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Conserved domains on  [gi|15598725|ref|NP_252219|]
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peroxidase [Pseudomonas aeruginosa PAO1]

Protein Classification

peroxiredoxin( domain architecture ID 11418685)

peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, is a thiol-specific antioxidant protein that protects cells against reactive oxygen species

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-198 6.82e-116

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


:

Pssm-ID: 440219  Cd Length: 196  Bit Score: 327.42  E-value: 6.82e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   1 MSVLVGKKAPDFNVAAVLGNGeiVESFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSH 80
Cdd:COG0450   1 MMPLIGDKAPDFTAEATHGGE--FKKISLSD-YKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  81 FTHNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVES-DGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVD 159
Cdd:COG0450  78 FSHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHpEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVD 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15598725 160 ALQFHEEHGEVCPANWKKGDKGMTASPEGVAKYLAENAS 198
Cdd:COG0450 158 ALQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFPE 196
 
Name Accession Description Interval E-value
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-198 6.82e-116

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 327.42  E-value: 6.82e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   1 MSVLVGKKAPDFNVAAVLGNGeiVESFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSH 80
Cdd:COG0450   1 MMPLIGDKAPDFTAEATHGGE--FKKISLSD-YKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  81 FTHNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVES-DGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVD 159
Cdd:COG0450  78 FSHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHpEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVD 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15598725 160 ALQFHEEHGEVCPANWKKGDKGMTASPEGVAKYLAENAS 198
Cdd:COG0450 158 ALQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFPE 196
PRK15000 PRK15000
peroxiredoxin C;
3-200 1.74e-105

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 301.59  E-value: 1.74e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    3 VLVGKKAPDFNVAAVLGNGEIVESFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFT 82
Cdd:PRK15000   2 VLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   83 HNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVE-SDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDAL 161
Cdd:PRK15000  82 HNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEhPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDAL 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15598725  162 QFHEEHGEVCPANWKKGDKGMTASPEGVAKYLAENASKL 200
Cdd:PRK15000 162 QFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 5-178 1.60e-102

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 292.87  E-value: 1.60e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   5 VGKKAPDFNVAAVLGNGEIVEsFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHN 84
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKE-ISLSD-YKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  85 AWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVES-DGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQF 163
Cdd:cd03015  79 AWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDeEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQF 158

                       170
                ....*....|....*
gi 15598725 164 HEEHGEVCPANWKKG 178
Cdd:cd03015 159 VEEHGEVCPANWKPG 173
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 4-191 1.39e-55

peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 211789  Cd Length: 187  Bit Score: 174.51  E-value: 1.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725     4 LVGKKAPDFNVAAVLgNGEIVEsfTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTH 83
Cdd:TIGR03137   3 LINTEIKPFKATAYH-NGEFVE--VTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    84 NAWRNTpvdKGGIGAVKYTLAADTKHEIAKAYDVESDG-GVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQ 162
Cdd:TIGR03137  80 KAWHDT---SEAIGKITYPMLGDPTGVLTRNFGVLIEEaGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQ 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 15598725   163 FHEEH-GEVCPANWKKGDKGMTASPEGVAK 191
Cdd:TIGR03137 157 YVAAHpGEVCPAKWKEGAETLKPSLDLVGK 186
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-191 1.64e-47

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 155.20  E-value: 1.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    1 MSVLVGKKAPDFNVAAVLGNGeiVESFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSH 80
Cdd:NF040737  34 MMIKVGKKAPDFTAPAYYKGG--FTNVKLSD-YLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   81 FTHNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDV-ESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVD 159
Cdd:NF040737 111 FVHKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVyDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQ 190

                        170       180       190
                 ....*....|....*....|....*....|....
gi 15598725  160 ALQFHEEHG--EVCPANWKKGDKGMTASPEGVAK 191
Cdd:NF040737 191 AFQHVRETKgtEATPSGWQPGKPTLKPGPDLVGK 224
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-138 9.55e-42

