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Conserved domains on  [gi|262118506|pdb|3A2X|B]
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Chain B, Probable peroxiredoxin

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13189 super family cl29163
peroxiredoxin; Provisional
 2-212 2.11e-122

peroxiredoxin; Provisional


The actual alignment was detected with superfamily member PRK13189:

Pssm-ID: 237297  Cd Length: 222  Bit Score: 346.97  E-value: 2.11e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         2 GSIPLIGERFPEMEVTTDHGVIKLPDHYvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSH 81
Cdd:PRK13189   6 IRMPLIGDKFPEFEVKTTHGPIKLPDDY--KGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        82 IKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALK 161
Cdd:PRK13189  84 IKWVEWIKEKLGVEIEFPIIADDRGEIAKKLGMISPGKGTNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQ 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
3A2X_B       162 LGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMES---GQYRCLDWWFC 212
Cdd:PRK13189 164 TSDEKGVATPANWPPNDLIKDKVIVPPASSVEEAKKRLEAkekGEYECYDWWFC 217
 
Name Accession Description Interval E-value
PRK13189 PRK13189
peroxiredoxin; Provisional
 2-212 2.11e-122

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 346.97  E-value: 2.11e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         2 GSIPLIGERFPEMEVTTDHGVIKLPDHYvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSH 81
Cdd:PRK13189   6 IRMPLIGDKFPEFEVKTTHGPIKLPDDY--KGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        82 IKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALK 161
Cdd:PRK13189  84 IKWVEWIKEKLGVEIEFPIIADDRGEIAKKLGMISPGKGTNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQ 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
3A2X_B       162 LGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMES---GQYRCLDWWFC 212
Cdd:PRK13189 164 TSDEKGVATPANWPPNDLIKDKVIVPPASSVEEAKKRLEAkekGEYECYDWWFC 217
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 7-213 4.12e-111

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: 317.95  E-value: 4.12e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        7 IGERFPEMEVTTDHGVIKLPDHYVsqGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKE 86
Cdd:cd03016   1 LGDTAPNFEADTTHGPIKFHDYLG--DSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       87 WIERHIGVRIPFPIIADPQGTVARRLGLLHA-ESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDS 165
Cdd:cd03016  79 DIEEYTGVEIPFPIIADPDREVAKLLGMIDPdAGSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTDK 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3A2X_B      166 LKRAVPADWPNneiiGEGLIVPPPTTEDQARARMESGqYRCLDWWFCW 213
Cdd:cd03016 159 HKVATPANWKP----GDDVIVPPSVSDEEAKKKFPKG-YETVDWYLRF 201
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
3-201 7.72e-94

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 273.88  E-value: 7.72e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        3 SIPLIGERFPEMEVTTDHG----VIKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSV 78
Cdd:COG0450   1 MMPLIGDKAPDFTAEATHGgefkKISLSDY---KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       79 FSHIKWKEWIERHIG-VRIPFPIIADPQGTVARRLGLLHAEsATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIV 157
Cdd:COG0450  78 FSHKAWHETIKEKGGiVKIKFPIIADPTGKIARAYGMLHPE-DGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVV 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
3A2X_B      158 KALKLGDSLKRAVPADWPNneiiGEGLIVPPPTTEDQARARMES 201
Cdd:COG0450 157 DALQFVDKHGEVCPANWKP----GDKVIIPPPDLVGKALERFPE 196
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 7-137 1.86e-39

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: 132.73  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B          7 IGERFPEMEVTTDHG-VIKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWK 85
Cdd:pfam00578   1 VGDKAPDFELPDGDGgTVSLSDY---RGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
3A2X_B         86 EWIErhigvrIPFPIIADPQGTVARRLGLLHaESATHTVRGVFIVDARGVIR 137
Cdd:pfam00578  78 EKYG------LPFPLLSDPDGEVARAYGVLN-EEEGGALRATFVIDPDGKVR 122
 
