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Conserved domains on  [gi|495777056|ref|WP_008501635|]
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MULTISPECIES: thioredoxin-dependent thiol peroxidase [Enterobacter]

Protein Classification

peroxiredoxin( domain architecture ID 10793262)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 1-154 4.61e-127

thioredoxin-dependent thiol peroxidase; Reviewed


:

Pssm-ID: 181857  Cd Length: 154  Bit Score: 352.32  E-value: 4.61e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   1 MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSR 80
Cdd:PRK09437   1 MNPLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777056  81 FAEKELLNFTLLSDEDHQVCEQFGVWGEKTFMGKTYDGIHRISFLIDADGKVEHVFDDFKTSNHHDVVLNWLKE 154
Cdd:PRK09437  81 FAEKELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLDYLKE 154
 
Name Accession Description Interval E-value
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 1-154 4.61e-127

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 352.32  E-value: 4.61e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   1 MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSR 80
Cdd:PRK09437   1 MNPLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777056  81 FAEKELLNFTLLSDEDHQVCEQFGVWGEKTFMGKTYDGIHRISFLIDADGKVEHVFDDFKTSNHHDVVLNWLKE 154
Cdd:PRK09437  81 FAEKELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLDYLKE 154
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 8-150 8.05e-73

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: 214.72  E-value: 8.05e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   8 DIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKELL 87
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777056  88 NFTLLSDEDHQVCEQFGVWGEKTfmgKTYDGIHRISFLIDADGKVEHVFDDFKTSNHHDVVLN 150
Cdd:cd03017   81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 7-135 1.34e-51

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: 160.47  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056    7 GDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKEL 86
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 495777056   87 LNFTLLSDEDHQVCEQFGVWGEKtfmgktYDGIHRISFLIDADGKVEHV 135
Cdd:pfam00578  82 LPFPLLSDPDGEVARAYGVLNEE------EGGALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
10-152 2.12e-51

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 160.42  E-value: 2.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  10 APKFSLPDQDGEQVNLTDFQGQRVLVYFYpKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKELLNF 89
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777056  90 TLLSDEDHQVCEQFGVWGEktfmgktydgihRISFLIDADGKVEHVF-DDFKTSNHHDVVLNWL 152
Cdd:COG1225   80 PLLSDPDGEVAKAYGVRGT------------PTTFLIDPDGKIRYVWvGPVDPRPHLEEVLEAL 131
 
Name Accession Description Interval E-value
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 1-154 4.61e-127

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 352.32  E-value: 4.61e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   1 MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSR 80
Cdd:PRK09437   1 MNPLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777056  81 FAEKELLNFTLLSDEDHQVCEQFGVWGEKTFMGKTYDGIHRISFLIDADGKVEHVFDDFKTSNHHDVVLNWLKE 154
Cdd:PRK09437  81 FAEKELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLDYLKE 154
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 8-150 8.05e-73

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: 214.72  E-value: 8.05e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   8 DIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKELL 87
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777056  88 NFTLLSDEDHQVCEQFGVWGEKTfmgKTYDGIHRISFLIDADGKVEHVFDDFKTSNHHDVVLN 150
Cdd:cd03017   81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 10-149 1.05e-51

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: 161.18  E-value: 1.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  10 APKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKEL-LN 88
Cdd:cd02971    2 APDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEGgLN 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495777056  89 FTLLSDEDHQVCEQFGVWGEKTFMgktYDGIHRISFLIDADGKVEHVFDDFKTSNHHDVVL 149
Cdd:cd02971   82 FPLLSDPDGEFAKAYGVLIEKSAG---GGLAARATFIIDPDGKIRYVEVEPLPTGRNAEEL 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 7-135 1.34e-51

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: 160.47  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056    7 GDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKEL 86
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 495777056   87 LNFTLLSDEDHQVCEQFGVWGEKtfmgktYDGIHRISFLIDADGKVEHV 135
Cdd:pfam00578  82 LPFPLLSDPDGEVARAYGVLNEE------EGGALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
10-152 2.12e-51

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 160.42  E-value: 2.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  10 APKFSLPDQDGEQVNLTDFQGQRVLVYFYpKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKELLNF 89
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777056  90 TLLSDEDHQVCEQFGVWGEktfmgktydgihRISFLIDADGKVEHVF-DDFKTSNHHDVVLNWL 152
Cdd:COG1225   80 PLLSDPDGEVAKAYGVRGT------------PTTFLIDPDGKIRYVWvGPVDPRPHLEEVLEAL 131
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 4-132 4.13e-35

