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Conserved domains on  [gi|2088339352|ref|WP_222570063|]
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peroxiredoxin [Halomonas sp. DP5N14-9]

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 ...
 7-149 5.51e-68

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: 202.39  E-value: 5.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   7 EPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQGF 86
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2088339352  87 NFELISDKDEAVCGLFDVIKLKKlygKEHLGIERSTFLIDSEGRLAREWRKVKVKGHVEEVLE 149
Cdd:cd03017    81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 7-149 5.51e-68

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: 202.39  E-value: 5.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   7 EPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQGF 86
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2088339352  87 NFELISDKDEAVCGLFDVIKLKKlygKEHLGIERSTFLIDSEGRLAREWRKVKVKGHVEEVLE 149
Cdd:cd03017    81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
9-151 3.07e-43

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 139.62  E-value: 3.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   9 VPDFSASATGDNTITLSQLRDRQVVIYFYpKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQGFNF 88
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088339352  89 ELISDKDEAVCGLFDVIKlkklygkehlgiERSTFLIDSEGRLAREW-RKVKVKGHVEEVLEAA 151
Cdd:COG1225    80 PLLSDPDGEVAKAYGVRG------------TPTTFLIDPDGKIRYVWvGPVDPRPHLEEVLEAL 131
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-149 9.36e-42

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 136.61  E-value: 9.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   2 TVSIGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFK 81
Cdd:PRK09437    3 PLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2088339352  82 AKQGFNFELISDKDEAVCGLFDVIKLKKLYGKEHLGIERSTFLIDSEGRLAREWRKVKVKGHVEEVLE 149
Cdd:PRK09437   83 EKELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLD 150
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-132 3.56e-40

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: 131.58  E-value: 3.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   5 IGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQ 84
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2088339352  85 GFNFELISDKDEAVCGLFDViklkklYGKEHLGIERSTFLIDSEGRLA 132
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGV------LNEEEGGALRATFVIDPDGKVR 122
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 7-149 5.51e-68

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: 202.39  E-value: 5.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   7 EPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQGF 86
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2088339352  87 NFELISDKDEAVCGLFDVIKLKKlygKEHLGIERSTFLIDSEGRLAREWRKVKVKGHVEEVLE 149
Cdd:cd03017    81 PFPLLSDPDGKLAKAYGVWGEKK---KKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 8-149 4.83e-46

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: 146.92  E-value: 4.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   8 PVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQG-F 86
Cdd:cd02971     1 KAPDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKEGgL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2088339352  87 NFELISDKDEAVCGLFDVIKLKKlygKEHLGIERSTFLIDSEGRLAREWRKVKVKGHVEEVLE 149
Cdd:cd02971    81 NFPLLSDPDGEFAKAYGVLIEKS---AGGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
9-151 3.07e-43

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 139.62  E-value: 3.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   9 VPDFSASATGDNTITLSQLRDRQVVIYFYpKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQGFNF 88
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088339352  89 ELISDKDEAVCGLFDVIKlkklygkehlgiERSTFLIDSEGRLAREW-RKVKVKGHVEEVLEAA 151
Cdd:COG1225    80 PLLSDPDGEVAKAYGVRG------------TPTTFLIDPDGKIRYVWvGPVDPRPHLEEVLEAL 131
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 2-149 9.36e-42

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 136.61  E-value: 9.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   2 TVSIGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFK 81
Cdd:PRK09437    3 PLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLSRFA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2088339352  82 AKQGFNFELISDKDEAVCGLFDVIKLKKLYGKEHLGIERSTFLIDSEGRLAREWRKVKVKGHVEEVLE 149
Cdd:PRK09437   83 EKELLNFTLLSDEDHQVAEQFGVWGEKKFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNHHDVVLD 150
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 5-132 3.56e-40

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: 131.58  E-value: 3.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   5 IGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQ 84
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2088339352  85 GFNFELISDKDEAVCGLFDViklkklYGKEHLGIERSTFLIDSEGRLA 132
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGV------LNEEEGGALRATFVIDPDGKVR 122
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 3-151 4.01e-27

