NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2315490305|dbj|GIW63182|]
View 

MAG: peroxiredoxin [Patescibacteria group bacterium]

Protein Classification

peroxiredoxin( domain architecture ID 10122458)

peroxiredoxin belonging to the bacterioferritin comigratory protein (BCP) subfamily is a thioredoxin-dependent thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively

CATH:  3.40.30.10
EC:  1.11.1.24
Gene Ontology:  GO:0051920|GO:0008379
PubMed:  15518547|12517450|10644761|15558583
SCOP:  4000042

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 1-143 1.19e-64

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: 193.92  E-value: 1.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   1 MKAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKL 80
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2315490305  81 NFPLLSDTSKEIIKKYEAWGKKrfmGREFEGILRISYLINPEGKVVKKYDKVKPEVHAKEVLD 143
Cdd:cd03017    81 PFPLLSDPDGKLAKAYGVWGEK---KKKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 1-143 1.19e-64

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: 193.92  E-value: 1.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   1 MKAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKL 80
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2315490305  81 NFPLLSDTSKEIIKKYEAWGKKrfmGREFEGILRISYLINPEGKVVKKYDKVKPEVHAKEVLD 143
Cdd:cd03017    81 PFPLLSDPDGKLAKAYGVWGEK---KKKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-147 8.54e-53

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 164.34  E-value: 8.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLN 81
Cdd:PRK09437    9 IAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAEKELLN 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315490305  82 FPLLSDTSKEIIKKYEAWGKKRFMGREFEGILRISYLINPEGKVVKKYDKVKPEVHAKEVLDDINK 147
Cdd:PRK09437   89 FTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLDYLKE 154
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 2-123 2.38e-47

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: 149.68  E-value: 2.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLN 81
Cdd:pfam00578   4 KAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYGLP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2315490305  82 FPLLSDTSKEIIKKYEAWGKkrfmgrEFEGILRISYLINPEG 123
Cdd:pfam00578  84 FPLLSDPDGEVARAYGVLNE------EEGGALRATFVIDPDG 119
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
3-145 1.62e-43

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 140.00  E-value: 1.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   3 AIDFLLPDQDNNFHSLKDYNGKWVLLYFYpKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLNF 82
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315490305  83 PLLSDTSKEIIKKYEAWGkkrfmgrefegiLRISYLINPEGK-VVKKYDKVKPEVHAKEVLDDI 145
Cdd:COG1225    80 PLLSDPDGEVAKAYGVRG------------TPTTFLIDPDGKiRYVWVGPVDPRPHLEEVLEAL 131
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
2-123 1.10e-14

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 68.53  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPD-QDNNFHSLK--DYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHK------ 72
Cdd:NF040737   41 KAPDFTAPAyYKGGFTNVKlsDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKmwndee 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2315490305  73 --KFAEKfKLNFPLLSDTSKEIIKKYEAWGkkrfmgrEFEGI-LRISYLINPEG 123
Cdd:NF040737  121 lsKMVTG-GVPFPMLSDGGGKIGKAYGVYD-------EAAGVdIRGRFIIDPDG 166
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 19-123 1.79e-13

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


Pssm-ID: 211789  Cd Length: 187  Bit Score: 64.34  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  19 KDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKF----KLNFPLLSDTSKEIIK 94
Cdd:TIGR03137  27 EDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWHDTSeaigKITYPMLGDPTGVLTR 106

                          90       100       110
                  ....*....|....*....|....*....|
gi 2315490305  95 KYEAWgkkrfmgREFEGI-LRISYLINPEG 123
Cdd:TIGR03137 107 NFGVL-------IEEAGLaDRGTFVIDPEG 129
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 1-143 1.19e-64

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: 193.92  E-value: 1.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   1 MKAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKL 80
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2315490305  81 NFPLLSDTSKEIIKKYEAWGKKrfmGREFEGILRISYLINPEGKVVKKYDKVKPEVHAKEVLD 143
Cdd:cd03017    81 PFPLLSDPDGKLAKAYGVWGEK---KKKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-147 8.54e-53

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 164.34  E-value: 8.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLN 81
Cdd:PRK09437    9 IAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAEKELLN 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315490305  82 FPLLSDTSKEIIKKYEAWGKKRFMGREFEGILRISYLINPEGKVVKKYDKVKPEVHAKEVLDDINK 147
Cdd:PRK09437   89 FTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLDYLKE 154
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 2-142 8.98e-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: 153.47  E-value: 8.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKF-KL 80
Cdd:cd02971     1 KAPDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEgGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2315490305  81 NFPLLSDTSKEIIKKYEAWGKKRFMGRefeGILRISYLINPEGKVVKKYDKVKPEVHAKEVL 142
Cdd:cd02971    81 NFPLLSDPDGEFAKAYGVLIEKSAGGG---LAARATFIIDPDGKIRYVEVEPLPTGRNAEEL 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 2-123 2.38e-47

