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Conserved domains on  [gi|170089117|ref|XP_001875781|]
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peroxiredoxin Q [Laccaria bicolor S238N-H82]

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

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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 ...
 9-134 2.30e-38

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: 127.66  E-value: 2.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   9 KPAPPITLKNYDGEDYTFTpGATGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAFVE 88
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLS-DLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEE---FKALGAVVIGVSPDSVESHAKFAE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 170089117  89 KERLTYPVLSDVDKEVFKTYGIPKG-MYGFVAVARVTFIVDKKGVVR 134
Cdd:cd03017   77 KYGLPFPLLSDPDGKLAKAYGVWGEkKKKYMGIERSTFLIDPDGKIV 123
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 9-134 2.30e-38

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: 127.66  E-value: 2.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   9 KPAPPITLKNYDGEDYTFTpGATGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAFVE 88
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLS-DLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEE---FKALGAVVIGVSPDSVESHAKFAE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 170089117  89 KERLTYPVLSDVDKEVFKTYGIPKG-MYGFVAVARVTFIVDKKGVVR 134
Cdd:cd03017   77 KYGLPFPLLSDPDGKLAKAYGVWGEkKKKYMGIERSTFLIDPDGKIV 123
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 7-136 2.05e-34

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: 117.33  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117    7 IGKPAPPITLKNYDGEDYTFTpGATGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAF 86
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLS-DYRGKWVVLFFYPADWTPVCTTELPALADLYEE---FKKLGVEVLGVSVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 170089117   87 VEKERLTYPVLSDVDKEVFKTYGIPKGMYGFvaVARVTFIVDKKGVVRDA 136
Cdd:pfam00578  77 AEKYGLPFPLLSDPDGEVARAYGVLNEEEGG--ALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
11-157 2.58e-30

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 107.26  E-value: 2.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  11 APPITLKNYDGEDYTFTpGATGLPTALFFYPeSGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAFVEKE 90
Cdd:COG1225    1 APDFTLPDLDGKTVSLS-DLRGKPVVLYFYA-TWCPGCTAELPELRDLYEE---FKDKGVEVLGVSSDSDEAHKKFAEKY 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170089117  91 RLTYPVLSDVDKEVFKTYGipkgmygfVAVARVTFIVDKKGVVRDALDATMNYGAHskfVEKWLDKL 157
Cdd:COG1225   76 GLPFPLLSDPDGEVAKAYG--------VRGTPTTFLIDPDGKIRYVWVGPVDPRPH---LEEVLEAL 131
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 8-133 3.50e-24

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 91.92  E-value: 3.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   8 GKPAPPITLKNYDGEDYTFTpGATGLPTALFFYPESGSMGCTRQACQFRDAiaeKDTFKPGKVQIIGISPDPVEKQKAFV 87
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLT-DFQGQRVLVYFYPKAMTPGCTVQACGLRDN---MDELKKAGVVVLGISTDKPEKLSRFA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 170089117  88 EKERLTYPVLSDVDKEVFKTYGI--PKGMYG--FVAVARVTFIVDKKGVV 133
Cdd:PRK09437  83 EKELLNFTLLSDEDHQVAEQFGVwgEKKFMGktYDGIHRISFLIDADGKI 132
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 9-134 2.30e-38

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: 127.66  E-value: 2.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   9 KPAPPITLKNYDGEDYTFTpGATGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAFVE 88
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLS-DLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEE---FKALGAVVIGVSPDSVESHAKFAE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 170089117  89 KERLTYPVLSDVDKEVFKTYGIPKG-MYGFVAVARVTFIVDKKGVVR 134
Cdd:cd03017   77 KYGLPFPLLSDPDGKLAKAYGVWGEkKKKYMGIERSTFLIDPDGKIV 123
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 7-136 2.05e-34

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: 117.33  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117    7 IGKPAPPITLKNYDGEDYTFTpGATGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAF 86
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLS-DYRGKWVVLFFYPADWTPVCTTELPALADLYEE---FKKLGVEVLGVSVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 170089117   87 VEKERLTYPVLSDVDKEVFKTYGIPKGMYGFvaVARVTFIVDKKGVVRDA 136
Cdd:pfam00578  77 AEKYGLPFPLLSDPDGEVARAYGVLNEEEGG--ALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
11-157 2.58e-30

