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Conserved domains on  [gi|1148550924|ref|WP_077298651|]
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glutathione peroxidase [Aquaspirillum sp. LM1]

Protein Classification

glutathione peroxidase( domain architecture ID 10785352)

glutathione peroxidase catalyzes the reduction of hydroperoxides using GSH as a specific electron donor

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0043295|GO:0004602
PubMed:  11215509
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 25-179 7.64e-79

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


:

Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 231.89  E-value: 7.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  25 CPPLLKHRFTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAE 103
Cdd:COG0386     1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924 104 FCKLTYFVDFPMIEKARVSSAQAMPFYRQLAAAT-----GQPPRWNFHKYVIAPGGKQVWAFPSEVEPDSPQLLKAIQPY 178
Cdd:COG0386    81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEApgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIEKL 160


                  .
gi 1148550924 179 L 179
Cdd:COG0386   161 L 161
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 25-179 7.64e-79

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 231.89  E-value: 7.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  25 CPPLLKHRFTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAE 103
Cdd:COG0386     1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924 104 FCKLTYFVDFPMIEKARVSSAQAMPFYRQLAAAT-----GQPPRWNFHKYVIAPGGKQVWAFPSEVEPDSPQLLKAIQPY 178
Cdd:COG0386    81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEApgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIEKL 160


                  .
gi 1148550924 179 L 179
Cdd:COG0386   161 L 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 33-175 1.91e-58

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: 180.02  E-value: 1.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  33 FTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFV 111
Cdd:cd00340     7 VKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIKEFCETNYGV 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148550924 112 DFPMIEKARVSSAQAMPFYRQLAAATGQP----PRWNFHKYVIAPGGKQVWAFPSEVEPdsPQLLKAI 175
Cdd:cd00340    87 TFPMFAKIDVNGENAHPLYKYLKEEAPGLlgkdIKWNFTKFLVDRDGEVVKRFAPTTDP--EELEKDI 152
btuE PRK10606
putative glutathione peroxidase; Provisional
 34-176 3.50e-39

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 131.82  E-value: 3.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  34 TTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFVD 112
Cdd:PRK10606   11 TTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFlGQEPGSDEEIKTYCRTTWGVT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924 113 FPMIEKARVSSAQAMPFYRQLAAAT------------------GQPPR------WNFHKYVIAPGGKQVWAFPSEVEPDS 168
Cdd:PRK10606   91 FPMFSKIEVNGEGRHPLYQKLIAAAptavapeesgfyarmvskGRAPLypddilWNFEKFLVGRDGQVIQRFSPDMTPED 170


                  ....*...
gi 1148550924 169 PQLLKAIQ 176
Cdd:PRK10606  171 PIVMESIK 178
GSHPx pfam00255
Glutathione peroxidase;
35-133 2.64e-31

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 109.36  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  35 TLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFVDF 113
Cdd:pfam00255   8 DIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFgKQEPGSNEEIKYFCPGGYGVTF 87

                          90       100
                  ....*....|....*....|
gi 1148550924 114 PMIEKARVSSAQAMPFYRQL 133
Cdd:pfam00255  88 PLFSKIEVNGEKAHPVYKFL 107
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 37-177 3.08e-27

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: 100.30  E-value: 3.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  37 QGQPLDLCAHQNKVILVVNTASKCGYTRQ-FEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFVDFP 114
Cdd:TIGR02540  11 RGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFgESEPDSSKEIESFARRNYGVTFP 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148550924 115 MIEKARVSSAQAMPFYRQLAAATGQPPRWNFHKYVIAPGGKQVWAFpsevEPDSPqlLKAIQP 177
Cdd:TIGR02540  91 MFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFW----RPEEP--VEEIRP 147
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 25-179 7.64e-79

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 231.89  E-value: 7.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  25 CPPLLKHRFTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAE 103
Cdd:COG0386     1 MMSIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924 104 FCKLTYFVDFPMIEKARVSSAQAMPFYRQLAAAT-----GQPPRWNFHKYVIAPGGKQVWAFPSEVEPDSPQLLKAIQPY 178
Cdd:COG0386    81 FCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEApgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIEKL 160


                  .
gi 1148550924 179 L 179
Cdd:COG0386   161 L 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 33-175 1.91e-58

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: 180.02  E-value: 1.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  33 FTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFV 111
Cdd:cd00340     7 VKDIDGEPVSLSKYKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIKEFCETNYGV 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148550924 112 DFPMIEKARVSSAQAMPFYRQLAAATGQP----PRWNFHKYVIAPGGKQVWAFPSEVEPdsPQLLKAI 175
Cdd:cd00340    87 TFPMFAKIDVNGENAHPLYKYLKEEAPGLlgkdIKWNFTKFLVDRDGEVVKRFAPTTDP--EELEKDI 152
btuE PRK10606
putative glutathione peroxidase; Provisional
 34-176 3.50e-39

putative glutathione peroxidase; Provisional


Pssm-ID: 182585 [Multi-domain]  Cd Length: 183  Bit Score: 131.82  E-value: 3.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  34 TTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFVD 112
Cdd:PRK10606   11 TTIDGEVTTLEKYAGNVLLIVNVASKCGLTPQYEQLENIQKAWADQGFVVLGFPCNQFlGQEPGSDEEIKTYCRTTWGVT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924 113 FPMIEKARVSSAQAMPFYRQLAAAT------------------GQPPR------WNFHKYVIAPGGKQVWAFPSEVEPDS 168
Cdd:PRK10606   91 FPMFSKIEVNGEGRHPLYQKLIAAAptavapeesgfyarmvskGRAPLypddilWNFEKFLVGRDGQVIQRFSPDMTPED 170


                  ....*...
gi 1148550924 169 PQLLKAIQ 176
Cdd:PRK10606  171 PIVMESIK 178
GSHPx pfam00255
Glutathione peroxidase;
35-133 2.64e-31

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 109.36  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  35 TLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFVDF 113
Cdd:pfam00255   8 DIDGEPVPFDQYRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFgKQEPGSNEEIKYFCPGGYGVTF 87

                          90       100
                  ....*....|....*....|
gi 1148550924 114 PMIEKARVSSAQAMPFYRQL 133
Cdd:pfam00255  88 PLFSKIEVNGEKAHPVYKFL 107
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 37-177 3.08e-27

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: 100.30  E-value: 3.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  37 QGQPLDLCAHQNKVILVVNTASKCGYTRQ-FEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFVDFP 114
Cdd:TIGR02540  11 RGRTVSLEKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFgESEPDSSKEIESFARRNYGVTFP 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148550924 115 MIEKARVSSAQAMPFYRQLAAATGQPPRWNFHKYVIAPGGKQVWAFpsevEPDSPqlLKAIQP 177
Cdd:TIGR02540  91 MFSKIKILGSEAEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFW----RPEEP--VEEIRP 147
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 49-174 3.08e-26

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 98.68  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  49 KVILVVNTASKCGYTRQ-FEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAEFCKLTYFVDFPMIEKARVSSAQA 126
Cdd:PTZ00256   42 KAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFmEQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENT 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148550924 127 MPFYRQL----------AAATGQPPrWNFHKYVIAPGGKQVWAF-----PSEVEPDSPQLLKA 174
Cdd:PTZ00256  122 HEIYKYLrrnselfqnnTNEARQIP-WNFAKFLIDGQGKVVKYFspkvnPNEMIQDIEKLLNA 183
PLN02412 PLN02412
probable glutathione peroxidase
 23-174 1.46e-22

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 88.89  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  23 ADCPPLLKHRFTT--LQGQPLDLCAHQNKVILVVNTASKCGYTR-QFEPLEALSRRWRDQGLLVIGFPSNDF-NQELASN 98
Cdd:PLN02412    2 AEESPKSIYDFTVkdIGGNDVSLNQYKGKVLLIVNVASKCGLTDsNYKELNVLYEKYKEQGFEILAFPCNQFlGQEPGSN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  99 QEVAEFCKLTYFVDFPMIEKARVSSAQAMPFYRQLAAATG----QPPRWNFHKYVIAPGGKQVWAF-----PSEVEPDSP 169
Cdd:PLN02412   82 EEIQQTVCTRFKAEFPIFDKVDVNGKNTAPLYKYLKAEKGglfgDAIKWNFTKFLVSKEGKVVQRYapttsPLKIEKDIQ 161