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: 98.89  E-value: 4.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   3 VSIGEPVPDFSASATGDNTITLSQLR-DRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFK 81
Cdd:cd03018     1 LEVGDKAPDFELPDQNGQEVRLSEFRgRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2088339352  82 AKQGFNFELISD--KDEAVCGLFDVIklkklygKEHLGI-ERSTFLIDSEGRLAREWRKVKVKGHVEEVLEAA 151
Cdd:cd03018    81 EENGLTFPLLSDfwPHGEVAKAYGVF-------DEDLGVaERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEA 146
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-131 5.94e-27

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 99.77  E-value: 5.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   1 MTVSIGEPVPDFSASAT---GDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDG---- 73
Cdd:COG0450     1 MMPLIGDKAPDFTAEAThggEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSvfsh 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2088339352  74 ---IRAQENFKAKQGFNFELISDKDEAVCGLFDVIklkklygKEHLGI-ERSTFLIDSEGRL 131
Cdd:COG0450    81 kawHETIKEKGGIVKIKFPIIADPTGKIARAYGML-------HPEDGVaVRGVFIIDPDGKI 135
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 5-129 1.61e-17

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: 74.85  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   5 IGEPVPDFSASATGDN----TITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDG------- 73
Cdd:cd03015     1 VGKKAPDFKATAVVPNgefkEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDShfshlaw 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2088339352  74 IRAQENFKAKQGFNFELISDKDEAVCGLFDVIklkklygKEHLGI-ERSTFLIDSEG 129
Cdd:cd03015    81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVL-------DEEEGVaLRGTFIIDPEG 130
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 5-131 4.47e-13

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: 63.71  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   5 IGEPVPDFSASATGDNtITLSQLRDRQVVIYF-YPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQ----EN 79
Cdd:cd03016     1 LGDTAPNFEADTTHGP-IKFHDYLGDSWGILFsHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHikwiED 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2088339352  80 FKAKQG--FNFELISDKDEAVCGLFDVIKLKKlygKEHLGIeRSTFLIDSEGRL 131
Cdd:cd03016    80 IEEYTGveIPFPIIADPDREVAKLLGMIDPDA---GSTLTV-RAVFIIDPDKKI 129
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 6-131 1.97e-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: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   6 GEPVPDFS--ASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIR-AQENFKA 82
Cdd:pfam08534   3 GDKAPDFTlpDAATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAfFVKRFWG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2088339352  83 KQGFNFELISDKDEAVcglfdVIKLKKLYGKEHLGIERS--TFLIDSEGRL 131
Cdd:pfam08534  83 KEGLPFPFLSDGNAAF-----TKALGLPIEEDASAGLRSprYAVIDEDGKV 128
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 4-153 4.15e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.00  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   4 SIGEPVPDFSASATGDNTITLSQLRDRQVVIYFYpkAST-PGCTTEGGDFRDHKADFDDANtvVIGVSRDGIRAQ-ENFK 81
Cdd:COG0526     3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFW--ATWcPPCRAEMPVLKELAEEYGGVV--FVGVDVDENPEAvKAFL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2088339352  82 AKQGFNFELISDKDEAVCglfdviklkklygkEHLGIER--STFLIDSEGRLAREWRKVKVKGHVEEVLEAARE 153
Cdd:COG0526    79 KELGLPYPVLLDPDGELA--------------KAYGVRGipTTVLIDKDGKIVARHVGPLSPEELEEALEKLLA 138
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 5-148 4.97e-09

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 52.60  E-value: 4.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   5 IGEPVPDFSASATGDN----TITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRA---- 76
Cdd:PTZ00253    8 INHPAPSFEEVALMPNgsfkKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAhlqw 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352  77 --QENFKAKQG-FNFELISDKDEAVCGLFDVIKLKKlygkehlGIE-RSTFLIDSEGRLarewRKVKVKG-----HVEEV 147
Cdd:PTZ00253   88 tlQERKKGGLGtMAIPMLADKTKSIARSYGVLEEEQ-------GVAyRGLFIIDPKGML----RQITVNDmpvgrNVEEV 156


                  .
gi 2088339352 148 L 148
Cdd:PTZ00253  157 L 157
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 3-129 1.17e-08

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 51.78  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   3 VSIGEPVPDFSASATgDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQ----E 78
Cdd:PRK13190    2 VKLGQKAPDFTVNTT-KGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHiawlR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2088339352  79 NFKAKQGFN--FELISDKDEAVCGLFDVIklkklygKEHLGIE-RSTFLIDSEG 129
Cdd:PRK13190   81 DIEERFGIKipFPVIADIDKELAREYNLI-------DENSGATvRGVFIIDPNQ 127
PRK13189 PRK13189
peroxiredoxin; Provisional
 3-129 2.06e-08

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 51.14  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   3 VSIGEPVPDFSASAT-GDntITLS-QLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQ--- 77
Cdd:PRK13189    9 PLIGDKFPEFEVKTThGP--IKLPdDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHikw 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2088339352  78 -ENFKAKQG--FNFELISDKDeavcglfdvIKLKKLYGKEHLGIE----RSTFLIDSEG 129
Cdd:PRK13189   87 vEWIKEKLGveIEFPIIADDR---------GEIAKKLGMISPGKGtntvRAVFIIDPKG 136
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 11-133 4.89e-08

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: 48.39  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352  11 DFSASATGDNTITLSQLRDRQVVIYFYpkAST-PGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQE--NFKAKQGFN 87
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFW--ASWcPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAvkAFLKKYGIT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2088339352  88 FELISDKDEAVCGLFDVIKLKklygkehlgierSTFLIDSEGRLAR 133
Cdd:cd02966    79 FPVLLDPDGELAKAYGVRGLP------------TTFLIDRDGRIRA 112
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 8-136 2.08e-07

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 47.74  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   8 PVPDFSASATGDNTITLSQL-RDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQGF 86
Cdd:cd02970     1 TAPDFELPDAGGETVTLSALlGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESPEKLEAFDKGKFL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2088339352  87 NFELISD-----------KDEAVCGLFDVIKLKKLYGKEHLGIERS------TFLIDSEGRLAREWR 136
Cdd:cd02970    81 PFPVYADpdrklyralglVRSLPWSNTPRALWKNAAIGFRGNDEGDglqlpgVFVIGPDGTILFAHV 147
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 4-132 5.15e-07

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: 46.42  E-value: 5.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   4 SIGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDdaNTVVIGVSRDGIRAQENFKAK 83
Cdd:cd03014     1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWCGA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2088339352  84 QGF-NFELISDKDEAVCGlfdviklkKLYG----KEHLgIERSTFLIDSEGRLA 132
Cdd:cd03014    79 EGVdNVTTLSDFRDHSFG--------KAYGvlikDLGL-LARAVFVIDENGKVI 123
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
3-149 3.54e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 44.61  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   3 VSIGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPgCTTEGGDFRDHKADFDDANTVVIGVSRDGIR-AQENFK 81
Cdd:PRK03147   35 VQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKP-CEKEMPYMNELYPKYKEKGVEIIAVNVDETElAVKNFV 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2088339352  82 AKQGFNFELISDKDEAVCGLFDVIKLKklygkehlgierSTFLIDSEGRLAREWRKVKVKGHVEEVLE 149
Cdd:PRK03147  114 NRYGLTFPVAIDKGRQVIDAYGVGPLP------------TTFLIDKDGKVVKVITGEMTEEQLEEYLE 169
tpx PRK00522
thiol peroxidase;
3-87 8.16e-06

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 43.35  E-value: 8.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   3 VSIGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDdaNTVVIGVSRDGIRAQENFKA 82
Cdd:PRK00522   18 PQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELD--NTVVLCISADLPFAQKRFCG 95


                  ....*
gi 2088339352  83 KQGFN 87
Cdd:PRK00522   96 AEGLE 100
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 6-156 2.30e-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: 42.23  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   6 GEPVPDFSASATGDNTITLSQLRD-RQVVIYF------YPKASTPGCTTEGGDFRDHkadfddaNTVVIGVSRDGIRAQ- 77
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFADgKALVVMFicnhcpYVKAIEDRLNRLAKEYGAK-------GVAVVAINSNDIEAYp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352  78 ----ENFKAK---QGFNFELISDKDEAVcglfdviklKKLYGKEHlgiersT---FLIDSEGRL--------AREWRKVK 139
Cdd:cd02969    74 edspENMKAKakeHGYPFPYLLDETQEV---------AKAYGAAC------TpdfFLFDPDGKLvyrgriddSRPGNDPP 138

                         170
                  ....*....|....*..
gi 2088339352 140 VKGHveEVLEAARELHA 156
Cdd:cd02969   139 VTGR--DLRAALDALLA 153
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 5-131 4.25e-05

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 42.24  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   5 IGEPVPDFSASAT-GDNTITLSQ---LRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENF 80
Cdd:PTZ00137   70 VGKLMPSFKGTALlNDDLVQFNSsdyFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAW 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2088339352  81 K-------AKQGFNFELISDKDEAVCGLFDVIKLKklyGKEHlgieRSTFLIDSEGRL 131
Cdd:PTZ00137  150 KeldvrqgGVSPLKFPLFSDISREVSKSFGLLRDE---GFSH----RASVLVDKAGVV 200
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 5-72 4.49e-05

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 41.76  E-value: 4.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2088339352   5 IGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRD 72
Cdd:PRK13191    9 IGEKFPEMEVITTHGKIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVD 76
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-129 4.48e-04

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 38.81  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   1 MTVsIGEPVPDFSASATGDNT---ITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQ 77
Cdd:PRK10382    1 MSL-INTKIKPFKNQAFKNGEfieVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2088339352  78 ENFKAKQ----GFNFELISDKDEAVCGLFDVIklkklygKEHLGI-ERSTFLIDSEG 129
Cdd:PRK10382   80 KAWHSSSetiaKIKYAMIGDPTGALTRNFDNM-------REDEGLaDRATFVVDPQG 129
PRK13599 PRK13599
peroxiredoxin;
5-155 4.62e-04

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 38.93  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352   5 IGEPVPDFSASATGDNTITLSQLRDRQVVIYFYPKASTPGCTTEGGDFRDHKADFDDANTVVIGVSRDG----IRAQENF 80
Cdd:PRK13599    4 LGEKFPSMEVVTTQGVKRLPEDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQvfshIKWVEWI 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2088339352  81 KAKQGFN--FELISDKDEAVCGlfdviKLKKLYGKEHLGIERSTFLIDSEG--RLAREWRKvKVKGHVEEVLEAARELH 155
Cdd:PRK13599   84 KDNTNIAipFPVIADDLGKVSN-----QLGMIHPGKGTNTVRAVFIVDDKGtiRLIMYYPQ-EVGRNVDEILRALKALQ 156
DUF899 pfam05988
Bacterial protein of unknown function (DUF899); This family consists of several ...
 17-135 5.36e-03

Bacterial protein of unknown function (DUF899); This family consists of several uncharacterized bacterial proteins of unknown function.


Pssm-ID: 428710  Cd Length: 216  Bit Score: 35.74  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088339352  17 TGDNTITLSQLRD--RQVVIY---FYPKAST--PGCTTEGGDFRDHKADFDDANTVVIGVSRDGIRAQENFKAKQGFNFE 89
Cdd:pfam05988  53 GPDGPVTLADLFEgrSQLIVYhfmFGPDWEAgcPGCSMLADHIDGELVHLAARDVTLAAVSRAPLAKLEAYKRRMGWTFP 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2088339352  90 LISDKDEAVCGLFDVIKLKKLYGKEHLGIerSTFLIDsEGRLAREW 135
Cdd:pfam05988 133 WYSSVGSDFNRDFGVSFDEEQYSGERPGI--SVFLRD-GGRVFHTY 175
 
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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