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 107.26  E-value: 2.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  11 APPITLKNYDGEDYTFTpGATGLPTALFFYPeSGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAFVEKE 90
Cdd:COG1225    1 APDFTLPDLDGKTVSLS-DLRGKPVVLYFYA-TWCPGCTAELPELRDLYEE---FKDKGVEVLGVSSDSDEAHKKFAEKY 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170089117  91 RLTYPVLSDVDKEVFKTYGipkgmygfVAVARVTFIVDKKGVVRDALDATMNYGAHskfVEKWLDKL 157
Cdd:COG1225   76 GLPFPLLSDPDGEVAKAYG--------VRGTPTTFLIDPDGKIRYVWVGPVDPRPH---LEEVLEAL 131
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 10-134 1.84e-29

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: 104.94  E-value: 1.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  10 PAPPITLKNYDGEDYTFtPGATGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAFVEK 89
Cdd:cd02971    1 KAPDFTLPATDGGEVSL-SDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEE---FAKGGAEVLGVSVDSPFSHKAWAEK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 170089117  90 ER-LTYPVLSDVDKEVFKTYG--IPKGMYGFVAvARVTFIVDKKGVVR 134
Cdd:cd02971   77 EGgLNFPLLSDPDGEFAKAYGvlIEKSAGGGLA-ARATFIIDPDGKIR 123
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 8-133 3.50e-24

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 91.92  E-value: 3.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   8 GKPAPPITLKNYDGEDYTFTpGATGLPTALFFYPESGSMGCTRQACQFRDAiaeKDTFKPGKVQIIGISPDPVEKQKAFV 87
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLT-DFQGQRVLVYFYPKAMTPGCTVQACGLRDN---MDELKKAGVVVLGISTDKPEKLSRFA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 170089117  88 EKERLTYPVLSDVDKEVFKTYGI--PKGMYG--FVAVARVTFIVDKKGVV 133
Cdd:PRK09437  83 EKELLNFTLLSDEDHQVAEQFGVwgEKKFMGktYDGIHRISFLIDADGKI 132
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 7-134 2.88e-22

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: 86.94  E-value: 2.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   7 IGKPAPPITLKNYDGEDYTFTPGATGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAF 86
Cdd:cd03018    3 VGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLEL---FEAAGAEVLGISVDSPFSLRAW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 170089117  87 VEKERLTYPVLSD--VDKEVFKTYGIpkgMYGFVAVA-RVTFIVDKKGVVR 134
Cdd:cd03018   80 AEENGLTFPLLSDfwPHGEVAKAYGV---FDEDLGVAeRAVFVIDRDGIIR 127
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 7-134 1.24e-12

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: 62.14  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   7 IGKPAPPITLKNY--DGEDYTFTPGAT-GLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQ 83
Cdd:cd03015    1 VGKKAPDFKATAVvpNGEFKEISLSDYkGKWVVLFFYPLDFTFVCPTEIIAFSDRYEE---FKKLNAEVLGVSTDSHFSH 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 170089117  84 KAFVEKER-------LTYPVLSDVDKEVFKTYGIPKGMYGfvaVA-RVTFIVDKKGVVR 134
Cdd:cd03015   78 LAWRNTPRkegglgkINFPLLADPKKKISRDYGVLDEEEG---VAlRGTFIIDPEGIIR 133
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 8-134 2.57e-12

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 60.85  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117    8 GKPAPPITLKNYDGEDYTFTPGA-TGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEK-QKA 85
Cdd:pfam08534   3 GDKAPDFTLPDAATDGNTVSLSDfKGKKVVLNFWPGAFCPTCSAEHPYLEKLNEL---YKEKGVDVVAVNSDNDAFfVKR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 170089117   86 FVEKERLTYPVLSDVDKEVFKTYG--IPKGMYGFVAvARVTFIVDKKGVVR 134
Cdd:pfam08534  80 FWGKEGLPFPFLSDGNAAFTKALGlpIEEDASAGLR-SPRYAVIDEDGKVV 129
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 10-113 3.53e-11

