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Conserved domains on  [gi|499802559|ref|WP_011483293|]
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peroxiredoxin [Polaromonas sp. JS666]

Protein Classification

peroxiredoxin( domain architecture ID 10122448)

peroxiredoxin is a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 6-212 3.27e-129

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: 362.24  E-value: 3.27e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   6 LGDIAPDFTQDSTEGKISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDI 85
Cdd:cd03016    1 LGDTAPNFEADTTHGPIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  86 NETQNTTVNFPILADADRKVANLYDMIHPNAlstGPTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLTD 165
Cdd:cd03016   81 EEYTGVEIPFPIIADPDREVAKLLGMIDPDA---GSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 499802559 166 GYKVATPVNWKDGDDVIIVPSLQDpAELAQRFPKGFKAVKPYLRITP 212
Cdd:cd03016  158 KHKVATPANWKPGDDVIVPPSVSD-EEAKKKFPKGYETVDWYLRFTP 203
 
Name Accession Description Interval E-value
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 6-212 3.27e-129

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: 362.24  E-value: 3.27e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   6 LGDIAPDFTQDSTEGKISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDI 85
Cdd:cd03016    1 LGDTAPNFEADTTHGPIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  86 NETQNTTVNFPILADADRKVANLYDMIHPNAlstGPTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLTD 165
Cdd:cd03016   81 EEYTGVEIPFPIIADPDREVAKLLGMIDPDA---GSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 499802559 166 GYKVATPVNWKDGDDVIIVPSLQDpAELAQRFPKGFKAVKPYLRITP 212
Cdd:cd03016  158 KHKVATPANWKPGDDVIVPPSVSD-EEAKKKFPKGYETVDWYLRFTP 203
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
3-199 4.02e-100

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 288.13  E-value: 4.02e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   3 TLRLGDIAPDFTQDSTEG----KISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESH 78
Cdd:COG0450    2 MPLIGDKAPDFTAEATHGgefkKISLSDYKG-KWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  79 GKWVHDINETQN-TTVNFPILADADRKVANLYDMIHPNAlstgpTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRV 157
Cdd:COG0450   81 KAWHETIKEKGGiVKIKFPIIADPTGKIARAYGMLHPED-----GVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 499802559 158 IDSLQLTDGYKVATPVNWKDGDDVIIvPSLQDPAELAQRFPK 199
Cdd:COG0450  156 VDALQFVDKHGEVCPANWKPGDKVII-PPPDLVGKALERFPE 196
PRK13189 PRK13189
peroxiredoxin; Provisional
 5-196 2.95e-75

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 226.40  E-value: 2.95e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   5 RLGDIAPDFTQDSTEGKISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHD 84
Cdd:PRK13189  10 LIGDKFPEFEVKTTHGPIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEW 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  85 INETQNTTVNFPILADADRKVANLYDMIHPNALSTgptaTVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLT 164
Cdd:PRK13189  90 IKEKLGVEIEFPIIADDRGEIAKKLGMISPGKGTN----TVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQTS 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499802559 165 DGYKVATPVNWKDGD---DVIIVPSLQDPAELAQR 196
Cdd:PRK13189 166 DEKGVATPANWPPNDlikDKVIVPPASSVEEAKKR 200
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 6-138 2.93e-36

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: 123.49  E-value: 2.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559    6 LGDIAPDFTQDSTEGK-ISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHD 84
Cdd:pfam00578   1 VGDKAPDFELPDGDGGtVSLSDYRG-KWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499802559   85 INetqnttVNFPILADADRKVANLYDMIHPNALstgptATVRSVFIIDPKKVIR 138
Cdd:pfam00578  80 YG------LPFPLLSDPDGEVARAYGVLNEEEG-----GALRATFVIDPDGKVR 122
 
Name Accession Description Interval E-value
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 6-212 3.27e-129

