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Conserved domains on  [gi|402881640|ref|XP_003904375|]
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thioredoxin-dependent peroxide reductase, mitochondrial [Papio anubis]

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
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 ...
 65-236 2.46e-115

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: 327.54  E-value: 2.46e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVVN-GEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAW 143
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 144 INTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVE 223
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                        170
                 ....*....|...
gi 402881640 224 THGEVCPADWTPD 236
Cdd:cd03015  161 EHGEVCPANWKPG 173
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 65-236 2.46e-115

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: 327.54  E-value: 2.46e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVVN-GEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAW 143
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 144 INTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVE 223
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                        170
                 ....*....|...
gi 402881640 224 THGEVCPADWTPD 236
Cdd:cd03015  161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
65-256 2.36e-107

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 308.16  E-value: 2.36e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:COG0450    5 IGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVET 224
Cdd:COG0450   85 ETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVDK 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 402881640 225 HGEVCPADWTPDSPTIKPNPAASKEYFQKVNQ 256
Cdd:COG0450  165 HGEVCPANWKPGDKVIIPPPDLVGKALERFPE 196
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 69-255 3.06e-96

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 280.25  E-value: 3.06e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  69 APYFKGTAVV-NGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTP 147
Cdd:PTZ00253  12 APSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTLQE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 148 RKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGE 227
Cdd:PTZ00253  92 RKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVEKHGE 171

                        170       180
                 ....*....|....*....|....*...
gi 402881640 228 VCPADWTPDSPTIKPNPAASKEYFQKVN 255
Cdd:PTZ00253 172 VCPANWKKGDPTMKPDPNKSKEGFFSKA 199
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 63-242 3.60e-69

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: 211.11  E-value: 3.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640   63 PAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLA 142
Cdd:TIGR03137   2 SLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  143 WINTprkNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYV 222
Cdd:TIGR03137  82 WHDT---SEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYV 158

                         170       180
                  ....*....|....*....|.
gi 402881640  223 ETH-GEVCPADWTPDSPTIKP 242
Cdd:TIGR03137 159 AAHpGEVCPAKWKEGAETLKP 179
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
65-245 5.83e-56

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 179.09  E-value: 5.83e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:NF040737  38 VGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMWN 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYV-E 223
Cdd:NF040737 118 DEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHVrE 197

                        170       180
                 ....*....|....*....|...
gi 402881640 224 THG-EVCPADWTPDSPTIKPNPA 245
Cdd:NF040737 198 TKGtEATPSGWQPGKPTLKPGPD 220
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 65-197 1.40e-47

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: 153.92  E-value: 1.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640   65 VTQHAPYFKGTavvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 402881640  145 NTPRkngglghMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKH 197
Cdd:pfam00578  78 EKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRY 123
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 65-236 2.46e-115

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: 327.54  E-value: 2.46e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVVN-GEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAW 143
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 144 INTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVE 223
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                        170
                 ....*....|...
gi 402881640 224 THGEVCPADWTPD 236
Cdd:cd03015  161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
65-256 2.36e-107

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 308.16  E-value: 2.36e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:COG0450    5 IGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHKAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVET 224
Cdd:COG0450   85 ETIKEKGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQFVDK 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 402881640 225 HGEVCPADWTPDSPTIKPNPAASKEYFQKVNQ 256
Cdd:COG0450  165 HGEVCPANWKPGDKVIIPPPDLVGKALERFPE 196
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 69-255 3.06e-96

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 280.25  E-value: 3.06e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  69 APYFKGTAVV-NGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTP 147
Cdd:PTZ00253  12 APSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTLQE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 148 RKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGE 227
Cdd:PTZ00253  92 RKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVEKHGE 171

                        170       180
                 ....*....|....*....|....*...
gi 402881640 228 VCPADWTPDSPTIKPNPAASKEYFQKVN 255
Cdd:PTZ00253 172 VCPANWKKGDPTMKPDPNKSKEGFFSKA 199
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 63-242 3.60e-69