Name Accession Description Interval E-value
PRK13189 PRK13189
peroxiredoxin; Provisional
 2-212 2.11e-122

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 346.97  E-value: 2.11e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         2 GSIPLIGERFPEMEVTTDHGVIKLPDHYvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSH 81
Cdd:PRK13189   6 IRMPLIGDKFPEFEVKTTHGPIKLPDDY--KGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        82 IKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALK 161
Cdd:PRK13189  84 IKWVEWIKEKLGVEIEFPIIADDRGEIAKKLGMISPGKGTNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQ 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
3A2X_B       162 LGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMES---GQYRCLDWWFC 212
Cdd:PRK13189 164 TSDEKGVATPANWPPNDLIKDKVIVPPASSVEEAKKRLEAkekGEYECYDWWFC 217
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 7-213 4.12e-111

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: 317.95  E-value: 4.12e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        7 IGERFPEMEVTTDHGVIKLPDHYVsqGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKE 86
Cdd:cd03016   1 LGDTAPNFEADTTHGPIKFHDYLG--DSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       87 WIERHIGVRIPFPIIADPQGTVARRLGLLHA-ESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDS 165
Cdd:cd03016  79 DIEEYTGVEIPFPIIADPDREVAKLLGMIDPdAGSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTDK 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3A2X_B      166 LKRAVPADWPNneiiGEGLIVPPPTTEDQARARMESGqYRCLDWWFCW 213
Cdd:cd03016 159 HKVATPANWKP----GDDVIVPPSVSDEEAKKKFPKG-YETVDWYLRF 201
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 2-213 8.98e-109

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 312.55  E-value: 8.98e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         2 GSIPLIGERFPEMEVTTDHGVIKLPDHYvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSH 81
Cdd:PRK13191   4 GRIPLIGEKFPEMEVITTHGKIKLPDDY--KGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        82 IKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALK 161
Cdd:PRK13191  82 IEWVMWIEKNLKVEVPFPIIADPMGNVAKRLGMIHAESSTATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQ 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
3A2X_B       162 LGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGqyrcLDWWFCW 213
Cdd:PRK13191 162 LVDKAGVVTPANWPNNELIGDKVINPAPRTIKDAKMRLGQP----FDWWFTY 209
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
3-201 7.72e-94

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 273.88  E-value: 7.72e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        3 SIPLIGERFPEMEVTTDHG----VIKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSV 78
Cdd:COG0450   1 MMPLIGDKAPDFTAEATHGgefkKISLSDY---KGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       79 FSHIKWKEWIERHIG-VRIPFPIIADPQGTVARRLGLLHAEsATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIV 157
Cdd:COG0450  78 FSHKAWHETIKEKGGiVKIKFPIIADPTGKIARAYGMLHPE-DGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVV 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
3A2X_B      158 KALKLGDSLKRAVPADWPNneiiGEGLIVPPPTTEDQARARMES 201
Cdd:COG0450 157 DALQFVDKHGEVCPANWKP----GDKVIIPPPDLVGKALERFPE 196
PRK13599 PRK13599
peroxiredoxin;
4-211 8.15e-87

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 256.95  E-value: 8.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         4 IPLIGERFPEMEVTTDHGVIKLPDHYVsqGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIK 83
Cdd:PRK13599   1 MKLLGEKFPSMEVVTTQGVKRLPEDYA--GKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        84 WKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLG 163
Cdd:PRK13599  79 WVEWIKDNTNIAIPFPVIADDLGKVSNQLGMIHPGKGTNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
3A2X_B       164 DSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME---SGQYRCLDWWF 211
Cdd:PRK13599 159 DQYGVALPEKWPNNYLIKDHVIVPPSTDEASANERKEkikSKEIEAFDWWF 209
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 7-199 2.51e-77

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 232.05  E-value: 2.51e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         7 IGERFPEMEVTTDHGVIKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKE 86
Cdd:PRK13190   4 LGQKAPDFTVNTTKGPIDLSKY---KGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        87 WIERHIGVRIPFPIIADPQGTVARRLGLLHaESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSL 166
Cdd:PRK13190  81 DIEERFGIKIPFPVIADIDKELAREYNLID-ENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVNWKR 159

