6TR8,2K8D,6SYM,3E0O,7E43


Conserved Protein Domain Family
SelR

?
pfam01641: SelR 
Click on image for an interactive view with Cn3D
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.
Statistics
?
PSSM-Id: 460278
Aligned: 805 rows
Threshold Bit Score: 99.3528
Created: 21-Mar-2022
Updated: 17-Oct-2022
Structure
?
Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
6TR8_A        31 EWRQRLSSEEYRVLREAGTEAPHTGEYT--------NTTTEGIYSCRACGTELFRSTEKFNSHCGWPSFFSPLAGDKVIE 102 Corynebacterium...
A0CJS4        29 ldrlSMDPHHYWIAVGKGMERPFTGEFC--------NHEQQGVYQCYHCKITLFQSDTKYQAQTGYASFFQHHKN-SVKI 99  Paramecium tetr...
A0C017        15 vdrLALTPHQYWIAAGKGMERPYTGEYW--------FNQEVGTYHCQHCDNQLFSFDSKYKSTTGYAQFWNHIPN-SVKL 85  Paramecium tetr...
EFC39086      39 EWMKILTSKQYEVLRRAGTEPSFCSGYKvfkdqlkeNNQEEGVFHCSGCDAPLFSAKTSFDSGSGWPSFWAPFKPKAIGY 118
XP_015782543  76 yLRSRLSAVAYEVTQEKGTELPFSGDLV--------HTDSAGVYYCLICDAELFSSKTKYDASCGWPSFYDAIDQSRVIL 147
EKC27912     388 SLRARLTPEQYHVTREKGTERRFSPGYD--------NH-KHGVYHCVVCNNTLFSSAHKYNSGTGWPSFYDRIGT-QMGI 457
Q7UMY6        68 ELRRRLNRIQYDVTQNAATEPAFSNAYW--------NNKKTGEYHCIVCDKPLFDSKTKFKSGTGWPSFYLPIEKDAVGY 139 Pirellula sp.
WP_015334104  52 AWRDQLSRAQYAVMWGGETEWPNSSALT--------TEHRAGTYHCAGCHNPLFSSATKFESHTGWPSFYAAIVDNAVYT 123 Fibrella aestua...
WP_008512297  40 EWKKLLTSNQYYIMVERGTEPPFKNAYF--------EMHDKGVFVSAATGEVLFSSADKFDSGTGWPSFVKPVDASKIEI 111 Mucilaginibacte...
XP_005852131  39 aaaapLTDFQRAVTLKARGRPGLRGRPC--------APHAQGVYVSAVGRLPLFSSEAKYDSGPGWPSFFAPIDPEHVGG 110
6TR8_A       103 RTDTSH-GMVRTEVICANCESHLGHVFAgEGYDTptDLRYCINSVCLTLIP 152 Corynebacterium diphtheriae
A0CJS4       100 IETKE--KFRYSALQCMNCQSYLGQISK-DGPPPt-FLRYSINSGALKFYq 146 Paramecium tetraurelia
A0C017        86 E--ESN-IKEERDLCCAGCDSFVGKVSF-DGPPPt-FIKYSINSAALNFKl 131 Paramecium tetraurelia
EFC39086     119 VVDKKF-GMERVEVVCTNCHSHLGHVFE-DGPRDktKLRYCINAVCLALKK 167
XP_015782543 148 TPDHTA-SRTRTEVSCARCDAHLGHFFQ-KET-TptGNRYCINSCALVFRK 195
EKC27912     458 VDDYAY-GMHRLEVTCERCGSHIGHVFN-DGPAPt-GLRYCMNSAAMLFVP 505
Q7UMY6       140 QTDYKM-IYPRTEVHCKRCKAHLGHLFD-DGPAPs-GKRFCMNSASMKFVE 187 Pirellula sp.
WP_015334104 124 EPDGN-----RTEVRCAVCDAHLGHVFN-DGPDp-tGLRYCLNGDALTFAl 167 Fibrella aestuarina
WP_008512297 112 VKDNSY-GMSRDEVIEKSTGLHLGHVFD-DGPADrgGKRYCMNSGALKFIK 160 Mucilaginibacter paludis
XP_005852131 111 DQDTSIpFMPRVEVVDARSGAHLGHVFD-DGPRPt-GKRYCMNAAALRFIP 159
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap