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Conserved domains on  [gi|516456498|ref|WP_017845338|]
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MULTISPECIES: glutathione peroxidase [Pseudomonas]

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 ...
 24-179 5.68e-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: 5.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  24 CPPLLEGQLPKLrAKESIDLCQrFAGKPLVIVNTASFCGFAPQFKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEET 102
Cdd:COG0386    1 MMSIYDFSVTTL-DGEPVSLSD-YKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498 103 AKVCYVNYGVTFTMTEPQAVKGPDAVHLFKVLAQQ------SSAPKWNFYKYVVDRQGKVIANFSSLTKPDSPDLLKAVE 176
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEapgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIE 158


                 ...
gi 516456498 177 AAL 179
Cdd:COG0386  159 KLL 161
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 24-179 5.68e-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: 5.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  24 CPPLLEGQLPKLrAKESIDLCQrFAGKPLVIVNTASFCGFAPQFKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEET 102
Cdd:COG0386    1 MMSIYDFSVTTL-DGEPVSLSD-YKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498 103 AKVCYVNYGVTFTMTEPQAVKGPDAVHLFKVLAQQ------SSAPKWNFYKYVVDRQGKVIANFSSLTKPDSPDLLKAVE 176
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEapgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIE 158


                 ...
gi 516456498 177 AAL 179
Cdd:COG0386  159 KLL 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 39-175 3.46e-60

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: 184.26  E-value: 3.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  39 ESIDLCQrFAGKPLVIVNTASFCGFAPQFKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYGVTFTMT 117
Cdd:cd00340   13 EPVSLSK-YKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIKEFCETNYGVTFPMF 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516456498 118 EPQAVKGPDAVHLFKVLAQQS-----SAPKWNFYKYVVDRQGKVIANFSSLTKPdsPDLLKAV 175
Cdd:cd00340   92 AKIDVNGENAHPLYKYLKEEApgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDP--EELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
33-134 4.12e-24

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 90.87  E-value: 4.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498   33 PKLRAKESIDLCQrFAGKPLVIVNTASFCGFAPQFKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYG 111
Cdd:pfam00255   6 AKDIDGEPVPFDQ-YRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFgKQEPGSNEEIKYFCPGGYG 84

                          90       100
                  ....*....|....*....|...
gi 516456498  112 VTFTMTEPQAVKGPDAVHLFKVL 134
Cdd:pfam00255  85 VTFPLFSKIEVNGEKAHPVYKFL 107
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 50-179 2.22e-21

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 85.97  E-value: 2.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  50 KPLVIVNTASFCGFAPQ-FKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYGVTFTMTEPQAVKGPDA 127
Cdd:PTZ00256  42 KAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFmEQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENT 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516456498 128 VHLFKVLAQQSSAPK----------WNFYKYVVDRQGKVIANFSSLTKPDspDLLKAVEAAL 179
Cdd:PTZ00256 122 HEIYKYLRRNSELFQnntnearqipWNFAKFLIDGQGKVVKYFSPKVNPN--EMIQDIEKLL 181
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 45-157 1.31e-19

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: 80.65  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498   45 QRFAGKPLVIVNTASFCGFAPQ-FKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYGVTFTMTEPQAV 122
Cdd:TIGR02540  18 EKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFgESEPDSSKEIESFARRNYGVTFPMFSKIKI 97

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 516456498  123 KGPDAVHLFKVLAQQSSA-PKWNFYKYVVDRQGKVI 157
Cdd:TIGR02540  98 LGSEAEPAFRFLVDSSKKePRWNFWKYLVNPEGQVV 133
 
Name Accession Description Interval E-value
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 24-179 5.68e-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: 5.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  24 CPPLLEGQLPKLrAKESIDLCQrFAGKPLVIVNTASFCGFAPQFKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEET 102
Cdd:COG0386    1 MMSIYDFSVTTL-DGEPVSLSD-YKGKVLLIVNTASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498 103 AKVCYVNYGVTFTMTEPQAVKGPDAVHLFKVLAQQ------SSAPKWNFYKYVVDRQGKVIANFSSLTKPDSPDLLKAVE 176
Cdd:COG0386   79 AEFCSLNYGVTFPMFAKIDVNGPNAHPLYKYLKEEapgllgGGDIKWNFTKFLIDRDGNVVARFAPTTKPEDPELEAAIE 158


                 ...
gi 516456498 177 AAL 179
Cdd:COG0386  159 KLL 161
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 39-175 3.46e-60

