|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
5-160 |
1.04e-78 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 230.73 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 5 NVYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKIS 84
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEFC 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581786437 85 REKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGS-PIKWNFTKFIIDRQGNVVNRFLPMEDPLD--ISTNIEILL 160
Cdd:COG0386 83 SLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKLL 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
5-156 |
9.61e-78 |
|
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.
Pssm-ID: 238207 [Multi-domain] Cd Length: 152 Bit Score: 227.78 E-value: 9.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 5 NVYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKIS 84
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581786437 85 REKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGSPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNI 156
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
4-163 |
5.66e-48 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 153.22 E-value: 5.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 4 RNVYDIEVSDYKGLTYKLEAFRGKVILVVNTATEC-IYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILK 82
Cdd:PLN02412 7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCgLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 83 ISREKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGSPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNIEILLQE 162
Cdd:PLN02412 87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLGQ 166
|
.
gi 581786437 163 S 163
Cdd:PLN02412 167 A 167
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
6-113 |
2.52e-37 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 124.00 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 6 VYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKISR 85
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*...
gi 581786437 86 EKFGVTFPVLAKISVNGNDEHPLFTHLK 113
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
7-160 |
3.90e-33 |
|
putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.
Pssm-ID: 131592 [Multi-domain] Cd Length: 153 Bit Score: 114.93 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 7 YDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQ-LKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKISR 85
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581786437 86 EKFGVTFPVLAKISVNGNDEHPLFTHLKNEQpgifGSPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNIEILL 160
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
5-160 |
1.04e-78 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 230.73 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 5 NVYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKIS 84
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEFC 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581786437 85 REKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGS-PIKWNFTKFIIDRQGNVVNRFLPMEDPLD--ISTNIEILL 160
Cdd:COG0386 83 SLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPGLLGGgDIKWNFTKFLIDRDGNVVARFAPTTKPEDpeLEAAIEKLL 161
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
5-156 |
9.61e-78 |
|
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.
Pssm-ID: 238207 [Multi-domain] Cd Length: 152 Bit Score: 227.78 E-value: 9.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 5 NVYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKIS 84
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEFC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581786437 85 REKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGSPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNI 156
Cdd:cd00340 81 ETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPGLLGKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
4-163 |
5.66e-48 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 153.22 E-value: 5.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 4 RNVYDIEVSDYKGLTYKLEAFRGKVILVVNTATEC-IYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILK 82
Cdd:PLN02412 7 KSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCgLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 83 ISREKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGSPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNIEILLQE 162
Cdd:PLN02412 87 TVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGGLFGDAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLGQ 166
|
.
gi 581786437 163 S 163
Cdd:PLN02412 167 A 167
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
6-149 |
7.83e-47 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 150.69 E-value: 7.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 6 VYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKISR 85
Cdd:PRK10606 5 ILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEIKTYCR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 86 EKFGVTFPVLAKISVNGNDEHPLFTHL--------KNEQPGIFG-------SP-----IKWNFTKFIIDRQGNVVNRFLP 145
Cdd:PRK10606 85 TTWGVTFPMFSKIEVNGEGRHPLYQKLiaaaptavAPEESGFYArmvskgrAPlypddILWNFEKFLVGRDGQVIQRFSP 164
|
....*..
gi 581786437 146 -M--EDP 149
Cdd:PRK10606 165 dMtpEDP 171
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
4-160 |
5.46e-40 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 135.03 E-value: 5.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 4 RNVYDIEVSDYKGLTYKLEAFRGKVILVVNTATEC-IYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILK 82
Cdd:PLN02399 77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCgLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQ 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581786437 83 ISREKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGSPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNIEILL 160
Cdd:PLN02399 157 FACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAGGFLGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKLL 234
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
6-113 |
2.52e-37 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 124.00 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 6 VYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKISR 85
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFCP 80
|
90 100
....*....|....*....|....*...
gi 581786437 86 EKFGVTFPVLAKISVNGNDEHPLFTHLK 113
Cdd:pfam00255 81 GGYGVTFPLFSKIEVNGEKAHPVYKFLK 108
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
5-161 |
1.15e-35 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 122.17 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 5 NVYDIEVSDYKGLTYKLEAFRG-KVILVVNTATEC-IYSEQLKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILK 82
Cdd:PTZ00256 19 SFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCgLTSDHYTQLVELYKQYKSQGLEILAFPCNQFMEQEPWDEPEIKE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 83 ISREKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFGSP-----IKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNIE 157
Cdd:PTZ00256 99 YVQKKFNVDFPLFQKIEVNGENTHEIYKYLRRNSELFQNNTnearqIPWNFAKFLIDGQGKVVKYFSPKVNPNEMIQDIE 178
|
....
gi 581786437 158 ILLQ 161
Cdd:PTZ00256 179 KLLN 182
|
|
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
7-160 |
3.90e-33 |
|
putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.
Pssm-ID: 131592 [Multi-domain] Cd Length: 153 Bit Score: 114.93 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 7 YDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQ-LKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILKISR 85
Cdd:TIGR02540 3 YSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESFAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581786437 86 EKFGVTFPVLAKISVNGNDEHPLFTHLKNEQpgifGSPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNIEILL 160
Cdd:TIGR02540 83 RNYGVTFPMFSKIKILGSEAEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
4-164 |
1.16e-31 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 112.25 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 4 RNVYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYSEQ-LKKLETLFQKYKDRGFVVLSFPNNNFDNRQPGSNEEILK 82
Cdd:PTZ00056 17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKhVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTKDIRK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 83 ISrEKFGVTFPVLAKISVNGNDEHPLFTHLKNEQPGIFG-----SPIKWNFTKFIIDRQGNVVNRFLPMEDPLDISTNIE 157
Cdd:PTZ00056 97 FN-DKNKIKYNFFEPIEVNGENTHELFKFLKANCDSMHDengtlKAIGWNFGKFLVNKSGNVVAYFSPRTEPLELEKKIA 175
|
....*..
gi 581786437 158 ILLQESS 164
Cdd:PTZ00056 176 ELLGVKD 182
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
4-162 |
8.88e-14 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 64.33 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 4 RNVYDIEVSDYKGLTYKLEAFRGKVILVVNTATECIYS-EQLKKLETLFQKYKdrGFVVLSFpnnNFDnrqpgSNEEILK 82
Cdd:COG0526 6 KPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCrAEMPVLKELAEEYG--GVVFVGV---DVD-----ENPEAVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 83 ISREKFGVTFPVLAkisvngNDEHPLFTHLkneqpGIFGSPikwnfTKFIIDRQGNVVNRFLPMEDPLDISTNIEILLQE 162
Cdd:COG0526 76 AFLKELGLPYPVLL------DPDGELAKAY-----GVRGIP-----TTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
8-162 |
1.23e-12 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 61.42 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 8 DIEVSDYKGLTYKLEAFRGKVILVVNTATECIYS-EQLKKLETLFQKYKDRGFVVLSFpnnNFDnrqpgSNEEILKIsRE 86
Cdd:COG1225 3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCtAELPELRDLYEEFKDKGVEVLGV---SSD-----SDEAHKKF-AE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581786437 87 KFGVTFPVLAkisvngnDEHPLFThlknEQPGIFGSPikwnfTKFIIDRQGNVVNRFL-PMEDPLDISTNIEILLQE 162
Cdd:COG1225 74 KYGLPFPLLS-------DPDGEVA----KAYGVRGTP-----TTFLIDPDGKIRYVWVgPVDPRPHLEEVLEALLAE 134
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
8-144 |
5.29e-09 |
|
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.
Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 51.47 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 8 DIEVSDYKGLTYKLEAFRGKVILVVNTATECIYS-EQLKKLETLFQKYKDRGFVVLSFpnnNFDNRQPGSNEEILKisre 86
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCrAEMPELEALAKEYKDDGVEVVGV---NVDDDDPAAVKAFLK---- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 581786437 87 KFGVTFPVLAkisvngNDEHPLFTHLkneqpGIFGSPikwnfTKFIIDRQGNVVNRFL 144
Cdd:cd02966 74 KYGITFPVLL------DPDGELAKAY-----GVRGLP-----TTFLIDRDGRIRARHV 115
|
|
| Redoxin |
pfam08534 |
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
18-153 |
2.55e-05 |
|
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 41.97 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581786437 18 TYKLEAFRGKVILVVNTATE----CiySEQLKKLETLFQKYKDRGFVVLSFpnnNFDNRQPGSNEEIlkisrEKFGVTFP 93
Cdd:pfam08534 20 TVSLSDFKGKKVVLNFWPGAfcptC--SAEHPYLEKLNELYKEKGVDVVAV---NSDNDAFFVKRFW-----GKEGLPFP 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581786437 94 VLAkisvngnDEHPLFTHlkneqpgIFGSPIKWNFTK-------FIIDRQGNVVNRFLPMEDPLDIS 153
Cdd:pfam08534 90 FLS-------DGNAAFTK-------ALGLPIEEDASAglrspryAVIDEDGKVVYLFVGPEPGVDVS 142
|
|
| TlpA_like_DipZ_like |
cd03012 |
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ... |
18-140 |
4.55e-04 |
|
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.
Pssm-ID: 239310 [Multi-domain] Cd Length: 126 Bit Score: 38.06 E-value: 4.55e-04
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gi 581786437 18 TYKLEAFRGKVILVVNTATECIYS----EQLKKLEtlfQKYKDRGFVVLSFPNNNFDNRQPGSNeeiLKISREKFGVTFP 93
Cdd:cd03012 15 PLSLAQLRGKVVLLDFWTYCCINClhtlPYLTDLE---QKYKDDGLVVIGVHSPEFAFERDLAN---VKSAVLRYGITYP 88
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90 100 110 120
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gi 581786437 94 VlakisVNGNDeHPLFTHLKNEQpgifgspikWNfTKFIIDRQGNVV 140
Cdd:cd03012 89 V-----ANDND-YATWRAYGNQY---------WP-ALYLIDPTGNVR 119
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