|
Name |
Accession |
Description |
Interval |
E-value |
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
26-178 |
6.67e-111 |
|
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: 312.93 E-value: 6.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPIEVIRPDIAALV 178
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
26-174 |
3.64e-72 |
|
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: 214.69 E-value: 3.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTdRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK----KEPRWNFWKYLVNPEGQVVKFWRPEEPIEVIRPDI 174
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
26-177 |
2.13e-56 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 175.27 E-value: 2.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTdRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFWR----PEEPIevIRPDIAA 176
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFApttkPEDPE--LEAAIEK 159
|
.
3CYN_A 177 L 177
Cdd:COG0386 160 L 160
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
14-180 |
7.56e-47 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 151.84 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 14 GTENLyfQSMINSFYAFEVKDAKGRTVSLEKYKG-KVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFG 92
Cdd:PTZ00256 9 GLEQI--QPPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 93 ESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFL------VDSSKKEPR---WNFWKYLVNPEGQVVKFWRP 163
Cdd:PTZ00256 87 EQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselFQNNTNEARqipWNFAKFLIDGQGKVVKYFSP 166
|
170
....*....|....*..
3CYN_A 164 EEPIEVIRPDIAALVRQ 180
Cdd:PTZ00256 167 KVNPNEMIQDIEKLLNA 183
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
27-134 |
1.35e-38 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 128.24 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 27 FYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDrNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESFA 106
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*...
3CYN_A 107 RKNYGVTFPIFHKIKILGSEGEPAFRFL 134
Cdd:pfam00255 80 PGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gpx7 |
TIGR02540 |
putative glutathione peroxidase Gpx7; This model represents one of several families of known ... |
26-178 |
6.67e-111 |
|
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: 312.93 E-value: 6.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:TIGR02540 1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVASECGFTDQNYRALQELHRELGPSHFNVLAFPCNQFGESEPDSSKEIESF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPIEVIRPDIAALV 178
Cdd:TIGR02540 81 ARRNYGVTFPMFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPVEEIRPEITALV 153
|
|
| GSH_Peroxidase |
cd00340 |
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ... |
26-174 |
3.64e-72 |
|
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: 214.69 E-value: 3.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTdRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:cd00340 1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIKEF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK----KEPRWNFWKYLVNPEGQVVKFWRPEEPIEVIRPDI 174
Cdd:cd00340 80 CETNYGVTFPMFAKIDVNGENAHPLYKYLKEEAPgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDPEELEKDI 152
|
|
| BtuE |
COG0386 |
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ... |
26-177 |
2.13e-56 |
|
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];
Pssm-ID: 440155 [Multi-domain] Cd Length: 161 Bit Score: 175.27 E-value: 2.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTdRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:COG0386 3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFT-PQYEGLEALYEKYKDRGLVVLGFPCNQFGGQEPGSNEEIAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSK-----KEPRWNFWKYLVNPEGQVVKFWR----PEEPIevIRPDIAA 176
Cdd:COG0386 82 CSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEAPgllggGDIKWNFTKFLIDRDGNVVARFApttkPEDPE--LEAAIEK 159
|
.
3CYN_A 177 L 177
Cdd:COG0386 160 L 160
|
|
| PTZ00256 |
PTZ00256 |
glutathione peroxidase; Provisional |
14-180 |
7.56e-47 |
|
glutathione peroxidase; Provisional
Pssm-ID: 173495 [Multi-domain] Cd Length: 183 Bit Score: 151.84 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 14 GTENLyfQSMINSFYAFEVKDAKGRTVSLEKYKG-KVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFG 92
Cdd:PTZ00256 9 GLEQI--QPPTKSFFEFEAIDIDGQLVQLSKFKGkKAIIVVNVACKCGLTSDHYTQLVELYKQYKSQGLEILAFPCNQFM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 93 ESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFL------VDSSKKEPR---WNFWKYLVNPEGQVVKFWRP 163
Cdd:PTZ00256 87 EQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENTHEIYKYLrrnselFQNNTNEARqipWNFAKFLIDGQGKVVKYFSP 166
|
170
....*....|....*..
3CYN_A 164 EEPIEVIRPDIAALVRQ 180
Cdd:PTZ00256 167 KVNPNEMIQDIEKLLNA 183
|
|
| GSHPx |
pfam00255 |
Glutathione peroxidase; |
27-134 |
1.35e-38 |
|
Glutathione peroxidase;
Pssm-ID: 395197 Cd Length: 108 Bit Score: 128.24 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 27 FYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDrNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESFA 106
Cdd:pfam00255 1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASKCGLTP-QYTQLEELQERYKDRGLVILGFPCNQFGKQEPGSNEEIKYFC 79
|
90 100
....*....|....*....|....*...
3CYN_A 107 RKNYGVTFPIFHKIKILGSEGEPAFRFL 134
Cdd:pfam00255 80 PGGYGVTFPLFSKIEVNGEKAHPVYKFL 107
|
|
| btuE |
PRK10606 |
putative glutathione peroxidase; Provisional |
23-169 |
5.00e-38 |
|
putative glutathione peroxidase; Provisional
Pssm-ID: 182585 [Multi-domain] Cd Length: 183 Bit Score: 129.12 E-value: 5.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 23 MINSFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTdRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEV 102
Cdd:PRK10606 1 MQDSILTTVVTTIDGEVTTLEKYAGNVLLIVNVASKCGLT-PQYEQLENIQKAWADQGFVVLGFPCNQFLGQEPGSDEEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 103 ESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVD------------------SSKKEPR------WNFWKYLVNPEGQVV 158
Cdd:PRK10606 80 KTYCRTTWGVTFPMFSKIEVNGEGRHPLYQKLIAaaptavapeesgfyarmvSKGRAPLypddilWNFEKFLVGRDGQVI 159
|
170
....*....|....*
3CYN_A 159 KFWR----PEEPIEV 169
Cdd:PRK10606 160 QRFSpdmtPEDPIVM 174
|
|
| PLN02412 |
PLN02412 |
probable glutathione peroxidase |
26-180 |
1.22e-37 |
|
probable glutathione peroxidase
Pssm-ID: 166053 [Multi-domain] Cd Length: 167 Bit Score: 127.80 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:PLN02412 8 SIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQFLGQEPGSNEEIQQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLvdSSKK------EPRWNFWKYLVNPEGQVVKFWRPEEPIEVIRPDIAALVR 179
Cdd:PLN02412 88 VCTRFKAEFPIFDKVDVNGKNTAPLYKYL--KAEKgglfgdAIKWNFTKFLVSKEGKVVQRYAPTTSPLKIEKDIQNLLG 165
|
.
3CYN_A 180 Q 180
Cdd:PLN02412 166 Q 166
|
|
| PLN02399 |
PLN02399 |
phospholipid hydroperoxide glutathione peroxidase |
26-177 |
1.78e-35 |
|
phospholipid hydroperoxide glutathione peroxidase
Pssm-ID: 178021 [Multi-domain] Cd Length: 236 Bit Score: 124.24 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESF 105
Cdd:PLN02399 78 SVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQFGGQEPGSNPEIKQF 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3CYN_A 106 ARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSS----KKEPRWNFWKYLVNPEGQVVKFWRPEEPIEVIRPDIAAL 177
Cdd:PLN02399 158 ACTRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAggflGDLIKWNFEKFLVDKNGKVVERYPPTTSPFQIEKDIQKL 233
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
21-178 |
1.96e-29 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 107.63 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 21 QSMINSFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSK 100
Cdd:PTZ00056 13 DELRKSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQFLNQEFPNTK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 101 EVESFARKNyGVTFPIFHKIKILGSEGEPAFRFLV---------DSSKKEPRWNFWKYLVNPEGQVVKFWRPE-EPIEVI 170
Cdd:PTZ00056 93 DIRKFNDKN-KIKYNFFEPIEVNGENTHELFKFLKancdsmhdeNGTLKAIGWNFGKFLVNKSGNVVAYFSPRtEPLELE 171
|
....*...
