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Conserved domains on  [gi|984740551|gb|AMC10073|]
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peroxiredoxin [Lutibacter profundi]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13189 super family cl29163
peroxiredoxin; Provisional
 5-225 8.16e-130

peroxiredoxin; Provisional


The actual alignment was detected with superfamily member PRK13189:

Pssm-ID: 237297  Cd Length: 222  Bit Score: 365.46  E-value: 8.16e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   5 QEFTSMPRIGDKAPEFKAVTTQGDINFPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYS 84
Cdd:PRK13189   3 YEEIRMPLIGDKFPEFEVKTTHGPIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  85 HIAWLRSIKEKIeykgmkNVDVKFPLIEDITMEIAKKYGMLQPNEDSTkAVRAVFFVDPKGIIRTIIYYPLSLGRNFDEL 164
Cdd:PRK13189  83 HIKWVEWIKEKL------GVEIEFPIIADDRGEIAKKLGMISPGKGTN-TVRAVFIIDPKGIIRAILYYPQEVGRNMDEI 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984740551 165 YRVLIALQAADAFDIATPADWRPG----DDVIIGPAGSCGTAKDRMEGKE--DMDCKDWYFCTKKIS 225
Cdd:PRK13189 156 LRLVKALQTSDEKGVATPANWPPNdlikDKVIVPPASSVEEAKKRLEAKEkgEYECYDWWFCYKKLE 222
 
Name Accession Description Interval E-value
PRK13189 PRK13189
peroxiredoxin; Provisional
 5-225 8.16e-130

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 365.46  E-value: 8.16e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   5 QEFTSMPRIGDKAPEFKAVTTQGDINFPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYS 84
Cdd:PRK13189   3 YEEIRMPLIGDKFPEFEVKTTHGPIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  85 HIAWLRSIKEKIeykgmkNVDVKFPLIEDITMEIAKKYGMLQPNEDSTkAVRAVFFVDPKGIIRTIIYYPLSLGRNFDEL 164
Cdd:PRK13189  83 HIKWVEWIKEKL------GVEIEFPIIADDRGEIAKKLGMISPGKGTN-TVRAVFIIDPKGIIRAILYYPQEVGRNMDEI 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984740551 165 YRVLIALQAADAFDIATPADWRPG----DDVIIGPAGSCGTAKDRMEGKE--DMDCKDWYFCTKKIS 225
Cdd:PRK13189 156 LRLVKALQTSDEKGVATPANWPPNdlikDKVIVPPASSVEEAKKRLEAKEkgEYECYDWWFCYKKLE 222
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
9-207 1.01e-105

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 303.15  E-value: 1.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   9 SMPRIGDKAPEFKAVTTQG----DINFpSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYS 84
Cdd:COG0450    1 MMPLIGDKAPDFTAEATHGgefkKISL-SDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  85 HIAWLRSIKEKieykgMKNVDVKFPLIEDITMEIAKKYGMLQPNEdsTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDEL 164
Cdd:COG0450   80 HKAWHETIKEK-----GGIVKIKFPIIADPTGKIARAYGMLHPED--GVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 984740551 165 YRVLIALQAADAFDIATPADWRPGDDVIIGPAGSCGTAKDRME 207
Cdd:COG0450  153 LRVVDALQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFP 195
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 13-223 2.90e-103

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: 297.53  E-value: 2.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  13 IGDKAPEFKAVTTQGDINFPsDYNGG-WSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWLRS 91
Cdd:cd03016    1 LGDTAPNFEADTTHGPIKFH-DYLGDsWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  92 IKEKIeykgmkNVDVKFPLIEDITMEIAKKYGMLQPNEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVLIAL 171
Cdd:cd03016   80 IEEYT------GVEIPFPIIADPDREVAKLLGMIDPDAGSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDAL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 984740551 172 QAADAFDIATPADWRPGDDVIIGPAGSCGTAKDRMegKEDMDCKDWYFCTKK 223
Cdd:cd03016  154 QLTDKHKVATPANWKPGDDVIVPPSVSDEEAKKKF--PKGYETVDWYLRFTP 203
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 13-148 3.18e-37

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: 126.57  E-value: 3.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   13 IGDKAPEFKAVTTQG-DINFpSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWLRS 91
Cdd:pfam00578   1 VGDKAPDFELPDGDGgTVSL-SDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 984740551   92 IKekieykgmknvdVKFPLIEDITMEIAKKYGMLqpNEDSTKAVRAVFFVDPKGIIR 148
Cdd:pfam00578  80 YG------------LPFPLLSDPDGEVARAYGVL--NEEEGGALRATFVIDPDGKVR 122
 