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: 149.68  E-value: 2.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLN 81
Cdd:pfam00578   4 KAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYGLP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2315490305  82 FPLLSDTSKEIIKKYEAWGKkrfmgrEFEGILRISYLINPEG 123
Cdd:pfam00578  84 FPLLSDPDGEVARAYGVLNE------EEGGALRATFVIDPDG 119
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
3-145 1.62e-43

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 140.00  E-value: 1.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   3 AIDFLLPDQDNNFHSLKDYNGKWVLLYFYpKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLNF 82
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315490305  83 PLLSDTSKEIIKKYEAWGkkrfmgrefegiLRISYLINPEGK-VVKKYDKVKPEVHAKEVLDDI 145
Cdd:COG1225    80 PLLSDPDGEVAKAYGVRG------------TPTTFLIDPDGKiRYVWVGPVDPRPHLEEVLEAL 131
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 2-123 6.03e-31

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: 108.52  E-value: 6.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNG-KWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKL 80
Cdd:cd03018     6 KAPDFELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWAEENGL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2315490305  81 NFPLLSD--TSKEIIKKYEAWgkkrfmgREFEGI-LRISYLINPEG 123
Cdd:cd03018    86 TFPLLSDfwPHGEVAKAYGVF-------DEDLGVaERAVFVIDRDG 124
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
2-123 8.53e-29

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 104.39  E-value: 8.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLP-DQDNNFH--SLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFA--- 75
Cdd:COG0450     8 KAPDFTAEaTHGGEFKkiSLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWHeti 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2315490305  76 -EKF---KLNFPLLSDTSKEIIKKYEawgkkrfMGREFEGI-LRISYLINPEG 123
Cdd:COG0450    88 kEKGgivKIKFPIIADPTGKIARAYG-------MLHPEDGVaVRGVFIIDPDG 133
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 2-123 9.98e-24

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: 90.64  E-value: 9.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLP--DQDNNFH--SLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEK 77
Cdd:cd03015     4 KAPDFKATavVPNGEFKeiSLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAWRNT 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2315490305  78 F-------KLNFPLLSDTSKEIIKKYeawgkkrfmG--REFEGI-LRISYLINPEG 123
Cdd:cd03015    84 PrkegglgKINFPLLADPKKKISRDY---------GvlDEEEGVaLRGTFIIDPEG 130
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 14-96 3.31e-18

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: 77.20  E-value: 3.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  14 NFHslkDYNG-KWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAE------KFKLNFPLLS 86
Cdd:cd03016    18 KFH---DYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEdieeytGVEIPFPIIA 94

                          90
                  ....*....|
gi 2315490305  87 DTSKEIIKKY 96
Cdd:cd03016    95 DPDREVAKLL 104
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 17-123 1.86e-17

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 75.27  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  17 SLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSH----KKFAEKF--KLNFPLLSDTSK 90
Cdd:PRK13190   21 DLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHiawlRDIEERFgiKIPFPVIADIDK 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2315490305  91 EIIKKYEAWGKKRfmgrefEGILRISYLINPEG 123
Cdd:PRK13190  101 ELAREYNLIDENS------GATVRGVFIIDPNQ 127
PRK13189 PRK13189
peroxiredoxin; Provisional
 20-96 1.40e-15

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 70.78  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  20 DYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLN------FPLLSDTSKEII 93
Cdd:PRK13189   32 DYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEWIKEKlgveieFPIIADDRGEIA 111


                  ...
gi 2315490305  94 KKY 96
Cdd:PRK13189  112 KKL 114
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
2-123 1.10e-14

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 68.53  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPD-QDNNFHSLK--DYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHK------ 72
Cdd:NF040737   41 KAPDFTAPAyYKGGFTNVKlsDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKmwndee 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2315490305  73 --KFAEKfKLNFPLLSDTSKEIIKKYEAWGkkrfmgrEFEGI-LRISYLINPEG 123
Cdd:NF040737  121 lsKMVTG-GVPFPMLSDGGGKIGKAYGVYD-------EAAGVdIRGRFIIDPDG 166
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 1-96 2.10e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 65.85  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   1 MKAIDFLLPD--QDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSH-KKFAEK 77
Cdd:pfam08534   4 DKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFvKRFWGK 83