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: 184.26  E-value: 3.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  39 ESIDLCQrFAGKPLVIVNTASFCGFAPQFKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYGVTFTMT 117
Cdd:cd00340   13 EPVSLSK-YKGKVLLIVNVASKCGFTPQYEGLEALYEKYKDRGLVVLGFPCNQFgGQEPGSNEEIKEFCETNYGVTFPMF 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516456498 118 EPQAVKGPDAVHLFKVLAQQS-----SAPKWNFYKYVVDRQGKVIANFSSLTKPdsPDLLKAV 175
Cdd:cd00340   92 AKIDVNGENAHPLYKYLKEEApgllgKDIKWNFTKFLVDRDGEVVKRFAPTTDP--EELEKDI 152
GSHPx pfam00255
Glutathione peroxidase;
33-134 4.12e-24

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 90.87  E-value: 4.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498   33 PKLRAKESIDLCQrFAGKPLVIVNTASFCGFAPQFKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYG 111
Cdd:pfam00255   6 AKDIDGEPVPFDQ-YRGKVVLIVNVASKCGLTPQYTQLEELQERYKDRGLVILGFPCNQFgKQEPGSNEEIKYFCPGGYG 84

                          90       100
                  ....*....|....*....|...
gi 516456498  112 VTFTMTEPQAVKGPDAVHLFKVL 134
Cdd:pfam00255  85 VTFPLFSKIEVNGEKAHPVYKFL 107
PTZ00256 PTZ00256
glutathione peroxidase; Provisional
 50-179 2.22e-21

glutathione peroxidase; Provisional


Pssm-ID: 173495 [Multi-domain]  Cd Length: 183  Bit Score: 85.97  E-value: 2.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  50 KPLVIVNTASFCGFAPQ-FKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYGVTFTMTEPQAVKGPDA 127
Cdd:PTZ00256  42 KAIIVVNVACKCGLTSDhYTQLVELYKQYKSQGLEILAFPCNQFmEQEPWDEPEIKEYVQKKFNVDFPLFQKIEVNGENT 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516456498 128 VHLFKVLAQQSSAPK----------WNFYKYVVDRQGKVIANFSSLTKPDspDLLKAVEAAL 179
Cdd:PTZ00256 122 HEIYKYLRRNSELFQnntnearqipWNFAKFLIDGQGKVVKYFSPKVNPN--EMIQDIEKLL 181
PLN02412 PLN02412
probable glutathione peroxidase
 47-166 3.94e-21

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 85.04  E-value: 3.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  47 FAGKPLVIVNTASFCGFA-PQFKGLEALYQRYKDQGLEVIGVPSDDFK-QEAKTGEETAKVCYVNYGVTFTMTEPQAVKG 124
Cdd:PLN02412  27 YKGKVLLIVNVASKCGLTdSNYKELNVLYEKYKEQGFEILAFPCNQFLgQEPGSNEEIQQTVCTRFKAEFPIFDKVDVNG 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 516456498 125 PDAVHLFKVLAQQS-----SAPKWNFYKYVVDRQGKVIANFSSLTKP 166
Cdd:PLN02412 107 KNTAPLYKYLKAEKgglfgDAIKWNFTKFLVSKEGKVVQRYAPTTSP 153
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 47-182 1.36e-20

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 84.52  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  47 FAGKPLVIVNTASFCGFAPQ-FKGLEALYQRYKDQGLEVIGVPSDDF-KQEAktgEETAKVCYVN--YGVTFTMTEPQAV 122
Cdd:PTZ00056  37 LKNKVLMITNSASKCGLTKKhVDQMNRLHSVFNPLGLEILAFPTSQFlNQEF---PNTKDIRKFNdkNKIKYNFFEPIEV 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498 123 KGPDAVHLFKVLAQ----------QSSAPKWNFYKYVVDRQGKVIANFSSLTKPDspDLLKAVEAALASK 182
Cdd:PTZ00056 114 NGENTHELFKFLKAncdsmhdengTLKAIGWNFGKFLVNKSGNVVAYFSPRTEPL--ELEKKIAELLGVK 181
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 45-157 1.31e-19

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: 80.65  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498   45 QRFAGKPLVIVNTASFCGFAPQ-FKGLEALYQRYKDQGLEVIGVPSDDF-KQEAKTGEETAKVCYVNYGVTFTMTEPQAV 122
Cdd:TIGR02540  18 EKYRGKVSLVVNVASECGFTDQnYRALQELHRELGPSHFNVLAFPCNQFgESEPDSSKEIESFARRNYGVTFPMFSKIKI 97

