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Conserved domains on  [gi|15230982|ref|NP_189235|]
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Thioredoxin superfamily protein [Arabidopsis thaliana]

Protein Classification

Thioredoxin_like and PRX_BCP domain-containing protein( domain architecture ID 10221596)

Thioredoxin_like and PRX_BCP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 73-211 5.97e-69

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: 207.40  E-value: 5.97e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  73 QAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKL 152
Cdd:cd03017   1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230982 153 PYTLLSDEGNKVRKDWGVPGDLFGALPG--RQTYVLDKNGVVQLIYNNqFQPEKHIDETLK 211
Cdd:cd03017  81 PFPLLSDPDGKLAKAYGVWGEKKKKYMGieRSTFLIDPDGKIVKVWRK-VKPKGHAEEVLE 140
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 1-133 1.95e-03

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member PLN02399:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 236  Bit Score: 37.96  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982    1 MAASSSSFTL--CNHTTLRTLPLRKTLVTKTQFSvpTKSSESNFFGSTLTHSSYISPVSSSSLK-GLIFAKVNKGQAAPD 77
Cdd:PLN02399   4 LTTSSSSYASfkTVFNSSPPPPSMAFLVPSLKSS--TGISKSAFLSNGFSLKSPNSPGFLSKSRsFGVYARAATEKSVHD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230982   78 FTLKDQNGKPVSLKKYKGKPvVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVI 133
Cdd:PLN02399  82 FTVKDIDGKDVALSKFKGKV-LLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEIL 136
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 73-211 5.97e-69

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: 207.40  E-value: 5.97e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  73 QAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKL 152
Cdd:cd03017   1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230982 153 PYTLLSDEGNKVRKDWGVPGDLFGALPG--RQTYVLDKNGVVQLIYNNqFQPEKHIDETLK 211
Cdd:cd03017  81 PFPLLSDPDGKLAKAYGVWGEKKKKYMGieRSTFLIDPDGKIVKVWRK-VKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
75-216 3.07e-57

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 177.36  E-value: 3.07e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  75 APDFTLKDQNGKPVSLKKYKGKPVVLYFYpADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKLPY 154
Cdd:COG1225   1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230982 155 TLLSDEGNKVRKDWGVPGdlfgalpGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKAA 216
Cdd:COG1225  80 PLLSDPDGEVAKAYGVRG-------TPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLAE 134
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 72-195 3.20e-56

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: 174.33  E-value: 3.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982    72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYK 151
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15230982   152 LPYTLLSDEGNKVRKDWGVPGDLFGaLPGRQTYVLDKNGVVQLI 195
Cdd:pfam00578  82 LPFPLLSDPDGEVARAYGVLNEEEG-GALRATFVIDPDGKVRYI 124
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 72-214 1.77e-36

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 125.05  E-value: 1.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYK 151
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAEKEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  152 LPYTLLSDEGNKVRKDWGVPGD-------LFGAlpGRQTYVLDKNGVVQLIYNNqFQPEKHIDETLKFLK 214
Cdd:PRK09437  87 LNFTLLSDEDHQVAEQFGVWGEkkfmgktYDGI--HRISFLIDADGKIEHVFDK-FKTSNHHDVVLDYLK 153
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 1-133 1.95e-03

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 37.96  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982    1 MAASSSSFTL--CNHTTLRTLPLRKTLVTKTQFSvpTKSSESNFFGSTLTHSSYISPVSSSSLK-GLIFAKVNKGQAAPD 77
Cdd:PLN02399   4 LTTSSSSYASfkTVFNSSPPPPSMAFLVPSLKSS--TGISKSAFLSNGFSLKSPNSPGFLSKSRsFGVYARAATEKSVHD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230982   78 FTLKDQNGKPVSLKKYKGKPvVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVI 133
Cdd:PLN02399  82 FTVKDIDGKDVALSKFKGKV-LLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEIL 136
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 73-211 5.97e-69