                        170       180       190
                 ....*....|....*....|....*....|...
3A2X_B       167 KRAVPADWPNneiiGEGLIVPPPTTEDQARARM 199
Cdd:PRK13190 160 KVATPANWQP----GQEGIVPAPSTLDEAEMRI 188
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 10-154 5.43e-49

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: 157.71  E-value: 5.43e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       10 RFPEMEV-TTDHGVIKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWI 88
Cdd:cd02971   1 KAPDFTLpATDGGEVSLSDF---KGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKE 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3A2X_B       89 ErhigvRIPFPIIADPQGTVARRLGLLHAESATH--TVRGVFIVDARGVIRTMLYYPMELGRLVDEIL 154
Cdd:cd02971  78 G-----GLNFPLLSDPDGEFAKAYGVLIEKSAGGglAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 7-174 3.64e-43

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: 144.18  E-value: 3.64e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        7 IGERFPEMEVTTDHGV-----IKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSH 81
Cdd:cd03015   1 VGKKAPDFKATAVVPNgefkeISLSDY---KGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSH 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       82 IKWKEWIERHIGV-RIPFPIIADPQGTVARRLGLLHAEsATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL 160
Cdd:cd03015  78 LAWRNTPRKEGGLgKINFPLLADPKKKISRDYGVLDEE-EGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDAL 156

                       170
                ....*....|....
3A2X_B      161 KLGDSLKRAVPADW 174
Cdd:cd03015 157 QFVEEHGEVCPANW 170
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 7-137 1.86e-39

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: 132.73  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B          7 IGERFPEMEVTTDHG-VIKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWK 85
Cdd:pfam00578   1 VGDKAPDFELPDGDGgTVSLSDY---RGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
3A2X_B         86 EWIErhigvrIPFPIIADPQGTVARRLGLLHaESATHTVRGVFIVDARGVIR 137
Cdd:pfam00578  78 EKYG------LPFPLLSDPDGEVARAYGVLN-EEEGGALRATFVIDPDGKVR 122
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 9-155 8.02e-30

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: 108.79  E-value: 8.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        9 ERFPEMEVTTDHG-VIKLPDHyvsQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHikwKEW 87
Cdd:cd03017   1 DKAPDFTLPDQDGeTVSLSDL---RGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESH---AKF 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       88 IERHigvRIPFPIIADPQGTVARRLGLLHAESATH--TVRGVFIVDARGVIRtMLYYPMELGRLVDEILR 155
Cdd:cd03017  75 AEKY---GLPFPLLSDPDGKLAKAYGVWGEKKKKYmgIERSTFLIDPDGKIV-KVWRKVKPKGHAEEVLE 140
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 6-174 1.64e-27

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 106.18  E-value: 1.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         6 LIGERFPEMEVTT--DHGVIKLPDHYVSQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIK 83
Cdd:PTZ00137  69 LVGKLMPSFKGTAllNDDLVQFNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        84 WKEWIERHIGVR-IPFPIIADPQGTVARRLGLLHAESATHtvRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKL 162
Cdd:PTZ00137 149 WKELDVRQGGVSpLKFPLFSDISREVSKSFGLLRDEGFSH--RASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQF 226

                        170
                 ....*....|..
3A2X_B       163 GDSLKRAVPADW 174
Cdd:PTZ00137 227 AEKTGNVCPVNW 238
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 32-174 1.75e-27

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 104.22  E-value: 1.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        32 QGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEwIERHIG--VRIPFPIIADPQGTVA 109
Cdd:PTZ00253  35 KGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTL-QERKKGglGTMAIPMLADKTKSIA 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
3A2X_B       110 RRLGLLHAESAThTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADW 174
Cdd:PTZ00253 114 RSYGVLEEEQGV-AYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVEKHGEVCPANW 177
PRK15000 PRK15000
peroxiredoxin C;
31-188 3.96e-27