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: 57.75  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  10 PAPPITLKNYDGEDYTFTPGATGLPTALFFYPESGSMGCTRQAcqfRDAIAEKDTFKPGKVQIIGISPDPVEKQKAFVEK 89
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYL---RALSKLLPELDALGVELVAVGPESPEKLEAFDKG 77

                         90       100
                 ....*....|....*....|....
gi 170089117  90 ERLTYPVLSDVDKEVFKTYGIPKG 113
Cdd:cd02970   78 KFLPFPVYADPDRKLYRALGLVRS 101
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
5-134 7.37e-11

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 57.78  E-value: 7.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   5 SLIGKPAPPITLKNYDG--------EDYTftpgatGLPTALFFYP---------ESGSMgctrqacqfrdaiAEK-DTFK 66
Cdd:COG0450    3 PLIGDKAPDFTAEATHGgefkkislSDYK------GKWVVLFFHPadftfvcptELGAF-------------AKRyEEFK 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170089117  67 PGKVQIIGISPDPVEKQKAFVEKER-------LTYPVLSDVDKEVFKTYGI--PKGMygfVAVaRVTFIVDKKGVVR 134
Cdd:COG0450   64 KLGVEVIGLSVDSVFSHKAWHETIKekggivkIKFPIIADPTGKIARAYGMlhPEDG---VAV-RGVFIIDPDGKIR 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 7-156 1.09e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 53.93  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   7 IGKPAPPITLKNYDGEDYTFTpGATGLPTALFFYpesgSMGCTrqACqfrdaIAEKDTF-----KPGKVQIIGISPD-PV 80
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLA-DLKGKPVLVNFW----ATWCP--PC-----RAEMPVLkelaeEYGGVVFVGVDVDeNP 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170089117  81 EKQKAFVEKERLTYPVLSDVDKEVFKTYG---IPkgmygfvavarVTFIVDKKGVVRDALDATMNYGAHSKFVEKWLDK 156
Cdd:COG0526   72 EAVKAFLKELGLPYPVLLDPDGELAKAYGvrgIP-----------TTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 62-134 7.67e-09

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: 51.08  E-value: 7.67e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170089117  62 KDTFKPGKVQIIGIS--PDPVEKQKAFVEKERLTYPVLSDVDKEVFKTYGipkgmygfVAVARVTFIVDKKGVVR 134
Cdd:cd02966   45 AKEYKDDGVEVVGVNvdDDDPAAVKAFLKKYGITFPVLLDPDGELAKAYG--------VRGLPTTFLIDRDGRIR 111
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 70-143 9.30e-07

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: 46.76  E-value: 9.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  70 VQIIGISPDPVEKQKAFVE------KERLTYPVLSDVDKEVFKTYG-IPKGMYGFVAVaRVTFIVDKKGVVRdaldATMN 142
Cdd:cd03016   60 VKLIGLSVDSVESHIKWIEdieeytGVEIPFPIIADPDREVAKLLGmIDPDAGSTLTV-RAVFIIDPDKKIR----LILY 134


                 .
gi 170089117 143 Y 143
Cdd:cd03016  135 Y 135
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 5-134 1.59e-06

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 46.48  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   5 SLIGKPAPPI--------TLKNYDGEDYTftPGATGLptaLFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGIS 76
Cdd:PTZ00137  68 SLVGKLMPSFkgtallndDLVQFNSSDYF--KDSYGL---LVFYPLDFTFVCPSELLGFSERLKE---FEERGVKVLGVS 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170089117  77 PDPVEKQKAFVEKE-------RLTYPVLSDVDKEVFKTYGIPKGMyGFVAvaRVTFIVDKKGVVR 134
Cdd:PTZ00137 140 VDSPFSHKAWKELDvrqggvsPLKFPLFSDISREVSKSFGLLRDE-GFSH--RASVLVDKAGVVK 201
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 7-134 5.54e-06