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: 136.97  E-value: 9.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725     5 VGKKAPDFNVAAVLGNgeiveSFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHN 84
Cdd:pfam00578   1 VGDKAPDFELPDGDGG-----TVSLSD-YRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598725    85 AWRNTPVdkggigaVKYTLAADTKHEIAKAYDVE-SDGGVAFRGAFLIDKEGVVR 138
Cdd:pfam00578  75 AFAEKYG-------LPFPLLSDPDGEVARAYGVLnEEEGGALRATFVIDPDGKVR 122
 
Name Accession Description Interval E-value
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-198 6.82e-116

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 327.42  E-value: 6.82e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   1 MSVLVGKKAPDFNVAAVLGNGeiVESFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSH 80
Cdd:COG0450   1 MMPLIGDKAPDFTAEATHGGE--FKKISLSD-YKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  81 FTHNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVES-DGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVD 159
Cdd:COG0450  78 FSHKAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHpEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVD 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15598725 160 ALQFHEEHGEVCPANWKKGDKGMTASPEGVAKYLAENAS 198
Cdd:COG0450 158 ALQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFPE 196
PRK15000 PRK15000
peroxiredoxin C;
3-200 1.74e-105

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 301.59  E-value: 1.74e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    3 VLVGKKAPDFNVAAVLGNGEIVESFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFT 82
Cdd:PRK15000   2 VLVTRQAPDFTAAAVLGSGEIVDKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   83 HNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVE-SDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDAL 161
Cdd:PRK15000  82 HNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEhPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDAL 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15598725  162 QFHEEHGEVCPANWKKGDKGMTASPEGVAKYLAENASKL 200
Cdd:PRK15000 162 QFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAENISSL 200
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 5-178 1.60e-102

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 292.87  E-value: 1.60e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   5 VGKKAPDFNVAAVLGNGEIVEsFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHN 84
Cdd:cd03015   1 VGKKAPDFKATAVVPNGEFKE-ISLSD-YKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  85 AWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVES-DGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQF 163
Cdd:cd03015  79 AWRNTPRKEGGLGKINFPLLADPKKKISRDYGVLDeEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQF 158

                       170
                ....*....|....*
gi 15598725 164 HEEHGEVCPANWKKG 178
Cdd:cd03015 159 VEEHGEVCPANWKPG 173
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 2-193 2.82e-70

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 214.43  E-value: 2.82e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    2 SVLVGKKAPDFNVAAVLgNGEIVEsFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHF 81
Cdd:PTZ00137  67 SSLVGKLMPSFKGTALL-NDDLVQ-FNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPF 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   82 THNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDAL 161
Cdd:PTZ00137 145 SHKAWKELDVRQGGVSPLKFPLFSDISREVSKSFGLLRDEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAV 224

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15598725  162 QFHEEHGEVCPANWKKGDKGMTASPEGVAKYL 193
Cdd:PTZ00137 225 QFAEKTGNVCPVNWKQGDQAMKPDSQSVKQYL 256
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 9-192 7.58e-68

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 205.91  E-value: 7.58e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    9 APDFNVAAVLGNGEIvESFTLSeAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHNAWRN 88
Cdd:PTZ00253  12 APSFEEVALMPNGSF-KKISLS-SYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   89 TPVDKGGIGAVKYTLAADTKHEIAKAYDV-ESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQFHEEH 167
Cdd:PTZ00253  90 QERKKGGLGTMAIPMLADKTKSIARSYGVlEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVEKH 169