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: 119.30  E-value: 4.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   4 LKAGDIAPKFSLPDQDGEQVNLTDFQGQR-VLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFA 82
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKpVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495777056  83 EKELLNFTLLSD--EDHQVCEQFGVWGEKTFMGKtydgihRISFLIDADGKV 132
Cdd:cd03018   81 EENGLTFPLLSDfwPHGEVAKAYGVFDEDLGVAE------RAVFVIDRDGII 126
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 5-147 5.63e-26

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 95.90  E-value: 5.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056    5 KAGDIAPKFSLPD--QDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKL-SRF 81
Cdd:pfam08534   1 KAGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFvKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495777056   82 AEKELLNFTLLSDEDHQVCEQFGV-WGEKTFMGktyDGIHRiSFLIDADGKVEHVF-DDFKTSNHHDV 147
Cdd:pfam08534  81 WGKEGLPFPFLSDGNAAFTKALGLpIEEDASAG---LRSPR-YAVIDEDGKVVYLFvGPEPGVDVSDA 144
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
7-135 9.91e-22

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 86.28  E-value: 9.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   7 GDIAPKFSLP---DQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDkpeklSRFA- 82
Cdd:COG0450    6 GDKAPDFTAEathGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVD-----SVFSh 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777056  83 ------EKELL-----NFTLLSDEDHQVCEQFGVWGEKTfmGKTYdgihRISFLIDADGKVEHV 135
Cdd:COG0450   81 kawhetIKEKGgivkiKFPIIADPTGKIARAYGMLHPED--GVAV----RGVFIIDPDGKIRAI 138
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 7-135 3.40e-18

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: 76.39  E-value: 3.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   7 GDIAPKFS----LPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDkpeklSRFA 82
Cdd:cd03015    2 GKKAPDFKatavVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTD-----SHFS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777056  83 EK------------ELLNFTLLSDEDHQVCEQFGVWGEKtfmgktyDGI-HRISFLIDADGKVEHV 135
Cdd:cd03015   77 HLawrntprkegglGKINFPLLADPKKKISRDYGVLDEE-------EGVaLRGTFIIDPEGIIRHI 135
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-136 3.90e-17

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 72.80  E-value: 3.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   1 MNPlkAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYpkamTPGCTVqaCglRDNMDELKKV-----GVEVLGISTDK- 74
Cdd:COG0526    1 MKA--VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFW----ATWCPP--C--RAEMPVLKELaeeygGVVFVGVDVDEn 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495777056  75 PEKLSRFAEKELLNFTLLSDEDHQVCEQFGVWGEKTFmgktydgihrisFLIDADGKVEHVF 136
Cdd:COG0526   71 PEAVKAFLKELGLPYPVLLDPDGELAKAYGVRGIPTT------------VLIDKDGKIVARH 120
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 13-136 2.00e-15

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: 68.03  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  13 FSLPDQDGEQVNLTDFQGQRVLVYFYpkamTPGCTVqaCglRDNMDELKKV-------GVEVLGISTDK--PEKLSRFAE 83
Cdd:cd02966    2 FSLPDLDGKPVSLSDLKGKVVLVNFW----ASWCPP--C--RAEMPELEALakeykddGVEVVGVNVDDddPAAVKAFLK 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495777056  84 KELLNFTLLSDEDHQVCEQFGVwgektfmgktyDGIHRiSFLIDADGKVEHVF 136
Cdd:cd02966   74 KYGITFPVLLDPDGELAKAYGV-----------RGLPT-TFLIDRDGRIRARH 114
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
5-135 5.28e-14

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 65.41  E-value: 5.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   5 KAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPgCTVQACGLRDNMDELKKVGVEVLGISTDKPE-KLSRFAE 83
Cdd:PRK03147  36 QVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKP-CEKEMPYMNELYPKYKEKGVEIIAVNVDETElAVKNFVN 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495777056  84 KELLNFTLLSDEDHQVCEQFGVWGEKTfmgktydgihriSFLIDADGKVEHV 135
Cdd:PRK03147 115 RYGLTFPVAIDKGRQVIDAYGVGPLPT------------TFLIDKDGKVVKV 154
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 5-135 9.29e-14

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: 64.14  E-value: 9.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   5 KAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKkvGVEVLGISTDKPEKLSRFAEK 84
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWCGA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495777056  85 ELL-NFTLLSD-EDHQVCEQFGVWGEKTFMgktydgIHRISFLIDADGKVEHV 135
Cdd:cd03014   79 EGVdNVTTLSDfRDHSFGKAYGVLIKDLGL------LARAVFVIDENGKVIYV 125
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 9-138 1.77e-12