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 44.51  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   7 IGKPAPPItlknydgEDYTFTPGAT----------GLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGIS 76
Cdd:PTZ00253   8 INHPAPSF-------EEVALMPNGSfkkislssykGKWVVLFFYPLDFTFVCPTEIIQFSDSVKR---FNELNCEVLACS 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170089117  77 PDPVEKQKAFVEKER-------LTYPVLSDVDKEVFKTYGIPKGMYGfVAVaRVTFIVDKKGVVR 134
Cdd:PTZ00253  78 MDSEYAHLQWTLQERkkgglgtMAIPMLADKTKSIARSYGVLEEEQG-VAY-RGLFIIDPKGMLR 140
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 9-134 2.30e-05

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: 41.79  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   9 KPAPPITLKNYDGEDYTFTPGA-TGLPTALFFYpesGSMgCTrqACQ----FRDAIAEKdtfkpGKVQIIGIS-PDPVEK 82
Cdd:cd03010    1 KPAPAFSLPALPGPDKTLTSADlKGKPYLLNVW---ASW-CA--PCReehpVLMALARQ-----GRVPIYGINyKDNPEN 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 170089117  83 QKAFVEKERLTY-PVLSDVDKEVfktyGIPKGMYGfvavARVTFIVDKKGVVR 134
Cdd:cd03010   70 ALAWLARHGNPYaAVGFDPDGRV----GIDLGVYG----VPETFLIDGDGIIR 114
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 13-134 2.63e-05

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 42.53  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  13 PITLKNYDGEdYTFtpgatglptaLFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPVEKQKAFVE--KE 90
Cdd:PRK13190  19 PIDLSKYKGK-WVL----------LFSHPADFTPVCTTEFIAFSRRYED---FKKLGVELVGLSVDSIYSHIAWLRdiEE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 170089117  91 R----LTYPVLSDVDKEVFKTYGIPKGMYGfvAVARVTFIVDKKGVVR 134
Cdd:PRK13190  85 RfgikIPFPVIADIDKELAREYNLIDENSG--ATVRGVFIIDPNQIVR 130
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 8-134 8.50e-05

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 40.69  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   8 GKPAPPITLKNYDGEDYTFTPGATGLPTALFFYpesgsmgCTRqaCQFRDAIAEK-----DTFKPGKVQIIGISPDPVEK 82
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFI-------CNH--CPYVKAIEDRlnrlaKEYGAKGVAVVAINSNDIEA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170089117  83 Q--------KAFVEKERLTYPVLSDVDKEVFKTYGipkgmygfvavARVT---FIVDKKGVVR 134
Cdd:cd02969   72 YpedspenmKAKAKEHGYPFPYLLDETQEVAKAYG-----------AACTpdfFLFDPDGKLV 123
PRK13599 PRK13599
peroxiredoxin;
6-134 3.61e-03

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 36.62  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117   6 LIGKPAPPITLKNYDG-----EDYTftpgatGLPTALFFYPESGSMGCTRQACQFRDAIAEkdtFKPGKVQIIGISPDPV 80
Cdd:PRK13599   3 LLGEKFPSMEVVTTQGvkrlpEDYA------GKWFVLFSHPADFTPVCTTEFVEFARKAND---FKELNTELIGLSVDQV 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  81 EKQKAFVE------KERLTYPVLSDVDKEVFKTYGIPKGMYGFVAVaRVTFIVDKKGVVR 134
Cdd:PRK13599  74 FSHIKWVEwikdntNIAIPFPVIADDLGKVSNQLGMIHPGKGTNTV-RAVFIVDDKGTIR 132
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
65-141 6.54e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 35.36  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170089117  65 FKPGKVQIIGISPDPVE-KQKAFVEKERLTYPVLSDVDKEVFKTYGI---PkgmygfvavarVTFIVDKKGVVRDALDAT 140
Cdd:PRK03147  90 YKEKGVEIIAVNVDETElAVKNFVNRYGLTFPVAIDKGRQVIDAYGVgplP-----------TTFLIDKDGKVVKVITGE 158


                 .
gi 170089117 141 M 141
Cdd:PRK03147 159 M 159
 
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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