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 103.60  E-value: 3.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        31 SQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERHIGV-RIPFPIIADPQGTVA 109
Cdd:PRK15000  32 TNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRNTPVDKGGIgPVKYAMVADVKREIQ 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3A2X_B       110 RRLGLLHAESAThTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAVPADWPNNEiigEGLIVPP 188
Cdd:PRK15000 112 KAYGIEHPDEGV-ALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQFHEEHGDVCPAQWEKGK---EGMNASP 186
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 5-155 6.30e-25

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: 96.19  E-value: 6.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        5 PLIGERFPEMEVTTDHG-VIKLPDhyVSQGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHik 83
Cdd:cd03018   1 LEVGDKAPDFELPDQNGqEVRLSE--FRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSL-- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3A2X_B       84 wKEWIERHigvRIPFPIIAD--PQGTVARRLGLLHaESATHTVRGVFIVDARGVIR----TMLYYPMELGRlVDEILR 155
Cdd:cd03018  77 -RAWAEEN---GLTFPLLSDfwPHGEVAKAYGVFD-EDLGVAERAVFVIDRDGIIRyawvSDDGEPRDLPD-YDEALD 148
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 32-178 1.82e-23

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 93.51  E-value: 1.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        32 QGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKWKEWIERhIGvRIPFPIIADPQGTVARR 111
Cdd:PRK10382  30 EGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSET-IA-KIKYAMIGDPTGALTRN 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3A2X_B       112 LGLLHaESATHTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLGDSLKRAV-PADWPNNE 178
Cdd:PRK10382 108 FDNMR-EDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVcPAKWKEGE 174
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
12-161 7.59e-23

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 90.31  E-value: 7.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       12 PEMEVTTDHG-VIKLPDHyvsQGKWFVLFSHpADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHikwKEWIER 90
Cdd:COG1225   2 PDFTLPDLDGkTVSLSDL---RGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAH---KKFAEK 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3A2X_B       91 HigvRIPFPIIADPQGTVARRLGLLhaesathTVRGVFIVDARGVIRTMLYYPMELGRLVDEILR-IVKALK 161
Cdd:COG1225  75 Y---GLPFPLLSDPDGEVAKAYGVR-------GTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEaLLAELK 136
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 32-137 4.34e-10

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 56.61  E-value: 4.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         32 QGKWFVLFSHPADFTPVSTTEFVSFARRYEDFQRLGVDLIGLSVDSVFSHIKwKEWIERHigvrIPFPIIADPQGTVARR 111
Cdd:pfam08534  27 KGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVK-RFWGKEG----LPFPFLSDGNAAFTKA 101

                          90       100
                  ....*....|....*....|....*...
3A2X_B        112 LGLLHAESATHTVR--GVFIVDARGVIR 137
Cdd:pfam08534 102 LGLPIEEDASAGLRspRYAVIDEDGKVV 129
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 60-137 8.22e-08

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: 49.54  E-value: 8.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       60 YEDFQRLGVDLIGLSVDSvFSHIKWKEWIERHigvRIPFPIIADPQGTVARRLGllhaesathtVRGV---FIVDARGVI 136
Cdd:cd02966  45 AKEYKDDGVEVVGVNVDD-DDPAAVKAFLKKY---GITFPVLLDPDGELAKAYG----------VRGLpttFLIDRDGRI 110


                .
3A2X_B      137 R 137
Cdd:cd02966 111 R 111
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 7-159 1.10e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.69  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        7 IGERFPEMEVTTDHG-VIKLPDHyvsQGKWFVLF-----------SHPadftpvsttEFVSFARRYEDFQrlgvdLIGLS 74
Cdd:COG0526   4 VGKPAPDFTLTDLDGkPLSLADL---KGKPVLVNfwatwcppcraEMP---------VLKELAEEYGGVV-----FVGVD 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       75 VDSvfSHIKWKEWIERHigvRIPFPIIADPQGTVARRLGllhaesathtVRGV---FIVDARGVIRTMLYYPMELGRLVD 151
Cdd:COG0526  67 VDE--NPEAVKAFLKEL---GLPYPVLLDPDGELAKAYG----------VRGIpttVLIDKDGKIVARHVGPLSPEELEE 131