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: 362.24  E-value: 3.27e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   6 LGDIAPDFTQDSTEGKISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDI 85
Cdd:cd03016    1 LGDTAPNFEADTTHGPIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  86 NETQNTTVNFPILADADRKVANLYDMIHPNAlstGPTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLTD 165
Cdd:cd03016   81 EEYTGVEIPFPIIADPDREVAKLLGMIDPDA---GSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 499802559 166 GYKVATPVNWKDGDDVIIVPSLQDpAELAQRFPKGFKAVKPYLRITP 212
Cdd:cd03016  158 KHKVATPANWKPGDDVIVPPSVSD-EEAKKKFPKGYETVDWYLRFTP 203
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
3-199 4.02e-100

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 288.13  E-value: 4.02e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   3 TLRLGDIAPDFTQDSTEG----KISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESH 78
Cdd:COG0450    2 MPLIGDKAPDFTAEATHGgefkKISLSDYKG-KWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  79 GKWVHDINETQN-TTVNFPILADADRKVANLYDMIHPNAlstgpTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRV 157
Cdd:COG0450   81 KAWHETIKEKGGiVKIKFPIIADPTGKIARAYGMLHPED-----GVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 499802559 158 IDSLQLTDGYKVATPVNWKDGDDVIIvPSLQDPAELAQRFPK 199
Cdd:COG0450  156 VDALQFVDKHGEVCPANWKPGDKVII-PPPDLVGKALERFPE 196
PRK13189 PRK13189
peroxiredoxin; Provisional
 5-196 2.95e-75

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 226.40  E-value: 2.95e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   5 RLGDIAPDFTQDSTEGKISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHD 84
Cdd:PRK13189  10 LIGDKFPEFEVKTTHGPIKLPDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEW 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  85 INETQNTTVNFPILADADRKVANLYDMIHPNALSTgptaTVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLT 164
Cdd:PRK13189  90 IKEKLGVEIEFPIIADDRGEIAKKLGMISPGKGTN----TVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQTS 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499802559 165 DGYKVATPVNWKDGD---DVIIVPSLQDPAELAQR 196
Cdd:PRK13189 166 DEKGVATPANWPPNDlikDKVIVPPASSVEEAKKR 200
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 4-198 8.17e-59

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 183.90  E-value: 8.17e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   4 LRLGDIAPDFTQDSTEGKISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVH 83
Cdd:PRK13190   2 VKLGQKAPDFTVNTTKGPIDLSKYKG-KWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  84 DINETQNTTVNFPILADADRKVANLYDMIHPNAlstgpTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQL 163
Cdd:PRK13190  81 DIEERFGIKIPFPVIADIDKELAREYNLIDENS-----GATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQV 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499802559 164 TDGYKVATPVNWKDGDDVII-VPSLQDPAELAQRFP 198
Cdd:PRK13190 156 NWKRKVATPANWQPGQEGIVpAPSTLDEAEMRIKEP 191
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 10-155 4.52e-47

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: 151.55  E-value: 4.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  10 APDFT-QDSTEGKISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDINEt 88
Cdd:cd02971    2 APDFTlPATDGGEVSLSDFKG-KWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEGG- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499802559  89 qnttVNFPILADADRKVANLYDMIHPNALSTGptATVRSVFIIDPKKVIRTTFTYPASTGRNFDEIL 155
Cdd:cd02971   80 ----LNFPLLSDPDGEFAKAYGVLIEKSAGGG--LAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 6-201 6.23e-46

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 151.54  E-value: 6.23e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   6 LGDIAPDFTQDSTEGKISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDI 85
Cdd:PRK13191   9 IGEKFPEMEVITTHGKIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  86 NETQNTTVNFPILADADRKVANLYDMIHPNAlstgPTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLTD 165
Cdd:PRK13191  89 EKNLKVEVPFPIIADPMGNVAKRLGMIHAES----STATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVD 164