Name Accession Description Interval E-value
PRK13189 PRK13189
peroxiredoxin; Provisional
 5-225 8.16e-130

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 365.46  E-value: 8.16e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   5 QEFTSMPRIGDKAPEFKAVTTQGDINFPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYS 84
Cdd:PRK13189   3 YEEIRMPLIGDKFPEFEVKTTHGPIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  85 HIAWLRSIKEKIeykgmkNVDVKFPLIEDITMEIAKKYGMLQPNEDSTkAVRAVFFVDPKGIIRTIIYYPLSLGRNFDEL 164
Cdd:PRK13189  83 HIKWVEWIKEKL------GVEIEFPIIADDRGEIAKKLGMISPGKGTN-TVRAVFIIDPKGIIRAILYYPQEVGRNMDEI 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984740551 165 YRVLIALQAADAFDIATPADWRPG----DDVIIGPAGSCGTAKDRMEGKE--DMDCKDWYFCTKKIS 225
Cdd:PRK13189 156 LRLVKALQTSDEKGVATPANWPPNdlikDKVIVPPASSVEEAKKRLEAKEkgEYECYDWWFCYKKLE 222
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
9-207 1.01e-105

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 303.15  E-value: 1.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   9 SMPRIGDKAPEFKAVTTQG----DINFpSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYS 84
Cdd:COG0450    1 MMPLIGDKAPDFTAEATHGgefkKISL-SDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  85 HIAWLRSIKEKieykgMKNVDVKFPLIEDITMEIAKKYGMLQPNEdsTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDEL 164
Cdd:COG0450   80 HKAWHETIKEK-----GGIVKIKFPIIADPTGKIARAYGMLHPED--GVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 984740551 165 YRVLIALQAADAFDIATPADWRPGDDVIIGPAGSCGTAKDRME 207
Cdd:COG0450  153 LRVVDALQFVDKHGEVCPANWKPGDKVIIPPPDLVGKALERFP 195
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 13-223 2.90e-103

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: 297.53  E-value: 2.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  13 IGDKAPEFKAVTTQGDINFPsDYNGG-WSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWLRS 91
Cdd:cd03016    1 LGDTAPNFEADTTHGPIKFH-DYLGDsWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  92 IKEKIeykgmkNVDVKFPLIEDITMEIAKKYGMLQPNEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVLIAL 171
Cdd:cd03016   80 IEEYT------GVEIPFPIIADPDREVAKLLGMIDPDAGSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDAL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 984740551 172 QAADAFDIATPADWRPGDDVIIGPAGSCGTAKDRMegKEDMDCKDWYFCTKK 223
Cdd:cd03016  154 QLTDKHKVATPANWKPGDDVIVPPSVSDEEAKKKF--PKGYETVDWYLRFTP 203
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 10-223 3.15e-70

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 213.56  E-value: 3.15e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  10 MPRIGDKAPEFKAVTTQGDINFpSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWL 89
Cdd:PRK13190   1 PVKLGQKAPDFTVNTTKGPIDL-SKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  90 RSIKEKIeykgmkNVDVKFPLIEDITMEIAKKYGMLqpNEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVLI 169
Cdd:PRK13190  80 RDIEERF------GIKIPFPVIADIDKELAREYNLI--DENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITK 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 984740551 170 ALQAADAFDIATPADWRPGDDVIIGPAGSCGTAKDRMegkEDMDCKDWYFCTKK 223
Cdd:PRK13190 152 ALQVNWKRKVATPANWQPGQEGIVPAPSTLDEAEMRI---KEPGAKTWYLKFKK 202
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 10-227 1.44e-65

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 202.38  E-value: 1.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  10 MPRIGDKAPEFKAVTTQGDINFPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWL 89
Cdd:PRK13191   6 IPLIGEKFPEMEVITTHGKIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  90 RSIKEKIEykgmknVDVKFPLIEDITMEIAKKYGMLQPnEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVLI 169
Cdd:PRK13191  86 MWIEKNLK------VEVPFPIIADPMGNVAKRLGMIHA-ESSTATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984740551 170 ALQAADAFDIATPADWrP-----GDDVIIGPAGSCGTAKDRMEgkedmDCKDWYFCTKKISKE 227
Cdd:PRK13191 159 ALQLVDKAGVVTPANW-PnneliGDKVINPAPRTIKDAKMRLG-----QPFDWWFTYKEVKTT 215
PRK13599 PRK13599
peroxiredoxin;
10-224 1.18e-59