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: 60.69  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   9 IAPKFSLPDQDGEQVNLTDFQGQRVLVYF-YpkamT--PG-CTVQACGLRDNMDELKKVG---VEVLGIS----TDKPEK 77
Cdd:cd02968    1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFgY----ThcPDvCPTTLANLAQALKQLGADGgddVQVVFISvdpeRDTPEV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777056  78 LSRFAEKELLNFTLL--SDED-HQVCEQFGV---WGEKTFMGKTYDGIHRIsFLIDADGKVEHVFDD 138
Cdd:cd02968   77 LKAYAKAFGPGWIGLtgTPEEiEALAKAFGVyyeKVPEDDGDYLVDHSAAI-YLVDPDGKLVRYYGG 142
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 7-132 3.53e-12

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


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 60.72  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   7 GDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYpkaMTPGCT-VQACGLRDNMD--ELKKVGVEVLGIST--------DKP 75
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMF---ICNHCPyVKAIEDRLNRLakEYGAKGVAVVAINSndieaypeDSP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495777056  76 EKLSRFAEKELLNFTLLSDEDHQVCEQFGVwgEKT--FmgktydgihrisFLIDADGKV 132
Cdd:cd02969   78 ENMKAKAKEHGYPFPYLLDETQEVAKAYGA--ACTpdF------------FLFDPDGKL 122
tpx PRK00522
thiol peroxidase;
4-135 6.29e-12

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 59.91  E-value: 6.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   4 LKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQacgLRDNMDELKKV-GVEVLGISTDKPEKLSRFA 82
Cdd:PRK00522  18 PQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATS---VRKFNQEAAELdNTVVLCISADLPFAQKRFC 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495777056  83 EKE-LLNFTLLSD-EDHQVCEQFGVW-GEKTFMGKTydgiHRISFLIDADGKVEHV 135
Cdd:PRK00522  95 GAEgLENVITLSDfRDHSFGKAYGVAiAEGPLKGLL----ARAVFVLDENNKVVYS 146
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 7-135 3.05e-11

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 59.58  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   7 GDIAPKF---SLPDQDGEQVNLTD-FQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPekLSRFA 82
Cdd:PTZ00137  71 GKLMPSFkgtALLNDDLVQFNSSDyFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSP--FSHKA 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495777056  83 EKEL---------LNFTLLSDEDHQVCEQFGVWGEKTFMgktydgiHRISFLIDADGKVEHV 135
Cdd:PTZ00137 149 WKELdvrqggvspLKFPLFSDISREVSKSFGLLRDEGFS-------HRASVLVDKAGVVKHV 203
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 10-136 3.18e-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: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  10 APKFSLPDQDGEQVNLTDFQGQR-VLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKELLN 88
Cdd:cd02970    2 APDFELPDAGGETVTLSALLGEGpVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEAFDKGKFLP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777056  89 FTLLSDEDHQVCEQFG-VWGE-KTFMGKTYDGIHRIS---------------FLIDADGKV--EHVF 136
Cdd:cd02970   82 FPVYADPDRKLYRALGlVRSLpWSNTPRALWKNAAIGfrgndegdglqlpgvFVIGPDGTIlfAHVD 148
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 14-137 1.49e-10

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 56.06  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  14 SLPDQDGEQVNLTDFQGQRVLVYF-Y---PKAmtpgCTVQACGLRDNMDELKKVG---VEVLGIST----DKPEKLSRFA 82
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFgYtscPDV----CPTTLANLAQVQEALGEDGgddVQVLFISVdperDTPEVLKAYA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  83 EK-ELLNFTLLS---DEDHQVCEQFGVWGEKTfMGKTYDGIHRISF-LIDADGKVEHVFD 137
Cdd:COG1999   80 EAfGAPRWIGLTgdpEEIAALAKAFGVYYEKV-PDGDYTFDHSAAVyLVDPDGRLRGYYP 138
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 7-132 1.26e-09

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: 54.47  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   7 GDIAPKFSLPDQDGEqVNLTDFQGQRVLVYF-YPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAE-- 83
Cdd:cd03016    2 GDTAPNFEADTTHGP-IKFHDYLGDSWGILFsHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEdi 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495777056  84 ----KELLNFTLLSDEDHQVCEQFGVWGEKTFMGKTYdgihRISFLIDADGKV 132
Cdd:cd03016   81 eeytGVEIPFPIIADPDREVAKLLGMIDPDAGSTLTV----RAVFIIDPDKKI 129
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 3-132 4.83e-09

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 52.93  E-value: 4.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   3 PLKAGDIAPKFSLPDQDGEqVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDK-------- 74
Cdd:PRK13190   1 PVKLGQKAPDFTVNTTKGP-IDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSiyshiawl 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495777056  75 PEKLSRFAEKelLNFTLLSDEDHQVCEQFGVWGEKTfmGKTYdgihRISFLIDADGKV 132
Cdd:PRK13190  80 RDIEERFGIK--IPFPVIADIDKELAREYNLIDENS--GATV----RGVFIIDPNQIV 129
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 13-132 1.12e-08

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: 50.64  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   13 FSLPDQDGEQVNLTDFQGQRVLVYFypkamtpG-------CTVQACGLRDNMDELKKVGVEVLGIS------TDKPEKLS 79
Cdd:pfam02630   4 FELVDQDGKAVTEADFEGRPSLVFF-------GfthcpdvCPTTLPNMAQVLDALGEEGIDVQPVFitvdpeRDTPEVLA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495777056   80 RFAEK---ELLNFTLLSDEDHQVCEQFGVWGEKTFM-GKTYDGIHRIS-FLIDADGKV 132
Cdd:pfam02630  77 EYLEAfgpRIIGLTGSPEQIAAAARAFRVYYEKVPDdGGDYTVDHTASvYLVDPDGRF 134
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 10-153 2.11e-08

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 51.06  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  10 APKFS----LPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKE 85
Cdd:PTZ00253  12 APSFEevalMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTLQE 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777056  86 -------LLNFTLLSDEDHQVCEQFGVWGEKTfmGKTYDGIhrisFLIDADGKVEHV-FDDFKTSNHHDVVLNWLK 153
Cdd:PTZ00253  92 rkkgglgTMAIPMLADKTKSIARSYGVLEEEQ--GVAYRGL----FIIDPKGMLRQItVNDMPVGRNVEEVLRLLE 161
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 18-135 6.63e-07

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 46.90  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  18 QDGEQVNLT--DFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDkpeklSRFAEKEL--------- 86
Cdd:PRK10382  17 KNGEFIEVTekDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTD-----THFTHKAWhsssetiak 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495777056  87 LNFTLLSDEDHQVCEQFGVWGEKTFMGKtydgihRISFLIDADGKVEHV 135
Cdd:PRK10382  92 IKYAMIGDPTGALTRNFDNMREDEGLAD------RATFVVDPQGIIQAI 134
PRK13189 PRK13189
peroxiredoxin; Provisional
 7-132 1.32e-06

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 46.13  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   7 GDIAPKFSLPDQDGEqVNLTD-FQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDkpeklSRFAE-- 83
Cdd:PRK13189  12 GDKFPEFEVKTTHGP-IKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSID-----QVFSHik 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777056  84 -----KELLN----FTLLSDEDHQVCEQFGVwgektfmgktydgIH--------RISFLIDADGKV 132
Cdd:PRK13189  86 wvewiKEKLGveieFPIIADDRGEIAKKLGM-------------ISpgkgtntvRAVFIIDPKGII 138
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 11-135 2.58e-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: 44.21  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  11 PKFSLPDQDGEQVNLTDFQGQRVLVYF------YPKAMTPgcTVQAcgLRDNmdelkkvgVEVLGIST--DKPEKLSRFA 82
Cdd:cd03011    1 PLFTATTLDGEQFDLESLSGKPVLVYFwatwcpVCRFTSP--TVNQ--LAAD--------YPVVSVALrsGDDGAVARFM 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495777056  83 EKELLNFTLLSDEDHQVCEQFGVWGEKTFmgktydgihrisFLIDADGKVEHV 135
Cdd:cd03011   69 QKKGYGFPVINDPDGVISARWGVSVTPAI------------VIVDPGGIVFVT 109
PRK15000 PRK15000
peroxiredoxin C;
4-149 5.31e-04

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 38.50  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056   4 LKAGDIAPKFSLPDQDgeqvnltdfQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDkpeklSRFAE 83
Cdd:PRK15000  17 LGSGEIVDKFNFKQHT---------NGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFD-----SEFVH 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495777056  84 KELLN------------FTLLSDEDHQVCEQFGVwgEKTFMGKTYDGihriSFLIDADGKVEH-VFDDFKTSNHHDVVL 149
Cdd:PRK15000  83 NAWRNtpvdkggigpvkYAMVADVKREIQKAYGI--EHPDEGVALRG----SFLIDANGIVRHqVVNDLPLGRNIDEML 155
PRK13599 PRK13599
peroxiredoxin;
27-132 2.57e-03

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 36.62  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777056  27 DFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTDKPEKLSRFAEKELLN------FTLLSDEDHQVC 100
Cdd:PRK13599  25 DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNtniaipFPVIADDLGKVS 104

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495777056 101 EQFGVwgekTFMGKTYDGIhRISFLIDADGKV 132
Cdd:PRK13599 105 NQLGM----IHPGKGTNTV-RAVFIVDDKGTI 131
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 12-73 9.22e-03

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 35.21  E-value: 9.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495777056  12 KFSLPDqdgeqvnltDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKVGVEVLGISTD 73
Cdd:PRK13191  24 KIKLPD---------DYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVD 76
 
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.
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