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Conserved domains on  [gi|695917253|ref|NP_001289201|]
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thioredoxin-dependent peroxide reductase, mitochondrial isoform c precursor [Homo sapiens]

Protein Classification

peroxiredoxin( domain architecture ID 10122432)

peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, is a thiol-specific antioxidant protein that protects cells against reactive oxygen species

CATH:  3.40.30.10
EC:  1.11.1.-
Gene Ontology:  GO:0008379
PubMed:  15518547|12517450|10049365|15558583
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 65-186 2.64e-75

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: 223.92  E-value: 2.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVVN-GEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAW 143
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 695917253 144 INTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGT 123
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 65-186 2.64e-75

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: 223.92  E-value: 2.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVVN-GEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAW 143
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 695917253 144 INTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGT 123
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
65-186 3.48e-64

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 196.45  E-value: 3.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:COG0450    5 IGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWH 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 695917253 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:COG0450   85 ETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGV 126
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 59-184 5.30e-53

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 168.16  E-value: 5.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  59 SCHAPAVTQHAPYFKGTAVV-NGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSH 137
Cdd:PTZ00253   2 SCGDAKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 695917253 138 FSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALR 184
Cdd:PTZ00253  82 YAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYR 128
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 65-186 7.30e-41

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: 134.66  E-value: 7.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253   65 VTQHAPYFKGTavvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 695917253  145 NTPRkngglghMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:pfam00578  78 EKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRAT 112
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 63-188 1.16e-39

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


Pssm-ID: 211789  Cd Length: 187  Bit Score: 133.68  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253   63 PAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLA 142
Cdd:TIGR03137   2 SLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 695917253  143 WINTprkNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSSQV 188
Cdd:TIGR03137  82 WHDT---SEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFV 124
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
65-184 1.45e-26

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 101.28  E-value: 1.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:NF040737  38 VGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMWN 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 695917253 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALR 184
Cdd:NF040737 118 DEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIR 157
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 65-186 2.64e-75

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: 223.92  E-value: 2.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVVN-GEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAW 143
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 695917253 144 INTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGT 123
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
65-186 3.48e-64

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 196.45  E-value: 3.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:COG0450    5 IGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWH 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 695917253 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:COG0450   85 ETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGV 126
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 59-184 5.30e-53

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 168.16  E-value: 5.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  59 SCHAPAVTQHAPYFKGTAVV-NGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSH 137
Cdd:PTZ00253   2 SCGDAKINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 695917253 138 FSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALR 184
Cdd:PTZ00253  82 YAHLQWTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYR 128
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 69-186 1.95e-43

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: 141.92  E-value: 1.95e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  69 APYFKGTAVVNGEFkdlSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTpr 148
Cdd:cd02971    2 APDFTLPATDGGEV---SLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEK-- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 695917253 149 knggLGHMNIALLSDLTKQISRDYGVLLE---GSGLALRSS 186
Cdd:cd02971   77 ----EGGLNFPLLSDPDGEFAKAYGVLIEksaGGGLAARAT 113
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 65-186 7.30e-41

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: 134.66  E-value: 7.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253   65 VTQHAPYFKGTavvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 695917253  145 NTPRkngglghMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:pfam00578  78 EKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRAT 112
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 63-188 1.16e-39

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


Pssm-ID: 211789  Cd Length: 187  Bit Score: 133.68  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253   63 PAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLA 142
Cdd:TIGR03137   2 SLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 695917253  143 WINTprkNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSSQV 188
Cdd:TIGR03137  82 WHDT---SEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFV 124
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 54-186 2.01e-34

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 122.36  E-value: 2.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  54 FSTSS-SCH---APAVTQHAPYFKGTAVVNGEFKDL-SLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCE 128
Cdd:PTZ00137  55 YSTSEgLCNtvtSSLVGKLMPSFKGTALLNDDLVQFnSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVK 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 695917253 129 VVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGvLLEGSGLALRSS 186
Cdd:PTZ00137 135 VLGVSVDSPFSHKAWKELDVRQGGVSPLKFPLFSDISREVSKSFG-LLRDEGFSHRAS 191
PRK15000 PRK15000
peroxiredoxin C;
65-186 9.39e-31

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 111.31  E-value: 9.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVV-NGEFkdLSLDDFK----GKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFS 139
Cdd:PRK15000   4 VTRQAPDFTAAAVLgSGEI--VDKFNFKqhtnGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 695917253 140 HLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:PRK15000  82 HNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGS 128
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 66-186 8.76e-29

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 105.84  E-value: 8.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  66 TQHAPyFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWIN 145
Cdd:PRK10382   6 TKIKP-FKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 695917253 146 TPRKnggLGHMNIALLSDLTKQISRDYGVLLEGSGLALRSS 186
Cdd:PRK10382  85 SSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRAT 122
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
65-184 1.45e-26

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 101.28  E-value: 1.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:NF040737  38 VGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMWN 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 695917253 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALR 184
Cdd:NF040737 118 DEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIR 157
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 69-186 8.42e-25

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: 94.26  E-value: 8.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  69 APYFkgtAVVNGEFKDLSLDDFKG-KYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWIntp 147
Cdd:cd03018    7 APDF---ELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA--- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 695917253 148 RKNGglghMNIALLSD--LTKQISRDYGVLLEGSGLALRSS 186
Cdd:cd03018   81 EENG----LTFPLLSDfwPHGEVAKAYGVFDEDLGVAERAV 117
PRK13189 PRK13189
peroxiredoxin; Provisional
 69-180 2.09e-23

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 92.74  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  69 APYFKgtavVNGEFKDLSL-DDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTP 147
Cdd:PRK13189  15 FPEFE----VKTTHGPIKLpDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEWI 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 695917253 148 RKNGGLgHMNIALLSDLTKQISRDYGVLLEGSG 180
Cdd:PRK13189  91 KEKLGV-EIEFPIIADDRGEIAKKLGMISPGKG 122
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 67-186 3.66e-23

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: 89.91  E-value: 3.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  67 QHAPYFKGTavvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINt 146
Cdd:cd03017    1 DKAPDFTLP---DQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 695917253 147 prKNGglghMNIALLSDLTKQISRDYGVLLE---GSGLALRSS 186
Cdd:cd03017   77 --KYG----LPFPLLSDPDGKLAKAYGVWGEkkkKYMGIERST 113
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 67-184 3.95e-23

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 91.45  E-value: 3.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  67 QHAPYFKgtavVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINT 146
Cdd:PRK13190   6 QKAPDFT----VNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLRD 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 695917253 147 PRKNGGLgHMNIALLSDLTKQISRDYGVLLEGSGLALR 184
Cdd:PRK13190  82 IEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVR 118
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-174 9.53e-22

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 86.07  E-value: 9.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  69 APYFKGTAVvNGefKDLSLDDFKGKYLVLFFYPlDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWIntpR 148
Cdd:COG1225    1 APDFTLPDL-DG--KTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                         90       100
                 ....*....|....*....|....*.
gi 695917253 149 KNGglghMNIALLSDLTKQISRDYGV 174
Cdd:COG1225   74 KYG----LPFPLLSDPDGEVAKAYGV 95
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 86-185 6.74e-20

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: 82.97  E-value: 6.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  86 SLDDFKG-KYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGlGHMNIALLSDL 164
Cdd:cd03016   18 KFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDIEEYTG-VEIPFPIIADP 96

                         90       100
                 ....*....|....*....|...
gi 695917253 165 TKQISRDYGVL--LEGSGLALRS 185
Cdd:cd03016   97 DREVAKLLGMIdpDAGSTLTVRA 119
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 88-197 4.08e-18

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 78.73  E-value: 4.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  88 DDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLgHMNIALLSDLTKQ 167
Cdd:PRK13191  29 DDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIADPMGN 107

                         90       100       110
                 ....*....|....*....|....*....|
gi 695917253 168 ISRDYGVLLEGSGLALRSSQVQLLPKSTFR 197
Cdd:PRK13191 108 VAKRLGMIHAESSTATVRAVFIVDDKGTVR 137
PRK13599 PRK13599
peroxiredoxin;
88-180 4.08e-18

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 78.60  E-value: 4.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  88 DDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLgHMNIALLSDLTKQ 167
Cdd:PRK13599  24 EDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGK 102

                         90
                 ....*....|...
gi 695917253 168 ISRDYGVLLEGSG 180
Cdd:PRK13599 103 VSNQLGMIHPGKG 115
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 64-185 3.68e-12

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: 61.06  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  64 AVTQHAPYFKgtaVVNGEFKDLSLDDFKGKYLVLFFYP-LDfTFVCPTEIVAFSDKANEFHDVNceVVAVSVDSHFSHLA 142
Cdd:cd03014    1 KVGDKAPDFT---LVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNTV--VLTISADLPFAQKR 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 695917253 143 WINTPrkngglGHMNIALLSDL-TKQISRDYGVLLEGSGLALRS 185
Cdd:cd03014   75 WCGAE------GVDNVTTLSDFrDHSFGKAYGVLIKDLGLLARA 112
tpx PRK00522
thiol peroxidase;
63-185 1.72e-09

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 54.52  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  63 PAVTQHAPYFKgtaVVNGEFKDLSLDDFKGKYLVLFFYP-LDfTFVCPTEIVAFSDKANEFHDVNceVVAVSVDSHFSHL 141
Cdd:PRK00522  18 PQVGDKAPDFT---LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELDNTV--VLCISADLPFAQK 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 695917253 142 AWIntprknGGLGHMNIALLSDL-TKQISRDYGVLLEGS---GLALRS 185
Cdd:PRK00522  92 RFC------GAEGLENVITLSDFrDHSFGKAYGVAIAEGplkGLLARA 133
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 64-185 5.86e-09

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 52.76  E-value: 5.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253   64 AVTQHAPYFKGTAVvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSH-FSHLA 142
Cdd:pfam08534   1 KAGDKAPDFTLPDA-ATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDaFFVKR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 695917253  143 WINTPrkngglgHMNIALLSDLTKQISRDYGV-LLEGSGLALRS 185
Cdd:pfam08534  80 FWGKE-------GLPFPFLSDGNAAFTKALGLpIEEDASAGLRS 116
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 79-174 6.57e-06

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 44.16  E-value: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  79 NGEFkdLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVD-----SHFSHlawintpRKNggl 153
Cdd:PRK09437  19 DGEQ--VSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDkpeklSRFAE-------KEL--- 86

                         90       100
                 ....*....|....*....|.
gi 695917253 154 ghMNIALLSDLTKQISRDYGV 174
Cdd:PRK09437  87 --LNFTLLSDEDHQVAEQFGV 105
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 64-174 1.62e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 42.75  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  64 AVTQHAPYFKGTAVvngEFKDLSLDDFKGKYLVLFFY-----PldftfvCPTEIVAFSDKANEFHDVncEVVAVSVDSHF 138
Cdd:COG0526    3 AVGKPAPDFTLTDL---DGKPLSLADLKGKPVLVNFWatwcpP------CRAEMPVLKELAEEYGGV--VFVGVDVDENP 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 695917253 139 ShlAWINTPRKNGglghMNIALLSDLTKQISRDYGV 174
Cdd:COG0526   72 E--AVKAFLKELG----LPYPVLLDPDGELAKAYGV 101
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 83-135 1.27e-03

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 37.96  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695917253  83 KDLSLDDFKGKYLVLFFyplDFTF---VCPTEIVAFSD-----KANEFHDVNceVVAVSVD 135
Cdd:COG1999   11 KPVTLADLRGKPVLVFF---GYTScpdVCPTTLANLAQvqealGEDGGDDVQ--VLFISVD 66
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 85-135 2.20e-03

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: 36.81  E-value: 2.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695917253  85 LSLDDFKGKYLVLFFYpldFTF---VCPTEIVAFSD-----KANEFHDVncEVVAVSVD 135
Cdd:cd02968   15 VTLSDLKGKPVLVYFG---YTHcpdVCPTTLANLAQalkqlGADGGDDV--QVVFISVD 68
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 81-174 3.73e-03

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: 35.67  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695917253  81 EFKDLSLDDFKGKYLVLFFY-----PldftfvCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSH--LAWIntpRKNGgl 153
Cdd:cd02966    8 DGKPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFL---KKYG-- 76

                         90       100
                 ....*....|....*....|.
gi 695917253 154 ghMNIALLSDLTKQISRDYGV 174
Cdd:cd02966   77 --ITFPVLLDPDGELAKAYGV 95
 
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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