3CYN_A 171 rPDIAALV 178
Cdd:PTZ00056 172 -KKIAELL 178
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
29-177 |
8.53e-09 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 51.79 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 29 AFEVKDAKGRTVSLEKYKGKVSLVVNVASDC-----QLTDrnylgLKELHKEFGPSHFSVLAFpcnqfgeSePRPSKEVE 103
Cdd:COG1225 3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCpgctaELPE-----LRDLYEEFKDKGVEVLGV-------S-SDSDEAHK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 104 SFARKnYGVTFPIF----HKI-KILGSEGEPAFrflvdsskkeprwnfwkYLVNPEGQVVKFWR-----PEEPIEVIRPD 173
Cdd:COG1225 70 KFAEK-YGLPFPLLsdpdGEVaKAYGVRGTPTT-----------------FLIDPDGKIRYVWVgpvdpRPHLEEVLEAL 131
|
....
3CYN_A 174 IAAL 177
Cdd:COG1225 132 LAEL 135
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
29-160 |
1.84e-07 |
|
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: 47.62 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 29 AFEVKDAKGRTVSLEKYKGKVsLVVNV-ASDC-----QLTDrnylgLKELHKEFGPSHFSVLAFpcNqFGESEPrpsKEV 102
Cdd:cd02966 1 DFSLPDLDGKPVSLSDLKGKV-VLVNFwASWCppcraEMPE-----LEALAKEYKDDGVEVVGV--N-VDDDDP---AAV 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
3CYN_A 103 ESFARKnYGVTFPIF----HKI-KILGSEGEPAFrflvdsskkeprwnfwkYLVNPEGQVVKF 160
Cdd:cd02966 69 KAFLKK-YGITFPVLldpdGELaKAYGVRGLPTT-----------------FLIDRDGRIRAR 113
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
30-136 |
1.36e-05 |
|
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).
Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 42.60 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 30 FEVKDAKGRTVSLEKYKGKVSLVVNVASD-CQLTDRNYLGLKELHKEFGPSHFSVLAFPCNqfgeseprPSKEVESFARK 108
Cdd:pfam00578 8 FELPDGDGGTVSLSDYRGKWVVLFFYPADwTPVCTTELPALADLYEEFKKLGVEVLGVSVD--------SPESHKAFAEK 79
|
90 100 110
....*....|....*....|....*....|....*...
3CYN_A 109 nYGVTFPIFH--------KIKILGSEGEPAFR--FLVD 136
Cdd:pfam00578 80 -YGLPFPLLSdpdgevarAYGVLNEEEGGALRatFVID 116
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
26-180 |
1.84e-05 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 42.75 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 26 SFYAFEVKDAKGRTVSLEKYKGKVsLVVNV-AS---DCQLTDRNylgLKELHKEFGPshFSVLAFPCNQFGEseprpskE 101
Cdd:COG0526 7 PAPDFTLTDLDGKPLSLADLKGKP-VLVNFwATwcpPCRAEMPV---LKELAEEYGG--VVFVGVDVDENPE-------A 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3CYN_A 102 VESFARKnYGVTFPIfhkikILGSEGEPAFRFLVDSSkkePRWnfwkYLVNPEGQVVKFWRPEEPIEVIRPDIAALVRQ 180
Cdd:COG0526 74 VKAFLKE-LGLPYPV-----LLDPDGELAKAYGVRGI---PTT----VLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
|
|
| Sco1 |
COG1999 |
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
31-179 |
3.22e-04 |
|
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441602 Cd Length: 156 Bit Score: 39.50 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 31 EVKDAKGRTVSLEKYKGKVSLVVNVASDCQ-----LTDRnylgLKELHKEFGP---SHFSVLAF---PCN-------QFG 92
Cdd:COG1999 4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPdvcptTLAN----LAQVQEALGEdggDDVQVLFIsvdPERdtpevlkAYA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CYN_A 93 ESEPRPS--------KEVESFARKnYGVTFpifhkikilgsEGEPAFRFLVDSSKkeprwNFwkYLVNPEGQVVKFWRPE 164
Cdd:COG1999 80 EAFGAPRwigltgdpEEIAALAKA-FGVYY-----------EKVPDGDYTFDHSA-----AV--YLVDPDGRLRGYYPAG 140
|
170
....*....|....*
3CYN_A 165 EPIEVIRPDIAALVR 179
Cdd:COG1999 141 EDPEELAADLKALLE 155
|
|
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