                        170       180
                 ....*....|....*....|....*
gi 15598725  168 GEVCPANWKKGDKGMTASPEGVAKY 192
Cdd:PTZ00253 170 GEVCPANWKKGDPTMKPDPNKSKEG 194
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 4-191 1.39e-55

peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(TIGR03140). Usually these are found as an apparent operon. The gene has been characterized in Bacteroides fragilis, where it is important in oxidative stress defense. This gene contains two invariant cysteine residues, one near the N-terminus and one near the C-terminus, each followed immediately by a proline residue. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 211789  Cd Length: 187  Bit Score: 174.51  E-value: 1.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725     4 LVGKKAPDFNVAAVLgNGEIVEsfTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTH 83
Cdd:TIGR03137   3 LINTEIKPFKATAYH-NGEFVE--VTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    84 NAWRNTpvdKGGIGAVKYTLAADTKHEIAKAYDVESDG-GVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQ 162
Cdd:TIGR03137  80 KAWHDT---SEAIGKITYPMLGDPTGVLTRNFGVLIEEaGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQ 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 15598725   163 FHEEH-GEVCPANWKKGDKGMTASPEGVAK 191
Cdd:TIGR03137 157 YVAAHpGEVCPAKWKEGAETLKPSLDLVGK 186
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 8-155 5.49e-50

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 158.48  E-value: 5.49e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   8 KAPDFNVAAVLGngeivESFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHNAWR 87
Cdd:cd02971   1 KAPDFTLPATDG-----GEVSLSD-FKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598725  88 NTpvdkggIGAVKYTLAADTKHEIAKAYDVESD----GGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELL 155
Cdd:cd02971  75 EK------EGGLNFPLLSDPDGEFAKAYGVLIEksagGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
1-191 1.64e-47

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 155.20  E-value: 1.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    1 MSVLVGKKAPDFNVAAVLGNGeiVESFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSH 80
Cdd:NF040737  34 MMIKVGKKAPDFTAPAYYKGG--FTNVKLSD-YLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   81 FTHNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDV-ESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVD 159
Cdd:NF040737 111 FVHKMWNDEELSKMVTGGVPFPMLSDGGGKIGKAYGVyDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQ 190

                        170       180       190
                 ....*....|....*....|....*....|....
gi 15598725  160 ALQFHEEHG--EVCPANWKKGDKGMTASPEGVAK 191
Cdd:NF040737 191 AFQHVRETKgtEATPSGWQPGKPTLKPGPDLVGK 224
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 6-180 1.89e-45

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 149.23  E-value: 1.89e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   6 GKKAPDFNVAAVLGNgeivesFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHNA 85
Cdd:cd03016   2 GDTAPNFEADTTHGP------IKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  86 WRNTPVDKGGIgAVKYTLAADTKHEIAKAY---DVESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQ 162
Cdd:cd03016  76 WIEDIEEYTGV-EIPFPIIADPDREVAKLLgmiDPDAGSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQ 154

                       170
                ....*....|....*...
gi 15598725 163 FHEEHGEVCPANWKKGDK 180
Cdd:cd03016 155 LTDKHKVATPANWKPGDD 172
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-191 4.67e-45

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 147.83  E-value: 4.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    1 MSVLVGKKAPDFNVAavLGNGEIVEsfTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSH 80
Cdd:PRK10382   1 MSLINTKIKPFKNQA--FKNGEFIE--VTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   81 FTHNAWRNTpvdKGGIGAVKYTLAADTKHEIAKAYDV-ESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVD 159
Cdd:PRK10382  77 FTHKAWHSS---SETIAKIKYAMIGDPTGALTRNFDNmREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIK 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15598725  160 ALQFHEEH-GEVCPANWKKGDKGMTASPEGVAK 191
Cdd:PRK10382 154 AAQYVASHpGEVCPAKWKEGEATLAPSLDLVGK 186
PRK13189 PRK13189
peroxiredoxin; Provisional
 3-179 4.67e-43

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 143.58  E-value: 4.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    3 VLVGKKAPDFNVAAVLGngeiveSFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFT 82
Cdd:PRK13189   9 PLIGDKFPEFEVKTTHG------PIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   83 HNAWRNTPVDKGGIgAVKYTLAADTKHEIAKAYDVESDGG--VAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDA 160
Cdd:PRK13189  83 HIKWVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKgtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKA 161

                        170
                 ....*....|....*....
gi 15598725  161 LQFHEEHGEVCPANWKKGD 179
Cdd:PRK13189 162 LQTSDEKGVATPANWPPND 180
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-138 9.55e-42