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 516456498  123 KGPDAVHLFKVLAQQSSA-PKWNFYKYVVDRQGKVI 157
Cdd:TIGR02540  98 LGSEAEPAFRFLVDSSKKePRWNFWKYLVNPEGQVV 133
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 46-166 4.13e-18

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 78.79  E-value: 4.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  46 RFAGKPLVIVNTASFCGF-APQFKGLEALYQRYKDQGLEVIGVPSDDFK-QEAKTGEETAKVCYVNYGVTFTMTEPQAVK 123
Cdd:PLN02399  96 KFKGKVLLIVNVASKCGLtSSNYSELSHLYEKYKTQGFEILAFPCNQFGgQEPGSNPEIKQFACTRFKAEFPIFDKVDVN 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 516456498 124 GPDAVHLFKVLaqQSSAP-------KWNFYKYVVDRQGKVIANFSSLTKP 166
Cdd:PLN02399 176 GPSTAPVYQFL--KSNAGgflgdliKWNFEKFLVDKNGKVVERYPPTTSP 223
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
47-183 3.31e-09

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 52.56  E-value: 3.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  47 FAGKPLVIVNTASFCGFA-PQFKGLEALYQRYKDQGLEVIGVPSDDFKQEAKTGEEtakvcyvnYGVTFTMT--EPQAVk 123
Cdd:COG1225   19 LRGKPVVLYFYATWCPGCtAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEK--------YGLPFPLLsdPDGEV- 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498 124 gpdaVHLFKVLAQQSSapkwnfykYVVDRQGKVIANFSSLTKPDsPDLLKAVEAALASKP 183
Cdd:COG1225   90 ----AKAYGVRGTPTT--------FLIDPDGKIRYVWVGPVDPR-PHLEEVLEALLAELK 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 26-181 1.71e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 45.45  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  26 PLLEGQLPKLRAKEsIDLcQRFAGKPLVIVNTASFCG----FAPQfkgLEALYQRYKdqGLEVIGVPSDDFKQEAKTGEE 101
Cdd:COG0526    7 PAPDFTLTDLDGKP-LSL-ADLKGKPVLVNFWATWCPpcraEMPV---LKELAEEYG--GVVFVGVDVDENPEAVKAFLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498 102 TakvcyvnYGVTFTMTEPQAVKGPDAvhlFKVlaqqSSAPkwnfYKYVVDRQGKVIANFSSltKPDSPDLLKAVEAALAS 181
Cdd:COG0526   80 E-------LGLPYPVLLDPDGELAKA---YGV----RGIP----TTVLIDKDGKIVARHVG--PLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 39-158 1.59e-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: 42.22  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  39 ESIDLcQRFAGKPLVIVNTASFCGF----APQfkgLEALYQRYKDQGLEVIGVPSDDFKQEAktGEETAKvcyvNYGVTF 114
Cdd:cd02966   10 KPVSL-SDLKGKVVLVNFWASWCPPcraeMPE---LEALAKEYKDDGVEVVGVNVDDDDPAA--VKAFLK----KYGITF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 516456498 115 tmtePQAVKGPDAVH-LFKVLAQQSSapkwnfykYVVDRQGKVIA 158
Cdd:cd02966   80 ----PVLLDPDGELAkAYGVRGLPTT--------FLIDRDGRIRA 112
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 70-158 5.85e-05

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: 40.75  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498  70 LEALYQRYKDQGLEVIGVPSDDFKQEAktgeetakvcyvnygvtftmtEPQAVKgpDAVHLFKV---LAQQSSAPKWNFY 146
Cdd:cd03012   45 LTDLEQKYKDDGLVVIGVHSPEFAFER---------------------DLANVK--SAVLRYGItypVANDNDYATWRAY 101

                         90
                 ....*....|....*....
gi 516456498 147 K-------YVVDRQGKVIA 158
Cdd:cd03012  102 GnqywpalYLIDPTGNVRH 120
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 47-158 4.35e-04

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: 38.36  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456498   47 FAGKPLVIVNTAS-FCGFAP-QFKGLEALYQRYKDQGLEVIGVPSDDFKQEAKTGEEtakvcyvnYGVTFTMtepqaVKG 124
Cdd:pfam00578  23 YRGKWVVLFFYPAdWTPVCTtELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK--------YGLPFPL-----LSD 89

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 516456498  125 PD--AVHLFKVLAQQSSAPKWNFykYVVDRQGKVIA 158
Cdd:pfam00578  90 PDgeVARAYGVLNEEEGGALRAT--FVIDPDGKVRY 123
 
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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