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499802559 166 GYKVATPVNWKDGD---DVIIVPSLQDPAELAQRFPKGF 201
Cdd:PRK13191 165 KAGVVTPANWPNNEligDKVINPAPRTIKDAKMRLGQPF 203
PRK13599 PRK13599
peroxiredoxin;
6-199 1.53e-42

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 142.93  E-value: 1.53e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   6 LGDIAPDFTQDSTEGKISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDI 85
Cdd:PRK13599   4 LGEKFPSMEVVTTQGVKRLPEDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  86 NETQNTTVNFPILADADRKVANLYDMIHPNAlstgPTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLTD 165
Cdd:PRK13599  84 KDNTNIAIPFPVIADDLGKVSNQLGMIHPGK----GTNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTAD 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 499802559 166 GYKVATPVNWKDG---DDVIIVPSLQDPAELAQRFPK 199
Cdd:PRK13599 160 QYGVALPEKWPNNyliKDHVIVPPSTDEASANERKEK 196
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 6-138 2.93e-36

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: 123.49  E-value: 2.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559    6 LGDIAPDFTQDSTEGK-ISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHD 84
Cdd:pfam00578   1 VGDKAPDFELPDGDGGtVSLSDYRG-KWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499802559   85 INetqnttVNFPILADADRKVANLYDMIHPNALstgptATVRSVFIIDPKKVIR 138
Cdd:pfam00578  80 YG------LPFPLLSDPDGEVARAYGVLNEEEG-----GALRATFVIDPDGKVR 122
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 6-178 1.33e-34

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: 121.07  E-value: 1.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   6 LGDIAPDFT-----QDSTEGKISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGK 80
Cdd:cd03015    1 VGKKAPDFKatavvPNGEFKEISLSDYKG-KWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  81 WvHDINETQNT--TVNFPILADADRKVANLYDMIHPN---ALstgptatvRSVFIIDPKKVIRTTFTYPASTGRNFDEIL 155
Cdd:cd03015   80 W-RNTPRKEGGlgKINFPLLADPKKKISRDYGVLDEEegvAL--------RGTFIIDPEGIIRHITVNDLPVGRSVDETL 150

                        170       180
                 ....*....|....*....|...
gi 499802559 156 RVIDSLQLTDGYKVATPVNWKDG 178
Cdd:cd03015  151 RVLDALQFVEEHGEVCPANWKPG 173
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 10-179 1.79e-24

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 95.74  E-value: 1.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  10 APDFTQ-----DSTEGKISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKW-VH 83
Cdd:PTZ00253  12 APSFEEvalmpNGSFKKISLSSYKG-KWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWtLQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  84 DINETQNTTVNFPILADADRKVANLYDMihpnaLSTGPTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQL 163
Cdd:PTZ00253  91 ERKKGGLGTMAIPMLADKTKSIARSYGV-----LEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQF 165

                        170
                 ....*....|....*.
gi 499802559 164 TDGYKVATPVNWKDGD 179
Cdd:PTZ00253 166 VEKHGEVCPANWKKGD 181
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 8-138 3.63e-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: 93.00  E-value: 3.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   8 DIAPDFT-QDSTEGKISFHAWAGdSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDIN 86
Cdd:cd03017    1 DKAPDFTlPDQDGETVSLSDLRG-KPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499802559  87 etqnttVNFPILADADRKVANLYDMihPNALSTGPTATVRSVFIIDPKKVIR 138
Cdd:cd03017   80 ------LPFPLLSDPDGKLAKAYGV--WGEKKKKYMGIERSTFLIDPDGKIV 123
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 6-197 4.44e-24

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 96.17  E-value: 4.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   6 LGDIAPDF------TQDSTEGKISfhAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHG 79
Cdd:PTZ00137  70 VGKLMPSFkgtallNDDLVQFNSS--DYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHK 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  80 KWVH-DINETQNTTVNFPILADADRKVANLYDMIHPNALSTgptatvRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVI 158
Cdd:PTZ00137 148 AWKElDVRQGGVSPLKFPLFSDISREVSKSFGLLRDEGFSH------RASVLVDKAGVVKHVAVYDLGLGRSVDETLRLF 221