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: 136.97  E-value: 9.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725     5 VGKKAPDFNVAAVLGNgeiveSFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHN 84
Cdd:pfam00578   1 VGDKAPDFELPDGDGG-----TVSLSD-YRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHK 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598725    85 AWRNTPVdkggigaVKYTLAADTKHEIAKAYDVE-SDGGVAFRGAFLIDKEGVVR 138
Cdd:pfam00578  75 AFAEKYG-------LPFPLLSDPDGEVARAYGVLnEEEGGALRATFVIDPDGKVR 122
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 3-186 2.99e-41

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 138.45  E-value: 2.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    3 VLVGKKAPDFNVAAVLGngeiveSFTLSEAiKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFT 82
Cdd:PRK13190   2 VKLGQKAPDFTVNTTKG------PIDLSKY-KGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   83 HNAWRNTPVDKGGIgAVKYTLAADTKHEIAKAYD-VESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDAL 161
Cdd:PRK13190  75 HIAWLRDIEERFGI-KIPFPVIADIDKELAREYNlIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKAL 153

                        170       180
                 ....*....|....*....|....*
gi 15598725  162 QFHEEHGEVCPANWKKGDKGMTASP 186
Cdd:PRK13190 154 QVNWKRKVATPANWQPGQEGIVPAP 178
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 3-160 5.17e-36

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 123.15  E-value: 5.17e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   3 VLVGKKAPDFNVAAVLGngeivESFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFT 82
Cdd:cd03018   1 LEVGDKAPDFELPDQNG-----QEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  83 HNAWRntpvDKGGIGavkYTLAAD--TKHEIAKAYDVE-SDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVD 159
Cdd:cd03018  76 LRAWA----EENGLT---FPLLSDfwPHGEVAKAYGVFdEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEALD 148


                .
gi 15598725 160 A 160
Cdd:cd03018 149 A 149
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 4-189 9.91e-29

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 106.47  E-value: 9.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    4 LVGKKAPDFNVAAVLGNgeivesFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTH 83
Cdd:PRK13191   8 LIGEKFPEMEVITTHGK------IKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   84 NAWRNTPVDKGGIgAVKYTLAADTKHEIAKAYDV---ESDGGVAfRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDA 160
Cdd:PRK13191  82 IEWVMWIEKNLKV-EVPFPIIADPMGNVAKRLGMihaESSTATV-RAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRA 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15598725  161 LQFHEEHGEVCPANWKK----GDKGMTASPEGV 189
Cdd:PRK13191 160 LQLVDKAGVVTPANWPNneliGDKVINPAPRTI 192
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
9-162 6.63e-26

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 96.86  E-value: 6.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   9 APDFNVAAVLGngeivESFTLSEaIKGKYGLVFFYPlDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHNAWrn 88
Cdd:COG1225   1 APDFTLPDLDG-----KTVSLSD-LRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKF-- 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598725  89 tpVDKGGIgavKYTLAADTKHEIAKAYDVesdggVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLR-LVDALQ 162
Cdd:COG1225  72 --AEKYGL---PFPLLSDPDGEVAKAYGV-----RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEaLLAELK 136
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 7-138 3.05e-24

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 92.61  E-value: 3.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   7 KKAPDFNVAAVLGngeivESFTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHNAW 86
Cdd:cd03017   1 DKAPDFTLPDQDG-----ETVSLSD-LRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKF 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598725  87 RntpvDKGGIgavKYTLAADTKHEIAKAYDVESDGGVAFRGA----FLIDKEGVVR 138
Cdd:cd03017  75 A----EKYGL---PFPLLSDPDGKLAKAYGVWGEKKKKYMGIerstFLIDPDGKIV 123
PRK13599 PRK13599
peroxiredoxin;
4-175 4.48e-23

