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Conserved domains on  [gi|13186328|gb|AAK15374|]
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alkyl hydroperoxide reductase small subunit [Candidatus Carsonella ruddii]

Protein Classification

peroxiredoxin( domain architecture ID 10122432)

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

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0008379
PubMed:  15518547|12517450|10049365|15558583
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 2-167 1.71e-71

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: 213.14  E-value: 1.71e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   2 LNTRIKPFKNISYYK-KKFYEIKEIDLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNW 80
Cdd:cd03015   1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  81 IENE-----LKFINFPFISDFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFIN 155
Cdd:cd03015  81 RNTPrkeggLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|..
gi 13186328 156 TNeNKLCPYSWN 167
Cdd:cd03015 161 EH-GEVCPANWK 171
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 2-167 1.71e-71

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: 213.14  E-value: 1.71e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   2 LNTRIKPFKNISYYK-KKFYEIKEIDLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNW 80
Cdd:cd03015   1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  81 IENE-----LKFINFPFISDFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFIN 155
Cdd:cd03015  81 RNTPrkeggLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|..
gi 13186328 156 TNeNKLCPYSWN 167
Cdd:cd03015 161 EH-GEVCPANWK 171
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-173 1.25e-51

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 163.71  E-value: 1.25e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   1 MLNTRIKPFKNISYYKKKFYEIKEIDLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNW 80
Cdd:COG0450   4 LIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  81 IENE-----LKFINFPFISDFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFIN 155
Cdd:COG0450  84 HETIkekggIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170
                ....*....|....*...
gi 13186328 156 TNeNKLCPYSWNNDSKSI 173
Cdd:COG0450 164 KH-GEVCPANWKPGDKVI 180
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-173 1.90e-44

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 145.13  E-value: 1.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328    1 MLNTRIKPFKNISYYKKKFYEIKEIDLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNW 80
Cdd:PRK10382   3 LINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   81 --IENELKFINFPFISDFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFINTNE 158
Cdd:PRK10382  83 hsSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHP 162

                        170
                 ....*....|....*
gi 13186328  159 NKLCPYSWNNDSKSI 173
Cdd:PRK10382 163 GEVCPAKWKEGEATL 177
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 26-130 2.21e-29

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: 104.61  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328    26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELkfINFPFISDFNHKISNNFN 105
Cdd:pfam00578  22 DYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYG--LPFPLLSDPDGEVARAYG 99

                          90       100
                  ....*....|....*....|....*
gi 13186328   106 ILNKKDGNCLRSTIIIDKNLIIKYI 130
Cdd:pfam00578 100 VLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 2-167 1.71e-71

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: 213.14  E-value: 1.71e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   2 LNTRIKPFKNISYYK-KKFYEIKEIDLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNW 80
Cdd:cd03015   1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  81 IENE-----LKFINFPFISDFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFIN 155
Cdd:cd03015  81 RNTPrkeggLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|..
gi 13186328 156 TNeNKLCPYSWN 167
Cdd:cd03015 161 EH-GEVCPANWK 171
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-173 1.25e-51

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 163.71  E-value: 1.25e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   1 MLNTRIKPFKNISYYKKKFYEIKEIDLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNW 80
Cdd:COG0450   4 LIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  81 IENE-----LKFINFPFISDFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFIN 155
Cdd:COG0450  84 HETIkekggIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVD 163

                       170
                ....*....|....*...
gi 13186328 156 TNeNKLCPYSWNNDSKSI 173
Cdd:COG0450 164 KH-GEVCPANWKPGDKVI 180
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-173 1.90e-44

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 145.13  E-value: 1.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328    1 MLNTRIKPFKNISYYKKKFYEIKEIDLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNW 80
Cdd:PRK10382   3 LINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   81 --IENELKFINFPFISDFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFINTNE 158
Cdd:PRK10382  83 hsSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHP 162