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499802559 159 DSLQLTDGYKVATPVNWKDGDDVIIVPSLQDPAELAQRF 197
Cdd:PTZ00137 222 DAVQFAEKTGNVCPVNWKQGDQAMKPDSQSVKQYLSNRF 260
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 4-159 8.92e-24

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: 92.34  E-value: 8.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   4 LRLGDIAPDFT---QDSTEGKISFHAwaGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGK 80
Cdd:cd03018    1 LEVGDKAPDFElpdQNGQEVRLSEFR--GRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  81 WvhdineTQNTTVNFPILAD--ADRKVANLYDMIHPNAlstgpTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVI 158
Cdd:cd03018   79 W------AEENGLTFPLLSDfwPHGEVAKAYGVFDEDL-----GVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEAL 147


                 .
gi 499802559 159 D 159
Cdd:cd03018  148 D 148
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
10-158 2.75e-23

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 90.69  E-value: 2.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  10 APDFTQDSTEGK-ISFHAWAGDSWVVLFShpADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVHDINet 88
Cdd:COG1225    1 APDFTLPDLDGKtVSLSDLRGKPVVLYFY--ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYG-- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  89 qnttVNFPILADADRKVANLYDMihpnalstgptATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVI 158
Cdd:COG1225   77 ----LPFPLLSDPDGEVAKAYGV-----------RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEAL 131
PRK15000 PRK15000
peroxiredoxin C;
10-180 1.39e-20

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 85.50  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  10 APDFTQDSTEG------KISFHAWAGDSWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWVH 83
Cdd:PRK15000   8 APDFTAAAVLGsgeivdKFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  84 D-INETQNTTVNFPILADADRKVANLYDMIHPNAlstgpTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQ 162
Cdd:PRK15000  88 TpVDKGGIGPVKYAMVADVKREIQKAYGIEHPDE-----GVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQ 162

                        170
                 ....*....|....*...
gi 499802559 163 LTDGYKVATPVNWKDGDD 180
Cdd:PRK15000 163 FHEEHGDVCPAQWEKGKE 180
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 12-187 1.72e-18

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 79.65  E-value: 1.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  12 DFTQDSTEGKisfhawagdsWVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHGKWvHDINETQnT 91
Cdd:PRK10382  23 EVTEKDTEGR----------WSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAW-HSSSETI-A 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  92 TVNFPILADADRKVANLYDMIHPnalstGPTATVRSVFIIDPKKVIRTTFTYPASTGRNFDEILRVIDSLQLTDGYK-VA 170
Cdd:PRK10382  91 KIKYAMIGDPTGALTRNFDNMRE-----DEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPgEV 165

                        170
                 ....*....|....*..
gi 499802559 171 TPVNWKDGdDVIIVPSL 187
Cdd:PRK10382 166 CPAKWKEG-EATLAPSL 181
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 7-158 1.17e-09

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 54.68  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559    7 GDIAPDFTQDS--TEGK-ISFHAWAGDSwVVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISV--DPLESHGKW 81
Cdd:pfam08534   3 GDKAPDFTLPDaaTDGNtVSLSDFKGKK-VVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSdnDAFFVKRFW 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499802559   82 VhdinetqNTTVNFPILADADRKVANLYDMIHPNALSTGPTAtvRSVFIIDPKKVIRTTFtYPASTGRNFDEILRVI 158
Cdd:pfam08534  82 G-------KEGLPFPFLSDGNAAFTKALGLPIEEDASAGLRS--PRYAVIDEDGKVVYLF-VGPEPGVDVSDAEAVL 148
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 1-142 2.52e-09