                ....*...
3A2X_B      152 EILRIVKA 159
Cdd:COG0526 132 ALEKLLAK 139
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
7-115 3.69e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 42.77  E-value: 3.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        7 IGERFPEMEVTT--DHGVIKLPDHYVSQGKWFVLFSHPADFTPV-STTEFVSFARRYEDFQRLGVDLI-GLSVDSVFSHI 82
Cdd:COG0678   4 VGDKLPDVTFKTrtADGPEDVTTDDLFAGKKVVLFAVPGAFTPTcSSAHLPGFVELADAFKAKGVDEIaCVSVNDAFVMN 83

                        90       100       110
                ....*....|....*....|....*....|...
3A2X_B       83 KWKEwiERHIGVRIPFpiIADPQGTVARRLGLL 115
Cdd:COG0678  84 AWGK--AQGAEGKITM--LADGNGEFTKALGLE 112
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 7-139 1.15e-03

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 38.31  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B        7 IGERFPEMEVTTD--HGVIKLPDHYVSQGKWFVLFSHPADFTPVSTTEFV-SFARRYEDFQRLGVD-LIGLSVDSVFSHI 82
Cdd:cd03013   1 VGDKLPNVTLFEYvpGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLpGYVENADELKAKGVDeVICVSVNDPFVMK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3A2X_B       83 KWKEW--IERHIGvripfpIIADPQGTVARRLGLLHAESATH----TVRGVFIVDaRGVIRTM 139
Cdd:cd03013  81 AWGKAlgAKDKIR------FLADGNGEFTKALGLTLDLSAAGggirSKRYALIVD-DGKVKYL 136
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 55-137 1.39e-03

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: 38.11  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       55 SFARRYEDFQRLGVDLIGLSVDSvfshikWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESATHTVR--------- 125
Cdd:cd02970  45 ALSKLLPELDALGVELVAVGPES------PEKLEAFDKGKFLPFPVYADPDRKLYRALGLVRSLPWSNTPRalwknaaig 118

                        90       100
                ....*....|....*....|....*
3A2X_B      126 -------------GVFIVDARGVIR 137
Cdd:cd02970 119 frgndegdglqlpGVFVIGPDGTIL 143
AhpC-TSA_2 pfam13911
AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide ...
 55-145 2.10e-03

AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 433575  Cd Length: 114  Bit Score: 36.90  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B         55 SFARRYEDFQRLGVDLIGLSVDSVfSHIKwkEWIERhigVRIPFPIIADPQGTVARRLGLlhaesathtVRGVFIVDARG 134
Cdd:pfam13911   1 RLSSLKPELDAAGIRLVAIGCGTP-GRIE--EFIKL---TGFPFPVYVDPSRKLYRALGL---------KRGLSGGLLPG 65

                          90
                  ....*....|.
3A2X_B        135 VIRTMLYYPME 145
Cdd:pfam13911  66 FLGKGLRNMTR 76
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 61-151 4.73e-03

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: 36.83  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3A2X_B       61 EDFQRLGVDLIGLSVDSVFSHI-----KWKEWIERHigvRIPFPIIADPQGTVARRLGllhaesATHTVRgVFIVDARGV 135
Cdd:cd02969  52 KEYGAKGVAVVAINSNDIEAYPedspeNMKAKAKEH---GYPFPYLLDETQEVAKAYG------AACTPD-FFLFDPDGK 121

                        90
                ....*....|....*.
3A2X_B      136 irtmLYYpmeLGRLVD 151
Cdd:cd02969 122 ----LVY---RGRIDD 130
 
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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