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 91.70  E-value: 4.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    4 LVGKKAPDFNVAAVLGNGEIVESFTlseaikGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTH 83
Cdd:PRK13599   3 LLGEKFPSMEVVTTQGVKRLPEDYA------GKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   84 NAWRNTPVDKGGIgAVKYTLAADTKHEIAKAYDV--ESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDAL 161
Cdd:PRK13599  77 IKWVEWIKDNTNI-AIPFPVIADDLGKVSNQLGMihPGKGTNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKAL 155

                        170
                 ....*....|....
gi 15598725  162 QFHEEHGEVCPANW 175
Cdd:PRK13599 156 QTADQYGVALPEKW 169
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 5-138 2.28e-15

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 69.71  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725     5 VGKKAPDFNVAAVLGNGEiveSFTLSEAiKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSI--DSHFT 82
Cdd:pfam08534   2 AGDKAPDFTLPDAATDGN---TVSLSDF-KGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSdnDAFFV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    83 HNAWrntpvDKGGigaVKYTLAADTKHEIAKAYDVE----SDGGVAFRGAFLIDKEGVVR 138
Cdd:pfam08534  78 KRFW-----GKEG---LPFPFLSDGNAAFTKALGLPieedASAGLRSPRYAVIDEDGKVV 129
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 160-193 5.96e-11

C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerization of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme. The domain is associated with family AhpC-TSA, pfam00578, which carries the catalytic cysteine.


Pssm-ID: 431271  Cd Length: 40  Bit Score: 55.29  E-value: 5.96e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 15598725   160 ALQFHEEHGEVCPANWKKGDKGM---TASPE-GVAKYL 193
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIvppPATQEeAVKRYL 38
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 1-137 1.37e-08

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 51.86  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    1 MSVL-VGKKAPDFNVAAvlGNGEIVesfTLSEaIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDs 79
Cdd:PRK09437   1 MNPLkAGDIAPKFSLPD--QDGEQV---SLTD-FQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTD- 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598725   80 hfthnawrntPVDKGGIGAVK----YTLAADTKHEIAKAYDV---------ESDGgvAFRGAFLIDKEGVV 137
Cdd:PRK09437  74 ----------KPEKLSRFAEKellnFTLLSDEDHQVAEQFGVwgekkfmgkTYDG--IHRISFLIDADGKI 132
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 5-161 2.10e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.84  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   5 VGKKAPDFNVAAVLGngeivESFTLSEaIKGKYGLVFFY-----PldftfvCPSElialdhrIPEFQA-----RNVEVIG 74
Cdd:COG0526   4 VGKPAPDFTLTDLDG-----KPLSLAD-LKGKPVLVNFWatwcpP------CRAE-------MPVLKElaeeyGGVVFVG 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  75 VSIDSHftHNAWRNTPVDKGgigaVKYTLAADTKHEIAKAYDVesdggvafRGA---FLIDKEGVVRSQIVNDLplgrNM 151
Cdd:COG0526  65 VDVDEN--PEAVKAFLKELG----LPYPVLLDPDGELAKAYGV--------RGIpttVLIDKDGKIVARHVGPL----SP 126

                       170
                ....*....|
gi 15598725 152 DELLRLVDAL 161
Cdd:COG0526 127 EELEEALEKL 136
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 6-161 1.12e-05

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 43.77  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   6 GKKAPDFNVAAVLGNgeiveSFTLSEAIKGKYGLVFFypldFTFVCP------SELIALDHripEFQARNVEVIGVSIDS 79
Cdd:cd02969   1 GSPAPDFSLPDTDGK-----TYSLADFADGKALVVMF----ICNHCPyvkaieDRLNRLAK---EYGAKGVAVVAINSND 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  80 HFTHnawrntPVDkggigAVKYTLAADTKHEIAKAYDVESDGGVA--FRGA-----FLIDKEGVVR-------SQIVNDL 145
Cdd:cd02969  69 IEAY------PED-----SPENMKAKAKEHGYPFPYLLDETQEVAkaYGAActpdfFLFDPDGKLVyrgriddSRPGNDP 137