                  ....*
gi 1148550924 170 QLLKA 174
Cdd:PLN02412  162 NLLGQ 166
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 26-172 8.37e-21

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 84.90  E-value: 8.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  26 PPLLKHRFTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQ-FEPLEALSRRWRDQGLLVIGFPSNDF-NQELASNQEVAE 103
Cdd:PTZ00056   17 KSIYDYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKhVDQMNRLHSVFNPLGLEILAFPTSQFlNQEFPNTKDIRK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924 104 FCKlTYFVDFPMIEKARVSSAQAMPFYRQLAAATG---------QPPRWNFHKYVIAPGGKQVWAF-----PSEVEPDSP 169
Cdd:PTZ00056   97 FND-KNKIKYNFFEPIEVNGENTHELFKFLKANCDsmhdengtlKAIGWNFGKFLVNKSGNVVAYFsprtePLELEKKIA 175


                  ...
gi 1148550924 170 QLL 172
Cdd:PTZ00056  176 ELL 178
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 31-179 5.36e-20

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 83.80  E-value: 5.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  31 HRFTT--LQGQPLDLCAHQNKVILVVNTASKCGYT-RQFEPLEALSRRWRDQGLLVIGFPSNDFN-QELASNQEVAEFCK 106
Cdd:PLN02399   80 HDFTVkdIDGKDVALSKFKGKVLLIVNVASKCGLTsSNYSELSHLYEKYKTQGFEILAFPCNQFGgQEPGSNPEIKQFAC 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148550924 107 LTYFVDFPMIEKARVSSAQAMPFYRQLAAAT----GQPPRWNFHKYVIAPGGKQVWAFPSEVEPDspQLLKAIQPYL 179
Cdd:PLN02399  160 TRFKAEFPIFDKVDVNGPSTAPVYQFLKSNAggflGDLIKWNFEKFLVDKNGKVVERYPPTTSPF--QIEKDIQKLL 234
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 23-181 5.60e-07

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 46.61  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  23 ADCPPLLKHRFTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEP-LEALSRRWRdqGLLVIGFPSNDfnqelaSNQEV 101
Cdd:COG0526     3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPvLKELAEEYG--GVVFVGVDVDE------NPEAV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924 102 AEFCKlTYFVDFPMIEKARVSSAQAMPfyrqlaaATGQPprwnfHKYVIAPGGKQVWAFPSEVEPDspQLLKAIQPYLRE 181
Cdd:COG0526    75 KAFLK-ELGLPYPVLLDPDGELAKAYG-------VRGIP-----TTVLIDKDGKIVARHVGPLSPE--ELEEALEKLLAK 139
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
33-181 1.48e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 42.93  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  33 FTTLQGQPLDLCAHQNKVILVVNTASKCGY-TRQFEPLEALSRRWRDQGLLVIGFpSNDfnqelaSNQEVAEFCKlTYFV 111
Cdd:COG1225     6 LPDLDGKTVSLSDLRGKPVVLYFYATWCPGcTAELPELRDLYEEFKDKGVEVLGV-SSD------SDEAHKKFAE-KYGL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148550924 112 DFPMI--EKARVSSAqampfYRqlaaATGQPprwnfHKYVIAPGGKQVWAFPSEVEPDsPQLLKAIQPYLRE 181
Cdd:COG1225    78 PFPLLsdPDGEVAKA-----YG----VRGTP-----TTFLIDPDGKIRYVWVGPVDPR-PHLEEVLEALLAE 134
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 33-128 8.23e-05

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: 40.30  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148550924  33 FTTLQGQPLDLCAHQNKVILVVNTASKCGYTRQFEP-LEALSRRWRDQGLLVIGfpsndFNQELASNQEVAEFCKlTYFV 111
Cdd:cd02966     4 LPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPeLEALAKEYKDDGVEVVG-----VNVDDDDPAAVKAFLK-KYGI 77

                          90       100
                  ....*....|....*....|..
gi 1148550924 112 DFPMI--EKARVSSA---QAMP 128
Cdd:cd02966    78 TFPVLldPDGELAKAygvRGLP 99
 
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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