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 54.17  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   1 MATLRLGDIAPDFT-QDSTEGKISFHAWAGDSWVVLFsHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHG 79
Cdd:PRK09437   1 MNPLKAGDIAPKFSlPDQDGEQVSLTDFQGQRVLVYF-YPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLS 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499802559  80 KWVhdinETQNttVNFPILADADRKVAN-------------LYDMIHpnalstgptatvRSVFIIDPKKVIRTTFT 142
Cdd:PRK09437  80 RFA----EKEL--LNFTLLSDEDHQVAEqfgvwgekkfmgkTYDGIH------------RISFLIDADGKIEHVFD 137
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 10-138 5.68e-07

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: 47.35  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559  10 APDFTQDSTEGK-ISFHAWAGDSWVVLFshpadFT-----PVCTTELGKTAALSREFAKRHVKPIAISVDPLEshgkwvH 83
Cdd:cd02970    2 APDFELPDAGGEtVTLSALLGEGPVVVV-----FYrgfgcPFCREYLRALSKLLPELDALGVELVAVGPESPE------K 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499802559  84 DINETQNTTVNFPILADADRKVANLYDM-------IHPNALSTGPTATVRS-----------VFIIDPKKVIR 138
Cdd:cd02970   71 LEAFDKGKFLPFPVYADPDRKLYRALGLvrslpwsNTPRALWKNAAIGFRGndegdglqlpgVFVIGPDGTIL 143
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 160-200 6.29e-07

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: 44.50  E-value: 6.29e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 499802559  160 SLQLTDGYKVATPVNWKDGDDVIIVPSlQDPAELAQRFPKG 200
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPP-ATQEEAVKRYLEG 40
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
5-142 1.15e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 41.14  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   5 RLGDIAPDFTQDSTEGK-ISFHAWAGDSwvVLFSHPADFTPVCTTELGKTAALSREFAKRHVKPIAISVDPLESHgkwVH 83
Cdd:PRK03147  36 QVGKEAPNFVLTDLEGKkIELKDLKGKG--VFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELA---VK 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499802559  84 DINETQNttVNFPILADADRKVANLYDMihpnalstGPTATvrsVFIIDP----KKVIRTTFT 142
Cdd:PRK03147 111 NFVNRYG--LTFPVAIDKGRQVIDAYGV--------GPLPT---TFLIDKdgkvVKVITGEMT 160
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 7-134 2.08e-04

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: 40.30  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   7 GDIAPDFTQDSTEGK-ISFHAWAGDSWVVLFshpadFT----PVCTTELGKTAALSREFAKRHVKPIAISVDPLESHG-- 79
Cdd:cd02969    1 GSPAPDFSLPDTDGKtYSLADFADGKALVVM-----FIcnhcPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPed 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499802559  80 ------KWVHDINetqnttVNFPILADADRKVANLYdmihpNALSTgPTAtvrsvFIIDPK 134
Cdd:cd02969   76 spenmkAKAKEHG------YPFPYLLDETQEVAKAY-----GAACT-PDF-----FLFDPD 119
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 9-143 5.91e-04

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 38.74  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499802559   9 IAPDFTQDSTEGK-ISFHAWAGDSWVVLFShpadFT--P-VCTTELGKTAALSREFAKRH---VKPIAISVDP----LES 77
Cdd:cd02968    1 IGPDFTLTDQDGRpVTLSDLKGKPVLVYFG----YThcPdVCPTTLANLAQALKQLGADGgddVQVVFISVDPerdtPEV 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499802559  78 HGKWVHDIN-----------ETQNTTVNFPILADADRKVANLYDMIHPNAlstgptatvrsVFIIDPKKVIRTTFTY 143
Cdd:cd02968   77 LKAYAKAFGpgwigltgtpeEIEALAKAFGVYYEKVPEDDGDYLVDHSAA-----------IYLVDPDGKLVRYYGG 142
 
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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