                        170
                 ....*....|....*
gi 13186328  159 NKLCPYSWNNDSKSI 173
Cdd:PRK10382 163 GEVCPAKWKEGEATL 177
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 26-145 4.48e-40

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: 132.29  E-value: 4.48e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELKfINFPFISDFNHKISNNFN 105
Cdd:cd02971  19 DFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEGG-LNFPLLSDPDGEFAKAYG 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 13186328 106 ILNKKD---GNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEIL 145
Cdd:cd02971  98 VLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 26-130 2.21e-29

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: 104.61  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328    26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELkfINFPFISDFNHKISNNFN 105
Cdd:pfam00578  22 DYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYG--LPFPLLSDPDGEVARAYG 99

                          90       100
                  ....*....|....*....|....*
gi 13186328   106 ILNKKDGNCLRSTIIIDKNLIIKYI 130
Cdd:pfam00578 100 VLNEEEGGALRATFVIDPDGKVRYI 124
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 23-174 3.01e-28

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 104.22  E-value: 3.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   23 KEIDL---KSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELK-----FINFPFIS 94
Cdd:PTZ00253  27 KKISLssyKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTLQERKkgglgTMAIPMLA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   95 DFNHKISNNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFINTNeNKLCPYSWNNDSKSIE 174
Cdd:PTZ00253 107 DKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVEKH-GEVCPANWKKGDPTMK 185
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 27-166 6.93e-27

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 101.95  E-value: 6.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   27 LKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELKF-----INFPFISDFNHKIS 101
Cdd:PTZ00137  96 FKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWKELDVRQggvspLKFPLFSDISREVS 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13186328  102 NNFNILnKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFiNTNENKLCPYSW 166
Cdd:PTZ00137 176 KSFGLL-RDEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQF-AEKTGNVCPVNW 238
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 16-173 1.11e-20

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: 84.51  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  16 KKKFYEIKeidlKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELKF----INFP 91
Cdd:cd03016  16 PIKFHDYL----GDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDIEEYtgveIPFP 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  92 FISDFNHKISNNFNILNKKDGNCL--RSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFinTNENKL-CPYSWNN 168
Cdd:cd03016  92 IIADPDREVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQL--TDKHKVaTPANWKP 169


                ....*
gi 13186328 169 DSKSI 173
Cdd:cd03016 170 GDDVI 174
PRK15000 PRK15000
peroxiredoxin C;
33-166 1.35e-20

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 84.34  E-value: 1.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   33 VFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWI-----ENELKFINFPFISDFNHKISNNFNIL 107
Cdd:PRK15000  38 VLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRntpvdKGGIGPVKYAMVADVKREIQKAYGIE 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13186328  108 NKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFiNTNENKLCPYSW 166
Cdd:PRK15000 118 HPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQF-HEEHGDVCPAQW 175
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 26-174 6.51e-20

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 82.59  E-value: 6.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIEN-ELKF---INFPFISDFNHKIS 101
Cdd:PRK13190  24 KYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLRDiEERFgikIPFPVIADIDKELA 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13186328  102 NNFNILNKKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFiNTNENKLCPYSWNNDSKSIE 174
Cdd:PRK13190 104 REYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQV-NWKRKVATPANWQPGQEGIV 175
PRK13599 PRK13599
peroxiredoxin;
26-169 5.07e-19

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 80.53  E-value: 5.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIE----NELKFINFPFISDFNHKIS 101
Cdd:PRK13599  25 DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEwikdNTNIAIPFPVIADDLGKVS 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13186328  102 NNFNILNKKDG-NCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFINTNENKLcPYSWNND 169
Cdd:PRK13599 105 NQLGMIHPGKGtNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVAL-PEKWPNN 172
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 33-146 2.78e-18

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: 76.93  E-value: 2.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  33 VFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELkfINFPFISDFNHK--ISNNFNILNKK 110
Cdd:cd03018  32 VLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWAEENG--LTFPLLSDFWPHgeVAKAYGVFDED 109

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13186328 111 DGNCLRSTIIIDKNLIIKYINIVDDSIGRS---IDEILK 146
Cdd:cd03018 110 LGVAERAVFVIDRDGIIRYAWVSDDGEPRDlpdYDEALD 148
PRK13189 PRK13189
peroxiredoxin; Provisional
 26-168 6.69e-18

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 77.33  E-value: 6.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISND---SHFVQKNWIENELKF-INFPFISDFNHKIS 101
Cdd:PRK13189  32 DYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDqvfSHIKWVEWIKEKLGVeIEFPIIADDRGEIA 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13186328  102 NNFNILN-KKDGNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQfINTNENKLCPYSWNN 168
Cdd:PRK13189 112 KKLGMISpGKGTNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQ-TSDEKGVATPANWPP 178
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
26-146 5.05e-17

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 72.98  E-value: 5.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  26 DLKSNWNVFFFYPySYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIEnELKFiNFPFISDFNHKISNNFN 105
Cdd:COG1225  18 DLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAE-KYGL-PFPLLSDPDGEVAKAYG 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13186328 106 IlnkkdgNCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILK 146
Cdd:COG1225  95 V------RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 26-169 7.76e-17

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 74.50  E-value: 7.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISND---SHFVQKNWIENELKF-INFPFISDFNHKIS 101
Cdd:PRK13191  30 DYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDsniSHIEWVMWIEKNLKVeVPFPIIADPMGNVA 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13186328  102 NNFNILNKKDG-NCLRSTIIIDKNLIIKYINIVDDSIGRSIDEILKNIKMLQFINTNENkLCPYSWNND 169
Cdd:PRK13191 110 KRLGMIHAESStATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGV-VTPANWPNN 177
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 26-130 1.90e-14

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: 66.42  E-value: 1.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIEnelKF-INFPFISDFNHKISNNF 104
Cdd:cd03017  20 DLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE---KYgLPFPLLSDPDGKLAKAY 96

                        90       100
                ....*....|....*....|....*....
gi 13186328 105 NIL---NKKDGNCLRSTIIIDKNLIIKYI 130
Cdd:cd03017  97 GVWgekKKKYMGIERSTFLIDPDGKIVKV 125
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 33-136 1.06e-07

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 48.91  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328    33 VFFFYPysySFICP------LELKNISNKIKEfKNLNTKIYAISNDSHFVQKNWIENELKFinfPFISDFNHKISNNFNI 106
Cdd:pfam08534  32 VLNFWP---GAFCPtcsaehPYLEKLNELYKE-KGVDVVAVNSDNDAFFVKRFWGKEGLPF---PFLSDGNAAFTKALGL 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 13186328   107 ---LNKKDGNCLRSTIIIDKNLIIKYINIVDDS 136
Cdd:pfam08534 105 pieEDASAGLRSPRYAVIDEDGKVVYLFVGPEP 137
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 44-135 3.61e-07

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: 47.19  E-value: 3.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328  44 ICPLELKNISNKIKEFKNlnTKIYAISNDSHFVQKNWIENE-LKfiNFPFISDF-NHKISNNFNILNKKDGNCLRSTIII 121
Cdd:cd03014  41 VCATQTKRFNKEAAKLDN--TVVLTISADLPFAQKRWCGAEgVD--NVTTLSDFrDHSFGKAYGVLIKDLGLLARAVFVI 116

                        90
                ....*....|....
gi 13186328 122 DKNLIIKYINIVDD 135
Cdd:cd03014 117 DENGKVIYVELVPE 130
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 26-110 2.12e-03

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 36.84  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186328   26 DLKSNWNVFFFYPYSYSFICPLELKNISNKIKEFKNLNTKIYAISNDSHFVQKNWIENELkfINFPFISDFNHKISNNFN 105
Cdd:PRK09437  27 DFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAEKEL--LNFTLLSDEDHQVAEQFG 104


                 ....*
gi 13186328  106 ILNKK 110
Cdd:PRK09437 105 VWGEK 109
 
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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