        10
                ....*....|....*....
gi 15234942 163 FWNRHDPTTLNRQGGDVGT 181
Cdd:cd12063   9 FWNLHDPTALNVRAGDVIT 27
 
Name Accession Description Interval E-value
MsrA COG0225
Peptide methionine sulfoxide reductase MsrA [Posttranslational modification, protein turnover, ...
 88-236 3.63e-90

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


Pssm-ID: 439995  Cd Length: 177  Bit Score: 264.26  E-value: 3.63e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942  88 SSGQQFAQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRH 167
Cdd:COG0225   1 PAGTETATFAGGCFWCVEAVFEQLPGVISVVSGYAGGHTPNPTYEEVCSGRTGHAEAVQVTYDPAVISYEELLEVFFEIH 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234942 168 DPTTLNRQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKILNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:COG0225  81 DPTQLNRQGNDRGTQYRSAIFYHDEEQKEIAEASIAALQASLDGPIVTEIEPAKTFYPAEDYHQDYLAK 149
PMSR pfam01625
Peptide methionine sulfoxide reductase; This enzyme repairs damaged proteins. Methionine ...
 96-236 2.22e-89

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: 261.17  E-value: 2.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942    96 FGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRHDPTTLNRQ 175
Cdd:pfam01625   4 FAGGCFWGVEALFERLPGVISTEVGYAGGHTENPTYEEVCSGTTGHAEAVQVVYDPEVISYEELLELFFEIHDPTTLNRQ 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234942   176 GGDVGTQYRSGIYYYTDEQERIAREAVEKQQK--ILNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:pfam01625  84 GNDVGTQYRSAIFYHDEEQKEIAEASIAELQAsgRYGKPIVTEIEPAGNFYPAEDYHQDYLEK 146
PRK05550 PRK05550
bifunctional methionine sulfoxide reductase B/A protein; Provisional
 82-238 1.14e-77

bifunctional methionine sulfoxide reductase B/A protein; Provisional


Pssm-ID: 235499 [Multi-domain]  Cd Length: 283  Bit Score: 236.33  E-value: 1.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942   82 PDDDvPSSGQQFAQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLD 161
Cdd:PRK05550 119 PAEE-GAYDTEEAIFAGGCFWGVEYYFKKLPGVLSVESGYTGGDTKNPTYEQVCSGTTGHAEAVRVEFDPAKISYETLLK 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234942  162 VFWNRHDPTTLNRQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKIlNKRIVTEILPATKFYRAENYHQQYLAKGG 238
Cdd:PRK05550 198 VFFEIHDPTQLNRQGPDIGTQYRSAIFYHDDEQKQIAEKLIAELTKK-GYPVVTEVEAAGPFYPAEDYHQDYYEKHG 273
msrA TIGR00401
methionine-S-sulfoxide reductase; This model describes peptide methionine sulfoxide reductase ...
 94-236 3.90e-74

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: 222.70  E-value: 3.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942    94 AQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRHDPTTLN 173
Cdd:TIGR00401   3 ATFAGGCFWGTEKYFRLIPGVVSTAVGYTNGYTPNPTYEEVCSGDTGHAEAVQVTYDPKVISYEELLDVFWEIHDPTTGN 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234942   174 RQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKILN--KRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:TIGR00401  83 RQGNDIGTQYRSGIYYHSDAQEKAAAASKERLQAAANygDPIVTEIEPAENFYYAEEYHQQYLKK 147
PRK13014 PRK13014
methionine sulfoxide reductase A; Provisional
 85-236 1.35e-71

methionine sulfoxide reductase A; Provisional


Pssm-ID: 237269  Cd Length: 186  Bit Score: 217.57  E-value: 1.35e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942   85 DVPSSGQQFAQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFW 164
Cdd:PRK13014   2 DAAADGMETATFAGGCFWGVEGVFQHVPGVVSVVSGYSGGHVDNPTYEQVCTGTTGHAEAVQITYDPKQVSYENLLQIFF 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234942  165 NRHDPTTLNRQGGDVGTQYRSGIYYYTDEQERIAREAVEK--QQKILNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:PRK13014  82 STHDPTQLNRQGPDRGEQYRSAIFYHDEEQKKVAEAYIAQldEAGIFKKPIVTPIKPYKNFYPAEDYHQDYLKK 155
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 99-236 3.10e-44

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: 156.19  E-value: 3.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942   99 GCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTtGHNEVVRVQYDPKECSFESLLDVFWNRHDPTTLNRQGGD 178
Cdd:PRK14018 206 GCFWGLEAYFQRIDGVVDAVSGYANGNTKNPSYEDVYRHS-GHAETVKVTYDADKLSLDTILQYYFRVVDPTSLNKQGND 284

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234942  179 VGTQYRSGIYYYTDEQERIAREAVEKQQKILNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:PRK14018 285 TGTQYRSGVYYTDPADKAVIAAALKREQQKYQLPLVVENEPLKNFYDAEEYHQDYLIK 342
PRK05528 PRK05528
peptide-methionine (S)-S-oxide reductase;
96-236 3.66e-28

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


Pssm-ID: 235497  Cd Length: 156  Bit Score: 105.10  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234942   96 FGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYE-DvctgttGHNEVVRVQYDPKECSFESLLDVFWNRHDPTTLNR 174
Cdd:PRK05528   6 FAGGCLWGVQAFFKTLPGVIHTEAGRANGRTSTLDGPyD------GYAECVKTHFDPRMVSITDLMGYLFEIIDPYSVNK 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234942  175 QGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKilNKRIVTEILPATKFYRAENYHQQYLAK 236
Cdd:PRK05528  80 QGNDVGEKYRTGIYSEVDDHLIEARQFIERRED--ADKIAVEVLPLTNYVKSAEEHQDRLEK 139
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 163-181 4.90e-03

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212996  Cd Length: 62  Bit Score: 34.56  E-value: 4.90e-03
                        10
                ....*....|....*....
gi 15234942 163 FWNRHDPTTLNRQGGDVGT 181
Cdd:cd12063   9 FWNLHDPTALNVRAGDVIT 27
 
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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