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: 207.40  E-value: 5.97e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  73 QAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKL 152
Cdd:cd03017   1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230982 153 PYTLLSDEGNKVRKDWGVPGDLFGALPG--RQTYVLDKNGVVQLIYNNqFQPEKHIDETLK 211
Cdd:cd03017  81 PFPLLSDPDGKLAKAYGVWGEKKKKYMGieRSTFLIDPDGKIVKVWRK-VKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
75-216 3.07e-57

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 177.36  E-value: 3.07e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  75 APDFTLKDQNGKPVSLKKYKGKPVVLYFYpADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKLPY 154
Cdd:COG1225   1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230982 155 TLLSDEGNKVRKDWGVPGdlfgalpGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKAA 216
Cdd:COG1225  80 PLLSDPDGEVAKAYGVRG-------TPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLAE 134
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 72-195 3.20e-56

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: 174.33  E-value: 3.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982    72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYK 151
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15230982   152 LPYTLLSDEGNKVRKDWGVPGDLFGaLPGRQTYVLDKNGVVQLI 195
Cdd:pfam00578  82 LPFPLLSDPDGEVARAYGVLNEEEG-GALRATFVIDPDGKVRYI 124
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 75-211 5.66e-54

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: 169.27  E-value: 5.66e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  75 APDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKY-KLP 153
Cdd:cd02971   2 APDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEgGLN 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982 154 YTLLSDEGNKVRKDWGVPGDL--FGALPGRQTYVLDKNGVVQLIYNNqFQPEKHIDETLK 211
Cdd:cd02971  82 FPLLSDPDGEFAKAYGVLIEKsaGGGLAARATFIIDPDGKIRYVEVE-PLPTGRNAEELL 140
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 69-211 7.21e-43

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: 141.26  E-value: 7.21e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  69 VNKGQAAPDFTLKDQNGKPVSLKKYKG-KPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFA 147
Cdd:cd03018   1 LEVGDKAPDFELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230982 148 SKYKLPYTLLSDEGNK--VRKDWGVPGDLFGaLPGRQTYVLDKNGVVQL-IYNNQFQP--EKHIDETLK 211
Cdd:cd03018  81 EENGLTFPLLSDFWPHgeVAKAYGVFDEDLG-VAERAVFVIDRDGIIRYaWVSDDGEPrdLPDYDEALD 148
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 72-214 1.77e-36

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 125.05  E-value: 1.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYK 151
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFAEKEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  152 LPYTLLSDEGNKVRKDWGVPGD-------LFGAlpGRQTYVLDKNGVVQLIYNNqFQPEKHIDETLKFLK 214
Cdd:PRK09437  87 LNFTLLSDEDHQVAEQFGVWGEkkfmgktYDGI--HRISFLIDADGKIEHVFDK-FKTSNHHDVVLDYLK 153
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
72-216 2.32e-29

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 108.24  E-value: 2.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  72 GQAAPDFTL---KDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAF-- 146
Cdd:COG0450   6 GDKAPDFTAeatHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWhe 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982 147 ASKY-----KLPYTLLSDEGNKVRKDWGV--PGDlfgALPGRQTYVLDKNGVVQLI-YN------NqfqpekhIDETLKF 212
Cdd:COG0450  86 TIKEkggivKIKFPIIADPTGKIARAYGMlhPED---GVAVRGVFIIDPDGKIRAIeVYplsvgrN-------VDEILRV 155


                ....
gi 15230982 213 LKAA 216
Cdd:COG0450 156 VDAL 159
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 72-216 1.78e-28

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: 105.28  E-value: 1.78e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  72 GQAAPDFT----LKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFA 147
Cdd:cd03015   2 GKKAPDFKatavVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAWR 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230982 148 SKY-------KLPYTLLSDEGNKVRKDWGVPGDLFG-ALPGrqTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKAA 216
Cdd:cd03015  82 NTPrkegglgKINFPLLADPKKKISRDYGVLDEEEGvALRG--TFIIDPEGIIRHITVNDLPVGRSVDETLRVLDAL 156
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 72-192 6.07e-27