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 187.23  E-value: 1.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  10 MPRIGDKAPEFKAVTTQGDINFPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWL 89
Cdd:PRK13599   1 MKLLGEKFPSMEVVTTQGVKRLPEDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  90 RSIKEKieykgmKNVDVKFPLIEDITMEIAKKYGMLQPNEdSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVLI 169
Cdd:PRK13599  81 EWIKDN------TNIAIPFPVIADDLGKVSNQLGMIHPGK-GTNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALK 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 984740551 170 ALQAADAFDIATPADWRPG----DDVIIGPAGSCGTAKDRME--GKEDMDCKDWYFCTKKI 224
Cdd:PRK13599 154 ALQTADQYGVALPEKWPNNylikDHVIVPPSTDEASANERKEkiKSKEIEAFDWWFVHKPL 214
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 13-188 3.45e-50

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: 161.52  E-value: 3.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  13 IGDKAPEFKAVTTQGDINFP----SDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAW 88
Cdd:cd03015    1 VGKKAPDFKATAVVPNGEFKeislSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  89 LRSIKEKIEYKgmknvDVKFPLIEDITMEIAKKYGMLqpNEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVL 168
Cdd:cd03015   81 RNTPRKEGGLG-----KINFPLLADPKKKISRDYGVL--DEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVL 153

                        170       180
                 ....*....|....*....|
gi 984740551 169 IALQAADAFDIATPADWRPG 188
Cdd:cd03015  154 DALQFVEEHGEVCPANWKPG 173
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 16-164 6.22e-46

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: 149.62  E-value: 6.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  16 KAPEFKAVTTQG-DINFpSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWlrsiKE 94
Cdd:cd02971    1 KAPDFTLPATDGgEVSL-SDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAW----AE 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 984740551  95 KIEykgmknvDVKFPLIEDITMEIAKKYGMLQPNED-STKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDEL 164
Cdd:cd02971   76 KEG-------GLNFPLLSDPDGEFAKAYGVLIEKSAgGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEEL 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 13-148 3.18e-37

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: 126.57  E-value: 3.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   13 IGDKAPEFKAVTTQG-DINFpSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWLRS 91
Cdd:pfam00578   1 VGDKAPDFELPDGDGgTVSL-SDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 984740551   92 IKekieykgmknvdVKFPLIEDITMEIAKKYGMLqpNEDSTKAVRAVFFVDPKGIIR 148
Cdd:pfam00578  80 YG------------LPFPLLSDPDGEVARAYGVL--NEEEGGALRATFVIDPDGKVR 122
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 12-189 4.36e-33

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 118.47  E-value: 4.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  12 RIGDKAPEFKAVTTQGDINFP----SDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIA 87
Cdd:PTZ00253   7 KINHPAPSFEEVALMPNGSFKkislSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  88 WLRSIKEKieyKGMKNVDVkfPLIEDITMEIAKKYGMLQpnEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRV 167
Cdd:PTZ00253  87 WTLQERKK---GGLGTMAI--PMLADKTKSIARSYGVLE--EEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRL 159

                        170       180
                 ....*....|....*....|..
gi 984740551 168 LIALQAADAFDIATPADWRPGD 189
Cdd:PTZ00253 160 LEAFQFVEKHGEVCPANWKKGD 181
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 13-189 6.68e-29

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 109.27  E-value: 6.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  13 IGDKAPEFKAVTTQGD--INF-PSDY-NGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAW 88
Cdd:PTZ00137  70 VGKLMPSFKGTALLNDdlVQFnSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAW 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  89 LRSIKEKIEYKGMknvdvKFPLIEDITMEIAKKYGMLQpneDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVL 168
Cdd:PTZ00137 150 KELDVRQGGVSPL-----KFPLFSDISREVSKSFGLLR---DEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLF 221

                        170       180
                 ....*....|....*....|.
gi 984740551 169 IALQAADAFDIATPADWRPGD 189
Cdd:PTZ00137 222 DAVQFAEKTGNVCPVNWKQGD 242
PRK15000 PRK15000
peroxiredoxin C;
10-190 9.70e-28

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 104.76  E-value: 9.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  10 MPRIGDKAPEFKAVTTQGD------INFPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLY 83
Cdd:PRK15000   1 MVLVTRQAPDFTAAAVLGSgeivdkFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  84 SHIAWLRSikeKIEYKGMKnvDVKFPLIEDITMEIAKKYGMLQPneDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDE 163
Cdd:PRK15000  81 VHNAWRNT---PVDKGGIG--PVKYAMVADVKREIQKAYGIEHP--DEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDE 153

                        170       180
                 ....*....|....*....|....*..
gi 984740551 164 LYRVLIALQAADAFDIATPADWRPGDD 190
Cdd:PRK15000 154 MLRMVDALQFHEEHGDVCPAQWEKGKE 180
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 11-168 2.04e-26