                       170
                ....*....|....*.
gi 15598725 146 PLGRNmdELLRLVDAL 161
Cdd:cd02969 138 PVTGR--DLRAALDAL 151
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 25-142 1.13e-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: 42.99  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  25 ESFTLSEAiKGKYGLVFFY-----PldftfvCPSELIALDHRIPEFQARNVEVIGVSIDShFTHNAWRNTpVDKGGIgav 99
Cdd:cd02966  10 KPVSLSDL-KGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDD-DDPAAVKAF-LKKYGI--- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598725 100 KYTLAADTKHEIAKAYdvesdGGVAFRGAFLIDKEGVVRSQIV 142
Cdd:cd02966  78 TFPVLLDPDGELAKAY-----GVRGLPTTFLIDRDGRIRARHV 115
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 5-145 3.39e-05

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 42.19  E-value: 3.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   5 VGKKAPDFNVAAVLGngeivESFTLSEAiKGKYGLVFFYP-LDfTFVCPSELIALDHRIPEFQarNVEVIGVSIDSHFTH 83
Cdd:cd03014   2 VGDKAPDFTLVTSDL-----SEVSLADF-AGKVKVISVFPsID-TPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQ 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598725  84 NAWrntpvdKGGIGAVKYTLAADTK-HEIAKAYDVE-SDGGVAFRGAFLIDKEGVVR-SQIVNDL 145
Cdd:cd03014  73 KRW------CGAEGVDNVTTLSDFRdHSFGKAYGVLiKDLGLLARAVFVIDENGKVIyVELVPEI 131
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 8-138 6.22e-05

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 41.58  E-value: 6.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   8 KAPDFNVAAVLGNgeiveSFTLSEAIKGKYGLVFFYPldfTFVCPS---ELIALDHRIPEFQARNVEVIGVSIDShfthn 84
Cdd:cd02970   1 TAPDFELPDAGGE-----TVTLSALLGEGPVVVVFYR---GFGCPFcreYLRALSKLLPELDALGVELVAVGPES----- 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598725  85 AWRNTPVDKGGigAVKYTLAADTKHEIAKAYDVESDGGVAFR------------------------GAFLIDKEGVVR 138
Cdd:cd02970  68 PEKLEAFDKGK--FLPFPVYADPDRKLYRALGLVRSLPWSNTpralwknaaigfrgndegdglqlpGVFVIGPDGTIL 143
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 25-161 1.69e-04

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 40.27  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725  25 ESFTLSEaIKGKYGLVFFyplDFTF---VCP---SELIALDHRIPEFQARNVEVIGVSIDShfthnaWRNTP------VD 92
Cdd:COG1999  11 KPVTLAD-LRGKPVLVFF---GYTScpdVCPttlANLAQVQEALGEDGGDDVQVLFISVDP------ERDTPevlkayAE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598725  93 KGGIGAVKY-TLAADTKHEIAKAYDV----ESDGGVAFR---GAFLIDKEGVVRSQIvndlPLGRNMDELLRLVDAL 161
Cdd:COG1999  81 AFGAPRWIGlTGDPEEIAALAKAFGVyyekVPDGDYTFDhsaAVYLVDPDGRLRGYY----PAGEDPEELAADLKAL 153
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
2-137 3.40e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 39.60  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725    2 SVLVGKKAPDFNVAAVlgNGEIVEsftLSEaIKGKyGlVFfypLDF--TFV--CPSELIALDHRIPEFQARNVEVIGVSI 77
Cdd:PRK03147  34 KVQVGKEAPNFVLTDL--EGKKIE---LKD-LKGK-G-VF---LNFwgTWCkpCEKEMPYMNELYPKYKEKGVEIIAVNV 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598725   78 DShfTHNAWRNTpVDKGGigaVKYTLAADTKHEIAKAYDVesdggVAFRGAFLIDKEGVV 137
Cdd:PRK03147 103 DE--TELAVKNF-VNRYG---LTFPVAIDKGRQVIDAYGV-----GPLPTTFLIDKDGKV 151
 
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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