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 100.52  E-value: 6.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982    72 GQAAPDFTLKD--QNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGI-SGDDSASHKAFAS 148
Cdd:pfam08534   3 GDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVnSDNDAFFVKRFWG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15230982   149 KYKLPYTLLSDEGNKVRKDWGVP--GDLFGALPGRQTYVLDKNGVV 192
Cdd:pfam08534  83 KEGLPFPFLSDGNAAFTKALGLPieEDASAGLRSPRYAVIDEDGKV 128
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 72-192 3.15e-23

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 90.52  E-value: 3.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYpADETPGCTKQACAFRDSYEKFKkaGAEVIGISGDDS-ASHKAFASKY 150
Cdd:COG0526   5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFW-ATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDENpEAVKAFLKEL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15230982 151 KLPYTLLSDEGNKVRKDWGVPGdlfgaLPgrQTYVLDKNGVV 192
Cdd:COG0526  82 GLPYPVLLDPDGELAKAYGVRG-----IP--TTVLIDKDGKI 116
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 69-216 3.80e-22

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 89.53  E-value: 3.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   69 VNKGQAAPDFTLKDQNGkPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAF-- 146
Cdd:PRK13190   2 VKLGQKAPDFTVNTTKG-PIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWlr 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230982  147 --ASKY--KLPYTLLSDEGNKVRKDWGVPGDLFGALPgRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKAA 216
Cdd:PRK13190  81 diEERFgiKIPFPVIADIDKELAREYNLIDENSGATV-RGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKAL 153
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 77-192 1.24e-21

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: 85.75  E-value: 1.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  77 DFTLKDQNGKPVSLKKYKGKPVVLYFYpADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASH--KAFASKYKLPY 154
Cdd:cd02966   1 DFSLPDLDGKPVSLSDLKGKVVLVNFW-ASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFLKKYGITF 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15230982 155 TLLSDEGNKVRKDWGVPGdlfgaLPGrqTYVLDKNGVV 192
Cdd:cd02966  80 PVLLDPDGELAKAYGVRG-----LPT--TFLIDRDGRI 110
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 67-215 1.63e-16

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 74.56  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   67 AKVNkgQAAPDFT----LKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSAS 142
Cdd:PTZ00253   6 AKIN--HPAPSFEevalMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  143 HKAFASKYK-------LPYTLLSDEGNKVRKDWGVPGDLFGaLPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKA 215
Cdd:PTZ00253  84 HLQWTLQERkkgglgtMAIPMLADKTKSIARSYGVLEEEQG-VAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEA 162
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 75-196 1.67e-16

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: 73.16  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  75 APDFTLKDQNGKPVSLKK-YKGKPVVLYFY-----PAdetpgCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFAS 148
Cdd:cd02970   2 APDFELPDAGGETVTLSAlLGEGPVVVVFYrgfgcPF-----CREYLRALSKLLPELDALGVELVAVGPESPEKLEAFDK 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230982 149 KYKLPYTLLSDEGNKVRKDWGV-------------------------PGDLFgALPGrqTYVLDKNGVVQLIY 196
Cdd:cd02970  77 GKFLPFPVYADPDRKLYRALGLvrslpwsntpralwknaaigfrgndEGDGL-QLPG--VFVIGPDGTILFAH 146
PRK15000 PRK15000
peroxiredoxin C;
73-215 1.01e-15

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 72.40  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   73 QAAPDFTLKD--QNGKPVSLKKYK----GKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAF 146
Cdd:PRK15000   6 RQAPDFTAAAvlGSGEIVDKFNFKqhtnGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHNAW 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230982  147 ASKY-------KLPYTLLSDEGNKVRKDWGVPGDLFGaLPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKA 215
Cdd:PRK15000  86 RNTPvdkggigPVKYAMVADVKREIQKAYGIEHPDEG-VALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 72-195 1.61e-15

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: 71.80  E-value: 1.61e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  72 GQAAPDFTLKDQNGkPVSLKKYKG-KPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFA--- 147
Cdd:cd03016   2 GDTAPNFEADTTHG-PIKFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIedi 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230982 148 ---SKYKLPYTLLSDEGNKVRKDWG-VPGDLFGALPGRQTYVLDKNGVVQLI 195
Cdd:cd03016  81 eeyTGVEIPFPIIADPDREVAKLLGmIDPDAGSTLTVRAVFIIDPDKKIRLI 132
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 72-216 3.03e-15

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: 70.35  E-value: 3.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  72 GQAAPDFTLKDQNGKPVSLKKY-KGKPVVLYFYpadetpgCTKqaCAFRDSYEK--------FKKAGAEVIGISGDDSAS 142
Cdd:cd02969   1 GSPAPDFSLPDTDGKTYSLADFaDGKALVVMFI-------CNH--CPYVKAIEDrlnrlakeYGAKGVAVVAINSNDIEA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982 143 H--------KAFASKYKLPYTLLSDEGNKVRKdwgvpgdLFGALPGRQTYVLDKNGvvQLIYNNQF---QPEKHIDETLK 211
Cdd:cd02969  72 YpedspenmKAKAKEHGYPFPYLLDETQEVAK-------AYGAACTPDFFLFDPDG--KLVYRGRIddsRPGNDPPVTGR 142


                ....*
gi 15230982 212 FLKAA 216
Cdd:cd02969 143 DLRAA 147
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
68-195 3.44e-15

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 70.42  E-value: 3.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   68 KVNKGQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYpADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSA-SHKAF 146
Cdd:PRK03147  34 KVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFW-GTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETElAVKNF 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15230982  147 ASKYKLPYTLLSDEGNKVRKDWGVpgdlfGALPgrQTYVLDKNG-VVQLI 195
Cdd:PRK03147 113 VNRYGLTFPVAIDKGRQVIDAYGV-----GPLP--TTFLIDKDGkVVKVI 155
PRK13599 PRK13599
peroxiredoxin;
72-215 3.68e-15

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 71.28  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYK 151
Cdd:PRK13599   5 GEKFPSMEVVTTQGVKRLPEDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIK 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230982  152 ------LPYTLLSDEGNKVRKDWGV--PGDlfGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKA 215
Cdd:PRK13599  85 dntniaIPFPVIADDLGKVSNQLGMihPGK--GTNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKA 154
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 72-215 8.27e-15

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 70.26  E-value: 8.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFAS--- 148
Cdd:PRK13191  10 GEKFPEMEVITTHGKIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMwie 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  149 ---KYKLPYTLLSDEGNKVRKDWGVPGDLFGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKA 215
Cdd:PRK13191  90 knlKVEVPFPIIADPMGNVAKRLGMIHAESSTATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRA 159
PRK13189 PRK13189
peroxiredoxin; Provisional
 72-215 1.00e-14

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 70.01  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   72 GQAAPDFTLKDQNGkPVSLKK-YKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFAS-- 148
Cdd:PRK13189  12 GDKFPEFEVKTTHG-PIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEwi 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230982  149 KYKL----PYTLLSDEGNKVRKDWGV--PGDlfGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKA 215
Cdd:PRK13189  91 KEKLgveiEFPIIADDRGEIAKKLGMisPGK--GTNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKA 161
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 83-195 2.36e-12

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 63.08  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   83 QNGK--PVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKY----KLPYTL 156
Cdd:PRK10382  17 KNGEfiEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSetiaKIKYAM 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15230982  157 LSDEGNKVRKDWGVPGDLFGaLPGRQTYVLDKNGVVQLI 195
Cdd:PRK10382  97 IGDPTGALTRNFDNMREDEG-LADRATFVVDPQGIIQAI 134
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 72-192 7.01e-11

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: 57.98  E-value: 7.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  72 GQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKkaGAEVIGISGDDSASHKAFASKYK 151
Cdd:cd03014   3 GDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWCGAEG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230982 152 LP-YTLLSDEGNKV-RKDWGVP-GDLFgaLPGRQTYVLDKNGVV 192
Cdd:cd03014  81 VDnVTTLSDFRDHSfGKAYGVLiKDLG--LLARAVFVIDENGKV 122
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-216 1.09e-10

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 58.18  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  69 VNKGQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQAcafrdsyEKFKKAGAE-----VIGISGDDSASH 143
Cdd:COG2077  18 PKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATST-------RKFNEEAAKldnvvVLTISADLPFAQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982 144 KAFASKYKLP-YTLLSD-EGNKVRKDWGV---PGDLFGaLPGRQTYVLDKNGVVqlIYnNQFQPEkhI------DETLKF 212
Cdd:COG2077  91 KRFCGAEGIDnVVTLSDfRDRSFGKDYGVlikEGPLLG-LLARAVFVLDENGKV--VY-TELVPE--ItdepdyDAALAA 164


                ....
gi 15230982 213 LKAA 216
Cdd:COG2077 165 LKAL 168
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 79-215 3.74e-10

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 56.45  E-value: 3.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  79 TLKDQNGKPVSLKKYKGKPVVLYF-YPAdetpgCTkQAC-----AFRDSYEKFKKAGAE---VIGISGD---DSASH-KA 145
Cdd:COG1999   4 TLTDQDGKPVTLADLRGKPVLVFFgYTS-----CP-DVCpttlaNLAQVQEALGEDGGDdvqVLFISVDperDTPEVlKA 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230982 146 FASKYKLP-YTLLS---DEGNKVRKDWGV-----PGDLFGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKA 215
Cdd:COG1999  78 YAEAFGAPrWIGLTgdpEEIAALAKAFGVyyekvPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
tpx PRK00522
thiol peroxidase;
69-192 3.02e-09

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 54.14  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   69 VNKGQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQAcafrdsyEKFKKAGAE-----VIGISGDDSASH 143
Cdd:PRK00522  18 PQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSV-------RKFNQEAAEldntvVLCISADLPFAQ 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15230982  144 KAFASKYKLP-YTLLSD-EGNKVRKDWGV---PGDLFGaLPGRQTYVLDKNGVV 192
Cdd:PRK00522  91 KRFCGAEGLEnVITLSDfRDHSFGKAYGVaiaEGPLKG-LLARAVFVLDENNKV 143
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 75-102 2.36e-08

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: 51.06  E-value: 2.36e-08
                        10        20
                ....*....|....*....|....*...
gi 15230982  75 APDFTLKDQNGKPVSLKKYKGKPVVLYF 102
Cdd:cd02968   2 GPDFTLTDQDGRPVTLSDLKGKPVLVYF 29
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 99-215 1.65e-07

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 50.33  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   99 VLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAF---------ASKYKLPytLLSDEGNKVRKDWG 169
Cdd:PTZ00137 102 LLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWkeldvrqggVSPLKFP--LFSDISREVSKSFG 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15230982  170 VPGDlfGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKA 215
Cdd:PTZ00137 180 LLRD--EGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDA 223
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 76-193 1.01e-06

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 46.14  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  76 PDFTLKDQNGKPVSLKKYKGKPVVLYFYpadeTPGCTkqAC--------AFRDSYekfkkagaEVIGI---SGDDSAShK 144
Cdd:cd03011   1 PLFTATTLDGEQFDLESLSGKPVLVYFW----ATWCP--VCrftsptvnQLAADY--------PVVSValrSGDDGAV-A 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15230982 145 AFASKYKLPYTLLSDEGNKVRKDWGVPgdlfgALPGrqTYVLDKNGVVQ 193
Cdd:cd03011  66 RFMQKKGYGFPVINDPDGVISARWGVS-----VTPA--IVIVDPGGIVF 107
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 75-192 3.39e-06

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 44.88  E-value: 3.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  75 APDFTLK--DQNGKPVSLKKYKGKPVVLYFYP------ADETPGCTKQAcafrdsyekfKKAGAEVIGIS-GDDSASHKA 145
Cdd:cd03010   3 APAFSLPalPGPDKTLTSADLKGKPYLLNVWAswcapcREEHPVLMALA----------RQGRVPIYGINyKDNPENALA 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15230982 146 FASKYKLPYTL-LSDEGNKVRKDWGVPGdlfgaLPgrQTYVLDKNGVV 192
Cdd:cd03010  73 WLARHGNPYAAvGFDPDGRVGIDLGVYG-----VP--ETFLIDGDGII 113
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 76-102 1.03e-04