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: 99.66  E-value: 2.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  11 PRIGDKAPEFKAVTTQGDINFPSDYNG-GWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWl 89
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAW- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  90 rsikekIEYKGMknvdvKFPLIED--ITMEIAKKYGMLqpNEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRV 167
Cdd:cd03018   80 ------AEENGL-----TFPLLSDfwPHGEVAKAYGVF--DEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEA 146


                 .
gi 984740551 168 L 168
Cdd:cd03018  147 L 147
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 15-152 1.51e-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: 94.54  E-value: 1.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  15 DKAPEFKAVTTQGDINFPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWlrsiKE 94
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKF----AE 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 984740551  95 KieYKgmknvdVKFPLIEDITMEIAKKYGMLQP-NEDSTKAVRAVFFVDPKGIIRTIIY 152
Cdd:cd03017   77 K--YG------LPFPLLSDPDGKLAKAYGVWGEkKKKYMGIERSTFLIDPDGKIVKVWR 127
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
17-170 2.40e-19

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 80.68  E-value: 2.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  17 APEFKAVTTQG-DINFpSDYNGGWSILFSHpADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWlrsikek 95
Cdd:COG1225    1 APDFTLPDLDGkTVSL-SDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKF------- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984740551  96 ieykgMKNVDVKFPLIEDITMEIAKKYGMlqpnedstKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVLIA 170
Cdd:COG1225   72 -----AEKYGLPFPLLSDPDGEVAKAYGV--------RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLA 133
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 16-189 6.34e-19

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 81.19  E-value: 6.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  16 KAPEFKAVTTQgdinfpsDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSIDGLYSHIAWlRSIKEK 95
Cdd:PRK10382  17 KNGEFIEVTEK-------DTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAW-HSSSET 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  96 IEykgmknvDVKFPLIEDITMEIAKKYGMLQpnEDSTKAVRAVFFVDPKGIIRTIIYYPLSLGRNFDELYRVLIALQ--A 173
Cdd:PRK10382  89 IA-------KIKYAMIGDPTGALTRNFDNMR--EDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQyvA 159

                        170
                 ....*....|....*.
gi 984740551 174 ADAFDIAtPADWRPGD 189
Cdd:PRK10382 160 SHPGEVC-PAKWKEGE 174
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 14-168 3.07e-12

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 62.39  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   14 GDKAPEFKAVTTQGDIN--FPSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANCSLIGLSI--DGLYSHIAWl 89
Cdd:pfam08534   3 GDKAPDFTLPDAATDGNtvSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSdnDAFFVKRFW- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551   90 rsikekieykgmKNVDVKFPLIEDITMEIAKKYGMLQPnEDSTKAVRA--VFFVDPKGIIRTIIYYPLSlGRNFDELYRV 167
Cdd:pfam08534  82 ------------GKEGLPFPFLSDGNAAFTKALGLPIE-EDASAGLRSprYAVIDEDGKVVYLFVGPEP-GVDVSDAEAV 147


                  .
gi 984740551  168 L 168
Cdd:pfam08534 148 L 148
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 170-209 1.13e-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: 57.60  E-value: 1.13e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 984740551  170 ALQAADAFDIATPADWRPGDDVIIGPAGSCGTAKDRMEGK 209
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPATQEEAVKRYLEG 40
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 13-148 1.60e-03

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: 37.56  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  13 IGDKAPEFKAVTTQG-DINFpSDYNGGWSILFSHPADFTPVCTSEFITFASLEDKFKEANcsLIGLSIDGLYSHIAWlrs 91
Cdd:cd03014    2 VGDKAPDFTLVTSDLsEVSL-ADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTV--VLTISADLPFAQKRW--- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 984740551  92 ikekIEYKGMKNVDvkfPLIEDITMEIAKKYGMLQpnEDSTKAVRAVFFVDPKGIIR 148
Cdd:cd03014   76 ----CGAEGVDNVT---TLSDFRDHSFGKAYGVLI--KDLGLLARAVFVIDENGKVI 123
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 51-151 2.20e-03

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: 36.83  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984740551  51 PVCTSEFITFASLEDKFKEANCSLIGLSIDGlYSHIAWLRSIKEKieykgmknvDVKFPLIEDITMEIAKKYGmlqpned 130
Cdd:cd02966   32 PPCRAEMPELEALAKEYKDDGVEVVGVNVDD-DDPAAVKAFLKKY---------GITFPVLLDPDGELAKAYG------- 94

                         90       100
                 ....*....|....*....|....
gi 984740551 131 stkaVRAV---FFVDPKGIIRTII 151
Cdd:cd02966   95 ----VRGLpttFLIDRDGRIRARH 114
 
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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