                          90
                  ....*....|....*....
gi 2315490305  78 FKLNFPLLSDTSKEIIKKY 96
Cdd:pfam08534  84 EGLPFPFLSDGNAAFTKAL 102
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 19-123 1.79e-13

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


Pssm-ID: 211789  Cd Length: 187  Bit Score: 64.34  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  19 KDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKF----KLNFPLLSDTSKEIIK 94
Cdd:TIGR03137  27 EDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWHDTSeaigKITYPMLGDPTGVLTR 106

                          90       100       110
                  ....*....|....*....|....*....|
gi 2315490305  95 KYEAWgkkrfmgREFEGI-LRISYLINPEG 123
Cdd:TIGR03137 107 NFGVL-------IEEAGLaDRGTFVIDPEG 129
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 7-123 6.26e-13

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 63.39  E-value: 6.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   7 LLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFA--EKFK----- 79
Cdd:PTZ00253   20 LMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTlqERKKgglgt 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2315490305  80 LNFPLLSDTSKEIIKKYEAWGKKRfmGREFEGIlrisYLINPEG 123
Cdd:PTZ00253  100 MAIPMLADKTKSIARSYGVLEEEQ--GVAYRGL----FIIDPKG 137
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 2-98 1.12e-12

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: 61.87  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYN-GKWVLLYF------YPKDNTPGCTKEAcgfrdsfEELKKHNVVVLGVSADSVSSH--- 71
Cdd:cd02969     3 PAPDFSLPDTDGKTYSLADFAdGKALVVMFicnhcpYVKAIEDRLNRLA-------KEYGAKGVAVVAINSNDIEAYped 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2315490305  72 -----KKFAEKFKLNFPLLSDTSKEIIKKYEA 98
Cdd:cd02969    76 spenmKAKAKEHGYPFPYLLDETQEVAKAYGA 107
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-123 5.38e-12

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 59.32  E-value: 5.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   1 MKAI-----DFLLPDQDNNFHSLKDYNGKWVLLYFYpkdNT--PGCTKEAcgfrDSFEELKK--HNVVVLGVSAD-SVSS 70
Cdd:COG0526     1 MKAVgkpapDFTLTDLDGKPLSLADLKGKPVLVNFW---ATwcPPCRAEM----PVLKELAEeyGGVVFVGVDVDeNPEA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2315490305  71 HKKFAEKFKLNFPLLSDTSKEIIKKYeawgkkrfmgrefeGILRI--SYLINPEG 123
Cdd:COG0526    74 VKAFLKELGLPYPVLLDPDGELAKAY--------------GVRGIptTVLIDKDG 114
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 7-96 5.66e-12

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 61.50  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   7 LLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEK-------FK 79
Cdd:PTZ00137   82 LLNDDLVQFNSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWKELdvrqggvSP 161

                          90
                  ....*....|....*..
gi 2315490305  80 LNFPLLSDTSKEIIKKY 96
Cdd:PTZ00137  162 LKFPLFSDISREVSKSF 178
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
2-123 2.39e-11

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 58.48  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPgCTKEACGFRDSFEELKKHNVVVLGVSADSVS-SHKKFAEKFKL 80
Cdd:PRK03147   40 EAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKP-CEKEMPYMNELYPKYKEKGVEIIAVNVDETElAVKNFVNRYGL 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2315490305  81 NFPLLSDTSKEIIKKYEAwgkkrfmgrefeGILRISYLINPEG 123
Cdd:PRK03147  119 TFPVAIDKGRQVIDAYGV------------GPLPTTFLIDKDG 149
PRK13599 PRK13599
peroxiredoxin;
19-87 2.92e-11

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 58.96  E-value: 2.92e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2315490305  19 KDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLN------FPLLSD 87
Cdd:PRK13599   24 EDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNtniaipFPVIAD 98
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 5-123 7.20e-11

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: 56.09  E-value: 7.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   5 DFLLPDQDNNFHSLKDYNGKWVLLYFY-----PkdntpgCTKEAcgfrDSFEELKKH----NVVVLGVSADSVSSH--KK 73
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWaswcpP------CRAEM----PELEALAKEykddGVEVVGVNVDDDDPAavKA 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2315490305  74 FAEKFKLNFPLLSDTSKEIIKKYeawgkkrfmgrefeGILRI--SYLINPEG 123
Cdd:cd02966    71 FLKKYGITFPVLLDPDGELAKAY--------------GVRGLptTFLIDRDG 108
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 19-123 1.55e-10