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 40.63  E-value: 1.03e-04
                          10        20
                  ....*....|....*....|....*..
gi 15230982    76 PDFTLKDQNGKPVSLKKYKGKPVVLYF 102
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFF 28
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 95-192 1.36e-04

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 39.60  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982    95 GKPVVLYFYpADETPGCTKQACAFRDSYEKFKKA-GAEVIGISGDDSASH-KAFASKYKLPYTLL---SDEGNKVRKDWG 169
Cdd:pfam13905   1 GKVVLLYFG-ASWCKPCRRFTPLLKELYEKLKKKkNVEIVFVSLDRDLEEfKDYLKKMPKDWLSVpfdDDERNELKRKYG 79

                          90       100
                  ....*....|....*....|...
gi 15230982   170 VPGdlfgaLPgrQTYVLDKNGVV 192
Cdd:pfam13905  80 VNA-----IP--TLVLLDPNGEV 95
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 77-134 2.60e-04

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 39.81  E-value: 2.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  77 DFTLKDQNGKPVSLKKYKGKpVVLYFYPAdetPGC--TKQACAFRDSYEKFKKAGAEVIG 134
Cdd:cd00340   4 DFSVKDIDGEPVSLSKYKGK-VLLIVNVA---SKCgfTPQYEGLEALYEKYKDRGLVVLG 59
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 80-172 1.11e-03

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 37.65  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982  80 LKDQNGKPVSLKKYKGKPVVLYFyPADETPGCtkqaCAF----RDSYEKFKKAGA--EVIGISGD-DSASHKAFASK--- 149
Cdd:cd03009   3 LLRNDGGKVPVSSLEGKTVGLYF-SASWCPPC----RAFtpklVEFYEKLKESGKnfEIVFISWDrDEESFNDYFSKmpw 77

                        90       100
                ....*....|....*....|...
gi 15230982 150 YKLPYTlLSDEGNKVRKDWGVPG 172
Cdd:cd03009  78 LAVPFS-DRERRSRLNRTFKIEG 99
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 1-133 1.95e-03

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 37.96  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982    1 MAASSSSFTL--CNHTTLRTLPLRKTLVTKTQFSvpTKSSESNFFGSTLTHSSYISPVSSSSLK-GLIFAKVNKGQAAPD 77
Cdd:PLN02399   4 LTTSSSSYASfkTVFNSSPPPPSMAFLVPSLKSS--TGISKSAFLSNGFSLKSPNSPGFLSKSRsFGVYARAATEKSVHD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230982   78 FTLKDQNGKPVSLKKYKGKPvVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVI 133
Cdd:PLN02399  82 FTVKDIDGKDVALSKFKGKV-LLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEIL 136
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 80-143 2.04e-03

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 37.21  E-value: 2.04e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230982  80 LKDQNGKpVSLKKYKGKPVVLYFyPADETPGC---TKQACAFrdsYEKFKKAGA--EVIGISGDDSASH 143
Cdd:cd02964   3 LLDGEGV-VPVSALEGKTVGLYF-SASWCPPCrafTPKLVEF---YEKLKEEGKnfEIVFVSRDRSEES 66
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 68-158 8.87e-03

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 35.98  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230982   68 KVNKGQAAP---DFTLKDQNGKPVSLKKYKGKpVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISG------- 137
Cdd:PTZ00056   9 TVSKDELRKsiyDYTVKTLEGTTVPMSSLKNK-VLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTsqflnqe 87

                         90       100
                 ....*....|....*....|..
gi 15230982  138 -DDSASHKAFASKYKLPYTLLS 158
Cdd:PTZ00056  88 fPNTKDIRKFNDKNKIKYNFFE 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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