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: 211.11  E-value: 3.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640   63 PAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLA 142
Cdd:TIGR03137   2 SLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  143 WINTprkNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYV 222
Cdd:TIGR03137  82 WHDT---SEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYV 158

                         170       180
                  ....*....|....*....|.
gi 402881640  223 ETH-GEVCPADWTPDSPTIKP 242
Cdd:TIGR03137 159 AAHpGEVCPAKWKEGAETLKP 179
PRK15000 PRK15000
peroxiredoxin C;
65-253 1.22e-57

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 182.18  E-value: 1.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVV-NGEFkdLSLDDFK----GKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFS 139
Cdd:PRK15000   4 VTRQAPDFTAAAVLgSGEI--VDKFNFKqhtnGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 140 HLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAF 219
Cdd:PRK15000  82 HNAWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDAL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 402881640 220 QYVETHGEVCPADWTPDSPTIKPNPAASKEYFQK 253
Cdd:PRK15000 162 QFHEEHGDVCPAQWEKGKEGMNASPDGVAKYLAE 195
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 48-253 1.51e-57

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 183.99  E-value: 1.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  48 SSQAKLFSTSSSyhaPAVTQHAPYFKGTAVVNGEFKDL-SLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVN 126
Cdd:PTZ00137  56 STSEGLCNTVTS---SLVGKLMPSFKGTALLNDDLVQFnSSDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 127 CEVVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGvLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVG 206
Cdd:PTZ00137 133 VKVLGVSVDSPFSHKAWKELDVRQGGVSPLKFPLFSDISREVSKSFG-LLRDEGFSHRASVLVDKAGVVKHVAVYDLGLG 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 402881640 207 RSVEETLRLVKAFQYVETHGEVCPADWTPDSPTIKPNPAASKEYFQK 253
Cdd:PTZ00137 212 RSVDETLRLFDAVQFAEKTGNVCPVNWKQGDQAMKPDSQSVKQYLSN 258
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 69-213 2.23e-57

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: 179.28  E-value: 2.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  69 APYFKGTAVVNGEFkdlSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTpr 148
Cdd:cd02971    2 APDFTLPATDGGEV---SLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEK-- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402881640 149 knggLGHMNIALLSDLTKQISRDYGVLLE---GPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETL 213
Cdd:cd02971   77 ----EGGLNFPLLSDPDGEFAKAYGVLIEksaGGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
65-245 5.83e-56

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 179.09  E-value: 5.83e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  65 VTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:NF040737  38 VGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMWN 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 145 NTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYV-E 223
Cdd:NF040737 118 DEELSKMVTGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHVrE 197

                        170       180
                 ....*....|....*....|...
gi 402881640 224 THG-EVCPADWTPDSPTIKPNPA 245
Cdd:NF040737 198 TKGtEATPSGWQPGKPTLKPGPD 220
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 66-243 6.70e-51

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 164.77  E-value: 6.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  66 TQHAPyFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWIN 145
Cdd:PRK10382   6 TKIKP-FKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 146 TPRKnggLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETH 225
Cdd:PRK10382  85 SSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASH 161

                        170
                 ....*....|....*....
gi 402881640 226 -GEVCPADWTPDSPTIKPN 243
Cdd:PRK10382 162 pGEVCPAKWKEGEATLAPS 180
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 65-197 1.40e-47

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: 153.92  E-value: 1.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640   65 VTQHAPYFKGTavvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWI 144
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 402881640  145 NTPRkngglghMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKH 197
Cdd:pfam00578  78 EKYG-------LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRY 123
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 67-256 1.36e-41

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 141.14  E-value: 1.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  67 QHAPYFKgtavVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINT 146
Cdd:PRK13190   6 QKAPDFT----VNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLRD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 147 PRKNGGLgHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHG 226
Cdd:PRK13190  82 IEERFGI-KIPFPVIADIDKELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVNWKRK 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 402881640 227 EVCPADWTPDSPTIKPNPAASKEYFQKVNQ 256
Cdd:PRK13190 161 VATPANWQPGQEGIVPAPSTLDEAEMRIKE 190
PRK13189 PRK13189
peroxiredoxin; Provisional
 69-249 2.59e-41

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 141.27  E-value: 2.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  69 APYFKgtavVNGEFKDLSL-DDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTP 147
Cdd:PRK13189  15 FPEFE----VKTTHGPIKLpDDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEWI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 148 RKNGGLgHMNIALLSDLTKQISRDYGVLLEGPG-LALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHG 226
Cdd:PRK13189  91 KEKLGV-EIEFPIIADDRGEIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQTSDEKG 169

                        170       180
                 ....*....|....*....|....*..
gi 402881640 227 EVCPADWTPDS----PTIKPnPAASKE 249
Cdd:PRK13189 170 VATPANWPPNDlikdKVIVP-PASSVE 195
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 86-255 2.38e-40

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: 138.06  E-value: 2.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  86 SLDDFKG-KYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGlGHMNIALLSDL 164
Cdd:cd03016   18 KFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDIEEYTG-VEIPFPIIADP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 165 TKQISRDYGVL--LEGPGLALRGLFIIDPNGVIKhLSVNdLP--VGRSVEETLRLVKAFQYVETHGEVCPADWTPDSPTI 240
Cdd:cd03016   97 DREVAKLLGMIdpDAGSTLTVRAVFIIDPDKKIR-LILY-YPatTGRNFDEILRVVDALQLTDKHKVATPANWKPGDDVI 174

                        170
                 ....*....|....*....
gi 402881640 241 KP----NPAASKEYFQKVN 255
Cdd:cd03016  175 VPpsvsDEEAKKKFPKGYE 193
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 88-256 3.80e-34

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 122.26  E-value: 3.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  88 DDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLgHMNIALLSDLTKQ 167
Cdd:PRK13191  29 DDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIADPMGN 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 168 ISRDYGVL-LEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGEVCPADWtPDSPTI-----K 241
Cdd:PRK13191 108 VAKRLGMIhAESSTATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANW-PNNELIgdkviN 186

                        170
                 ....*....|....*
gi 402881640 242 PNPAASKEYFQKVNQ 256
Cdd:PRK13191 187 PAPRTIKDAKMRLGQ 201
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 69-208 6.06e-32

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: 114.68  E-value: 6.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  69 APYFkgtAVVNGEFKDLSLDDFKG-KYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWIntp 147
Cdd:cd03018    7 APDF---ELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA--- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402881640 148 RKNGglghMNIALLSD--LTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRS 208
Cdd:cd03018   81 EENG----LTFPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRD 139
PRK13599 PRK13599
peroxiredoxin;
88-241 3.72e-31

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 114.81  E-value: 3.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  88 DDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLgHMNIALLSDLTKQ 167
Cdd:PRK13599  24 EDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGK 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402881640 168 ISRDYGVLLEGPGL-ALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGEVCPADWtPDSPTIK 241
Cdd:PRK13599 103 VSNQLGMIHPGKGTnTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW-PNNYLIK 176
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 67-214 2.21e-29

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: 107.63  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  67 QHAPYFKGTavvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINt 146
Cdd:cd03017    1 DKAPDFTLP---DQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAE- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402881640 147 prKNGglghMNIALLSDLTKQISRDYGVLLE---GPGLALRGLFIIDPNGVIKHLSVNDLPVGrSVEETLR 214
Cdd:cd03017   77 --KYG----LPFPLLSDPDGKLAKAYGVWGEkkkKYMGIERSTFLIDPDGKIVKVWRKVKPKG-HAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-214 4.76e-29

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 106.87  E-value: 4.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  69 APYFKGTAVvNGefKDLSLDDFKGKYLVLFFYPlDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWIntpR 148
Cdd:COG1225    1 APDFTLPDL-DG--KTVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402881640 149 KNGglghMNIALLSDLTKQISRDYGVllegpgLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLR 214
Cdd:COG1225   74 KYG----LPFPLLSDPDGEVAKAYGV------RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 64-197 2.25e-17

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: 76.08  E-value: 2.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  64 AVTQHAPYFKgtaVVNGEFKDLSLDDFKGKYLVLFFYP-LDfTFVCPTEIVAFSDKANEFHDVNceVVAVSVDSHFSHLA 142
Cdd:cd03014    1 KVGDKAPDFT---LVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNTV--VLTISADLPFAQKR 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 402881640 143 WINTPrkngglGHMNIALLSDL-TKQISRDYGVLLEGPGLALRGLFIIDPNGVIKH 197
Cdd:cd03014   75 WCGAE------GVDNVTTLSDFrDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIY 124
tpx PRK00522
thiol peroxidase;
63-197 3.63e-14

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 68.39  E-value: 3.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  63 PAVTQHAPYFKgtaVVNGEFKDLSLDDFKGKYLVLFFYP-LDfTFVCPTEIVAFSDKANEFHDVNceVVAVSVDSHFSHL 141
Cdd:PRK00522  18 PQVGDKAPDFT---LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELDNTV--VLCISADLPFAQK 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 142 AWIntprknGGLGHMNIALLSDL-TKQISRDYGVLL-EGP--GLALRGLFIIDPNGVIKH 197
Cdd:PRK00522  92 RFC------GAEGLENVITLSDFrDHSFGKAYGVAIaEGPlkGLLARAVFVLDENNKVVY 145
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 64-204 6.67e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 67.01  E-value: 6.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640   64 AVTQHAPYFKGTAVvNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSH-FSHLA 142
Cdd:pfam08534   1 KAGDKAPDFTLPDA-ATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDaFFVKR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402881640  143 WINTPrkngglgHMNIALLSDLTKQISRDYGVLLEGP---GLALRGLFIIDPNGVIKHLSVNDLP 204
Cdd:pfam08534  80 FWGKE-------GLPFPFLSDGNAAFTKALGLPIEEDasaGLRSPRYAVIDEDGKVVYLFVGPEP 137
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 218-253 5.05e-11

C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerization of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme. The domain is associated with family AhpC-TSA, pfam00578, which carries the catalytic cysteine.


Pssm-ID: 431271  Cd Length: 40  Bit Score: 56.06  E-value: 5.05e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 402881640  218 AFQYVETHGEVCPADWTPDSPTIKPNPA----ASKEYFQK 253
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRPGDKVIVPPPAtqeeAVKRYLEG 40
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 79-198 4.42e-08

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 51.09  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  79 NGEFkdLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVD-----SHFSHlawintpRKNggl 153
Cdd:PRK09437  19 DGEQ--VSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDkpeklSRFAE-------KEL--- 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 402881640 154 ghMNIALLSDLTKQISRDYGVLLEGP--GLALRGL----FIIDPNGVIKHL 198
Cdd:PRK09437  87 --LNFTLLSDEDHQVAEQFGVWGEKKfmGKTYDGIhrisFLIDADGKIEHV 135
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 64-197 8.44e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.07  E-value: 8.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  64 AVTQHAPYFKGTAVvngEFKDLSLDDFKGKYLVLFFY-----PldftfvCPTEIVAFSDKANEFHDVncEVVAVSVDSHF 138
Cdd:COG0526    3 AVGKPAPDFTLTDL---DGKPLSLADLKGKPVLVNFWatwcpP------CRAEMPVLKELAEEYGGV--VFVGVDVDENP 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402881640 139 ShlAWINTPRKNGglghMNIALLSDLTKQISRDYGVllegpglalRGL---FIIDPNGVIKH 197
Cdd:COG0526   72 E--AVKAFLKELG----LPYPVLLDPDGELAKAYGV---------RGIpttVLIDKDGKIVA 118
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 81-197 9.28e-06

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: 43.76  E-value: 9.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  81 EFKDLSLDDFKGKYLVLFFY-----PldftfvCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSH--LAWIntpRKNGgl 153
Cdd:cd02966    8 DGKPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAavKAFL---KKYG-- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 402881640 154 ghMNIALLSDLTKQISRDYGVllegpglalRGL---FIIDPNGVIKH 197
Cdd:cd02966   77 --ITFPVLLDPDGELAKAYGV---------RGLpttFLIDRDGRIRA 112
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 92-195 5.54e-05

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


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 41.14  E-value: 5.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640   92 GKYLVLFFYPLDftfvCPtEIVAFSDKANEFHDV-----NCEVVAVSVDShfSHLAWINTPRKNGGlGHMNIALLSDLTK 166
Cdd:pfam13905   1 GKVVLLYFGASW----CK-PCRRFTPLLKELYEKlkkkkNVEIVFVSLDR--DLEEFKDYLKKMPK-DWLSVPFDDDERN 72

                          90       100
                  ....*....|....*....|....*....
gi 402881640  167 QISRDYGVLlEGPGLalrglFIIDPNGVI 195
Cdd:pfam13905  73 ELKRKYGVN-AIPTL-----VLLDPNGEV 95
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 78-200 7.23e-04

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 39.08  E-value: 7.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  78 VNGEFKDLSLDD-FKGKYLVLFFYPLDFTFVCP-TEIVAFSDKANEFHD--VNcEVVAVSVDSHFSHLAWintPRKNGGL 153
Cdd:cd03013   14 VPGPPNPVNLSElFKGKKVVIFGVPGAFTPTCSaQHLPGYVENADELKAkgVD-EVICVSVNDPFVMKAW---GKALGAK 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 402881640 154 GHmnIALLSDLTKQISRDYGVLLEGPGLAL-----RGLFIIDpNGVIKHLSV 200
Cdd:cd03013   90 DK--IRFLADGNGEFTKALGLTLDLSAAGGgirskRYALIVD-DGKVKYLFV 138
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 83-218 1.65e-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: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  83 KDLSLDDFKGKYLVLFFyplDFTF---VCPTEIVAFSD-----KANEFHDVNceVVAVSVD-------------SHFSHL 141
Cdd:COG1999   11 KPVTLADLRGKPVLVFF---GYTScpdVCPTTLANLAQvqealGEDGGDDVQ--VLFISVDperdtpevlkayaEAFGAP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640 142 AWIntprkngglghmniaLLS---DLTKQISRDYGVLLEGPGLALR------GLFIIDPNGVIKHLsvndLPVGRSVEET 212
Cdd:COG1999   86 RWI---------------GLTgdpEEIAALAKAFGVYYEKVPDGDYtfdhsaAVYLVDPDGRLRGY----YPAGEDPEEL 146


                 ....*.
gi 402881640 213 LRLVKA 218
Cdd:COG1999  147 AADLKA 152
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 78-195 4.06e-03

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: 36.95  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402881640  78 VNGEFKDLSlDDFKGKYLVLFFYPldfTFVCP---TEIVAFSDKANEFHDVNCEVVAVSVDSHfSHLAWINTprknggLG 154
Cdd:cd02970   10 AGGETVTLS-ALLGEGPVVVVFYR---GFGCPfcrEYLRALSKLLPELDALGVELVAVGPESP-EKLEAFDK------GK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402881640 155 HMNIALLSDLTKQISRDYGVL-----------------------LEGPGLALRGLFIIDPNGVI 195
Cdd:cd02970   79 FLPFPVYADPDRKLYRALGLVrslpwsntpralwknaaigfrgnDEGDGLQLPGVFVIGPDGTI 142
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 85-135 4.61e-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: 36.43  E-value: 4.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 402881640  85 LSLDDFKGKYLVLFFYpldFTF---VCPTEIVAFSD-----KANEFHDVncEVVAVSVD 135
Cdd:cd02968   15 VTLSDLKGKPVLVYFG---YTHcpdVCPTTLANLAQalkqlGADGGDDV--QVVFISVD 68
 
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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