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 56.53  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  19 KDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKF----KLNFPLLSDTSKEIIK 94
Cdd:PRK10382   27 KDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSetiaKIKYAMIGDPTGALTR 106

                          90       100       110
                  ....*....|....*....|....*....|
gi 2315490305  95 KYEAWgkkrfmgREFEGIL-RISYLINPEG 123
Cdd:PRK10382  107 NFDNM-------REDEGLAdRATFVVDPQG 129
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 20-95 2.61e-10

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 56.39  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  20 DYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAE------KFKLNFPLLSDTSKEII 93
Cdd:PRK13191   30 DYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMwieknlKVEVPFPIIADPMGNVA 109


                  ..
gi 2315490305  94 KK 95
Cdd:PRK13191  110 KR 111
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 2-103 4.54e-09

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: 51.98  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNG-KWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKL 80
Cdd:cd02970     1 TAPDFELPDAGGETVTLSALLGeGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEAFDKGKFL 80

                          90       100
                  ....*....|....*....|...
gi 2315490305  81 NFPLLSDTSKeiiKKYEAWGKKR 103
Cdd:cd02970    81 PFPVYADPDR---KLYRALGLVR 100
PRK15000 PRK15000
peroxiredoxin C;
14-123 2.69e-07

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 47.75  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305  14 NFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRDSFEELKKHNVVVLGVSADSVSSHKKFAEK-------FKLNFPLLS 86
Cdd:PRK15000   25 KFNFKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAWRNTpvdkggiGPVKYAMVA 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2315490305  87 DTSKEIIKKYeawgkkrfmGREF--EGI-LRISYLINPEG 123
Cdd:PRK15000  105 DVKREIQKAY---------GIEHpdEGVaLRGSFLIDANG 135
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 2-87 4.64e-06

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: 43.73  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEAcgfRDSFEELKKH-NVVVLGVSADSVSSHKKFAEKFKL 80
Cdd:cd03014     5 KAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQT---KRFNKEAAKLdNTVVLTISADLPFAQKRWCGAEGV 81


                  ....*...
gi 2315490305  81 -NFPLLSD 87
Cdd:cd03014    82 dNVTTLSD 89
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 5-123 2.85e-05

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: 41.43  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   5 DFLLPDQDNNFHSLKDYNGKWVLLYFypkdntpGCT--KEAC-----GFRDSFEELKKH---NVVVLGVS----ADSVSS 70
Cdd:cd02968     4 DFTLTDQDGRPVTLSDLKGKPVLVYF-------GYThcPDVCpttlaNLAQALKQLGADggdDVQVVFISvdpeRDTPEV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2315490305  71 HKKFAEKFKLNFPLLSDTSKEIIKKYEAWG---KKRFMGREFEGIL--RISYLINPEG 123
Cdd:cd02968    77 LKAYAKAFGPGWIGLTGTPEEIEALAKAFGvyyEKVPEDDGDYLVDhsAAIYLVDPDG 134
AhpC-TSA_2 pfam13911
AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide ...
 46-109 4.28e-05

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: 40.37  E-value: 4.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315490305  46 FRDSFEELKKHNVVVLGVSADSVSSHKKFAEKFKLNFPLLSDTSKEIikkYEAWGKKRFMGREF 109
Cdd:pfam13911   2 LSSLKPELDAAGIRLVAIGCGTPGRIEEFIKLTGFPFPVYVDPSRKL---YRALGLKRGLSGGL 62
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 8-123 2.47e-04

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 39.11  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315490305   8 LPDQDNNFHSLKDYNGKWVLLYF-YPKdntpgCTkEAC--------GFRDSFEELKKHNVVVLGVS----ADSVSSHKKF 74
Cdd:COG1999     5 LTDQDGKPVTLADLRGKPVLVFFgYTS-----CP-DVCpttlanlaQVQEALGEDGGDDVQVLFISvdpeRDTPEVLKAY 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2315490305  75 AEKFKL-NFPLLSDTSKEI---IKKYEAW-GKKRFMGREFEGILRIsYLINPEG 123
Cdd:COG1999    79 AEAFGApRWIGLTGDPEEIaalAKAFGVYyEKVPDGDYTFDHSAAV-YLVDPDG 131
tpx PRK00522
thiol peroxidase;
2-74 6.83e-04

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 37.96  E-value: 6.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315490305   2 KAIDFLLPDQDNNFHSLKDYNGKWVLLYFYPKDNTPGCTKEACGFRdsfEELKKH-NVVVLGVSADSVSSHKKF 74
Cdd:PRK00522   23 KAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFN---QEAAELdNTVVLCISADLPFAQKRF 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH