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Conserved domains on  [gi|114052210|ref|NP_001040464|]
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thioredoxin peroxidase [Bombyx mori]

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

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 ...
 36-206 1.06e-110

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: 314.83  E-value: 1.06e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  36 VQKPAPDFSATAVVN-GEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAW 114
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 115 INTPRKDGGLGKMEIPLLADYKKQISKDYDVLL-DDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFAD 193
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDeEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                        170
                 ....*....|...
gi 114052210 194 KHGEVCPAGWNPD 206
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 ...
 36-206 1.06e-110

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: 314.83  E-value: 1.06e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  36 VQKPAPDFSATAVVN-GEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAW 114
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 115 INTPRKDGGLGKMEIPLLADYKKQISKDYDVLL-DDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFAD 193
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDeEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                        170
                 ....*....|...
gi 114052210 194 KHGEVCPAGWNPD 206
Cdd:cd03015  161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
32-225 7.51e-105

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 300.84  E-value: 7.51e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  32 RAPKVQKPAPDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSH 111
Cdd:COG0450    1 MMPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 112 LAWINTPRKDGGLGKMEIPLLADYKKQISKDYDVLL-DDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQ 190
Cdd:COG0450   81 KAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHpEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQ 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 114052210 191 FADKHGEVCPAGWNPdtNADTIKPNPKDSKEYFQK 225
Cdd:COG0450  161 FVDKHGEVCPANWKP--GDKVIIPPPDLVGKALER 193
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 35-223 6.39e-88

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 258.30  E-value: 6.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  35 KVQKPAPDFSATAVV-NGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLA 113
Cdd:PTZ00253   7 KINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 114 WINTPRKDGGLGKMEIPLLADYKKQISKDYDVLLD-DGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFA 192
Cdd:PTZ00253  87 WTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEeQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFV 166

                        170       180       190
                 ....*....|....*....|....*....|.
gi 114052210 193 DKHGEVCPAGWNPdtNADTIKPNPKDSKEYF 223
Cdd:PTZ00253 167 EKHGEVCPANWKK--GDPTMKPDPNKSKEGF 195
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
35-216 6.48e-58

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 182.94  E-value: 6.48e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  35 KVQKPAPDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAW 114
Cdd:NF040737  37 KVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMW 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 115 intprKDGGLGKM-----EIPLLADYKKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKA 188
Cdd:NF040737 117 -----NDEELSKMvtggvPFPMLSDGGGKIGKAYGVYDEAaGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQA 191

                        170       180       190
                 ....*....|....*....|....*....|
gi 114052210 189 FQF--ADKHGEVCPAGWNPdtNADTIKPNP 216
Cdd:NF040737 192 FQHvrETKGTEATPSGWQP--GKPTLKPGP 219
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 41-214 4.48e-56

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: 176.82  E-value: 4.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210   41 PDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTPRK 120
Cdd:TIGR03137   9 KPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWHDTSEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  121 dggLGKMEIPLLADYKKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFADKH-GEV 198
Cdd:TIGR03137  89 ---IGKITYPMLGDPTGVLTRNFGVLIEEaGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAAHpGEV 165

                         170
                  ....*....|....*.
gi 114052210  199 CPAGWNPDtnADTIKP 214
Cdd:TIGR03137 166 CPAKWKEG--AETLKP 179
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 36-168 1.74e-46

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: 150.07  E-value: 1.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210   36 VQKPAPDFSATavvNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWI 115
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 114052210  116 NTPrkdgglgKMEIPLLADYKKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHM 168
Cdd:pfam00578  78 EKY-------GLPFPLLSDPDGEVARAYGVLNEEeGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 36-206 1.06e-110

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: 314.83  E-value: 1.06e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  36 VQKPAPDFSATAVVN-GEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAW 114
Cdd:cd03015    1 VGKKAPDFKATAVVPnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 115 INTPRKDGGLGKMEIPLLADYKKQISKDYDVLL-DDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFAD 193
Cdd:cd03015   81 RNTPRKEGGLGKINFPLLADPKKKISRDYGVLDeEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                        170
                 ....*....|...
gi 114052210 194 KHGEVCPAGWNPD 206
Cdd:cd03015  161 EHGEVCPANWKPG 173
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
32-225 7.51e-105

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 300.84  E-value: 7.51e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  32 RAPKVQKPAPDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSH 111
Cdd:COG0450    1 MMPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 112 LAWINTPRKDGGLGKMEIPLLADYKKQISKDYDVLL-DDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQ 190
Cdd:COG0450   81 KAWHETIKEKGGIVKIKFPIIADPTGKIARAYGMLHpEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQ 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 114052210 191 FADKHGEVCPAGWNPdtNADTIKPNPKDSKEYFQK 225
Cdd:COG0450  161 FVDKHGEVCPANWKP--GDKVIIPPPDLVGKALER 193
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 35-223 6.39e-88

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 258.30  E-value: 6.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  35 KVQKPAPDFSATAVV-NGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLA 113
Cdd:PTZ00253   7 KINHPAPSFEEVALMpNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 114 WINTPRKDGGLGKMEIPLLADYKKQISKDYDVLLD-DGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFA 192
Cdd:PTZ00253  87 WTLQERKKGGLGTMAIPMLADKTKSIARSYGVLEEeQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFV 166

                        170       180       190
                 ....*....|....*....|....*....|.
gi 114052210 193 DKHGEVCPAGWNPdtNADTIKPNPKDSKEYF 223
Cdd:PTZ00253 167 EKHGEVCPANWKK--GDPTMKPDPNKSKEGF 195
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 24-225 1.13e-60

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 190.93  E-value: 1.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  24 NFSTTS----TTRAPKVQKPAPDFSATAVVNGEFNQLKLSD-FTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDC 98
Cdd:PTZ00137  54 NYSTSEglcnTVTSSLVGKLMPSFKGTALLNDDLVQFNSSDyFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  99 QVIGVSTDSEFSHLAWINTPRKDGGLGKMEIPLLADYKKQISKDYDVLLDDGFALRGLFIIDRNGTLRHMSVNDLPVGRS 178
Cdd:PTZ00137 134 KVLGVSVDSPFSHKAWKELDVRQGGVSPLKFPLFSDISREVSKSFGLLRDEGFSHRASVLVDKAGVVKHVAVYDLGLGRS 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 114052210 179 VDETLRLVKAFQFADKHGEVCPAGWNPDTNAdtIKPNPKDSKEYFQK 225
Cdd:PTZ00137 214 VDETLRLFDAVQFAEKTGNVCPVNWKQGDQA--MKPDSQSVKQYLSN 258
PRK15000 PRK15000
peroxiredoxin C;
36-203 3.52e-59

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 185.26  E-value: 3.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  36 VQKPAPDFSATAVV-NGEF-NQLKLSDFT-GKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHL 112
Cdd:PRK15000   4 VTRQAPDFTAAAVLgSGEIvDKFNFKQHTnGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEFVHN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 113 AWINTPRKDGGLGKMEIPLLADYKKQISKDYDV-LLDDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQF 191
Cdd:PRK15000  84 AWRNTPVDKGGIGPVKYAMVADVKREIQKAYGIeHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDALQF 163

                        170
                 ....*....|..
gi 114052210 192 ADKHGEVCPAGW 203
Cdd:PRK15000 164 HEEHGDVCPAQW 175
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
35-216 6.48e-58

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 182.94  E-value: 6.48e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  35 KVQKPAPDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAW 114
Cdd:NF040737  37 KVGKKAPDFTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMW 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 115 intprKDGGLGKM-----EIPLLADYKKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKA 188
Cdd:NF040737 117 -----NDEELSKMvtggvPFPMLSDGGGKIGKAYGVYDEAaGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQA 191

                        170       180       190
                 ....*....|....*....|....*....|
gi 114052210 189 FQF--ADKHGEVCPAGWNPdtNADTIKPNP 216
Cdd:NF040737 192 FQHvrETKGTEATPSGWQP--GKPTLKPGP 219
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 39-183 2.42e-56

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: 175.81  E-value: 2.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  39 PAPDFSATAVVNGEFNqlkLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTp 118
Cdd:cd02971    1 KAPDFTLPATDGGEVS---LSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEK- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114052210 119 rkdggLGKMEIPLLADYKKQISKDYDVLLDD----GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETL 183
Cdd:cd02971   77 -----EGGLNFPLLSDPDGEFAKAYGVLIEKsaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 41-214 4.48e-56

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: 176.82  E-value: 4.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210   41 PDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTPRK 120
Cdd:TIGR03137   9 KPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHKAWHDTSEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  121 dggLGKMEIPLLADYKKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFADKH-GEV 198
Cdd:TIGR03137  89 ---IGKITYPMLGDPTGVLTRNFGVLIEEaGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAAHpGEV 165

                         170
                  ....*....|....*.
gi 114052210  199 CPAGWNPDtnADTIKP 214
Cdd:TIGR03137 166 CPAKWKEG--AETLKP 179
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 36-168 1.74e-46

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: 150.07  E-value: 1.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210   36 VQKPAPDFSATavvNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWI 115
Cdd:pfam00578   1 VGDKAPDFELP---DGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 114052210  116 NTPrkdgglgKMEIPLLADYKKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHM 168
Cdd:pfam00578  78 EKY-------GLPFPLLSDPDGEVARAYGVLNEEeGGALRATFVIDPDGKVRYI 124
PRK13189 PRK13189
peroxiredoxin; Provisional
 28-221 2.69e-42

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 142.81  E-value: 2.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  28 TSTTRAPKVQKPAPDFSATAVvngeFNQLKLSD-FTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTD 106
Cdd:PRK13189   3 YEEIRMPLIGDKFPEFEVKTT----HGPIKLPDdYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 107 SEFSHLAWINTPRKDGGLgKMEIPLLADYKKQISKDYDVLLDDG--FALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLR 184
Cdd:PRK13189  79 QVFSHIKWVEWIKEKLGV-EIEFPIIADDRGEIAKKLGMISPGKgtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILR 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 114052210 185 LVKAFQFADKHGEVCPAGWNPDT--NADTIKPNPKDSKE 221
Cdd:PRK13189 158 LVKALQTSDEKGVATPANWPPNDliKDKVIVPPASSVEE 196
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 39-205 1.74e-41

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: 139.98  E-value: 1.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  39 PAPDFSATAVVnGEFnqlKLSDFTG-KYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINT 117
Cdd:cd03016    4 TAPNFEADTTH-GPI---KFHDYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 118 PRKDGGlGKMEIPLLADYKKQISKDYDvLLD----DGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFAD 193
Cdd:cd03016   80 IEEYTG-VEIPFPIIADPDREVAKLLG-MIDpdagSTLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTD 157

                        170
                 ....*....|..
gi 114052210 194 KHGEVCPAGWNP 205
Cdd:cd03016  158 KHKVATPANWKP 169
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 35-227 8.55e-41

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 138.06  E-value: 8.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  35 KVQKPAPDFSatavVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAW 114
Cdd:PRK13190   3 KLGQKAPDFT----VNTTKGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 115 INTPRKDGGLgKMEIPLLADYKKQISKDYDvLLDD--GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFA 192
Cdd:PRK13190  79 LRDIEERFGI-KIPFPVIADIDKELAREYN-LIDEnsGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQVN 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 114052210 193 DKHGEVCPAGWNPdtNADTIKPNPKDSKEYFQKAN 227
Cdd:PRK13190 157 WKRKVATPANWQP--GQEGIVPAPSTLDEAEMRIK 189
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 43-203 2.90e-38

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 131.26  E-value: 2.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  43 FSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTPRKdg 122
Cdd:PRK10382  11 FKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSET-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 123 gLGKMEIPLLADYKKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFADKH-GEVCP 200
Cdd:PRK10382  89 -IAKIKYAMIGDPTGALTRNFDNMREDeGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHpGEVCP 167


                 ...
gi 114052210 201 AGW 203
Cdd:PRK10382 168 AKW 170
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 34-188 6.77e-33

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: 116.22  E-value: 6.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  34 PKVQKPAPDFSATAVvNGEfnQLKLSDFTG-KYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHL 112
Cdd:cd03018    1 LEVGDKAPDFELPDQ-NGQ--EVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114052210 113 AWintpRKDGGLgkmEIPLLADY--KKQISKDYDVLLDD-GFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKA 188
Cdd:cd03018   78 AW----AEENGL---TFPLLSDFwpHGEVAKAYGVFDEDlGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEALDA 149
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 55-225 3.34e-32

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 116.48  E-value: 3.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  55 QLKLSD-FTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTPRKDGGLgKMEIPLLA 133
Cdd:PRK13191  24 KIKLPDdYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKV-EVPFPIIA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 134 DYKKQISKDYDVLLDDGF--ALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFADKHGEVCPAGW--NPDTNA 209
Cdd:PRK13191 103 DPMGNVAKRLGMIHAESStaTVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANWpnNELIGD 182

                        170
                 ....*....|....*....
gi 114052210 210 DTIKPNP---KDSKEYFQK 225
Cdd:PRK13191 183 KVINPAPrtiKDAKMRLGQ 201
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 38-184 1.30e-30

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: 109.94  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  38 KPAPDFSATavvNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWint 117
Cdd:cd03017    1 DKAPDFTLP---DQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKF--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114052210 118 pRKDGGLGkmeIPLLADYKKQISKDYDVLLDD----GFALRGLFIIDRNGTLRHmSVNDLPVGRSVDETLR 184
Cdd:cd03017   75 -AEKYGLP---FPLLSDPDGKLAKAYGVWGEKkkkyMGIERSTFLIDPDGKIVK-VWRKVKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
40-184 7.17e-30

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 108.03  E-value: 7.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  40 APDFSATAVvNGEfnQLKLSDFTGKYVVLFFYPlDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWIntpR 119
Cdd:COG1225    1 APDFTLPDL-DGK--TVSLSDLRGKPVVLYFYA-TWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFA---E 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114052210 120 KDGglgkMEIPLLADYKKQISKDYDVllddgFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLR 184
Cdd:COG1225   74 KYG----LPFPLLSDPDGEVAKAYGV-----RGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
PRK13599 PRK13599
peroxiredoxin;
60-203 4.46e-28

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 105.95  E-value: 4.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  60 DFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTPRKDGGLgKMEIPLLADYKKQI 139
Cdd:PRK13599  25 DYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKDNTNI-AIPFPVIADDLGKV 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114052210 140 SKDYDVLL--DDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFADKHGEVCPAGW 203
Cdd:PRK13599 104 SNQLGMIHpgKGTNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQYGVALPEKW 169
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
34-167 3.62e-14

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 67.81  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  34 PKVQKPAPDFSataVVNGEFNQLKLSDFTGKYVVLFFYP-LDfTFVCPTELIAFSDKAKDFAgiDCQVIGVSTDSEFSHL 112
Cdd:COG2077   18 PKVGDKAPDFT---LVDTDLSDVTLSDFAGKRKVLNIVPsLD-TPVCATSTRKFNEEAAKLD--NVVVLTISADLPFAQK 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 113 AWINTprkdGGLGKMEipLLADYK-KQISKDYDVLLDDGFAL----RGLFIIDRNGTLRH 167
Cdd:COG2077   92 RFCGA----EGIDNVV--TLSDFRdRSFGKDYGVLIKEGPLLgllaRAVFVLDENGKVVY 145
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 35-174 4.52e-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: 4.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210   35 KVQKPAPDFSATAVvNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDS-EFSHLA 113
Cdd:pfam08534   1 KAGDKAPDFTLPDA-ATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNdAFFVKR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114052210  114 WIntprKDGGLgkmEIPLLADYKKQISKDYDVLLD----DGFALRGLFIIDRNGTLRHMSVNDLP 174
Cdd:pfam08534  80 FW----GKEGL---PFPFLSDGNAAFTKALGLPIEedasAGLRSPRYAVIDEDGKVVYLFVGPEP 137
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 35-167 3.28e-13

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 64.53  E-value: 3.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  35 KVQKPAPDFSataVVNGEFNQLKLSDFTGKYVVLFFYP-LDfTFVCPTELIAFSDKAKDFAGIDcqVIGVSTDSEFSHLA 113
Cdd:cd03014    1 KVGDKAPDFT---LVTSDLSEVSLADFAGKVKVISVFPsID-TPVCATQTKRFNKEAAKLDNTV--VLTISADLPFAQKR 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 114052210 114 WINTPrkdgGLGKMEIplLADYK-KQISKDYDVLLDD-GFALRGLFIIDRNGTLRH 167
Cdd:cd03014   75 WCGAE----GVDNVTT--LSDFRdHSFGKAYGVLIKDlGLLARAVFVIDENGKVIY 124
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 188-225 2.89e-10

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: 53.75  E-value: 2.89e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 114052210  188 AFQFADKHGEVCPAGWNPdtNADTIKPNPKD----SKEYFQK 225
Cdd:pfam10417   1 ALQFVDKHGVVCPANWRP--GDKVIVPPPATqeeaVKRYLEG 40
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-167 1.03e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 55.08  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  36 VQKPAPDFSATAVvngEFNQLKLSDFTGKYVVLFFYpldFTFvCPT------ELIAFSDKAKDFagidcQVIGVSTDSEF 109
Cdd:COG0526    4 VGKPAPDFTLTDL---DGKPLSLADLKGKPVLVNFW---ATW-CPPcraempVLKELAEEYGGV-----VFVGVDVDENP 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114052210 110 ShlAWINTPRKDGglgkMEIPLLADYKKQISKDYDVllddgfalRGL---FIIDRNGTLRH 167
Cdd:COG0526   72 E--AVKAFLKELG----LPYPVLLDPDGELAKAYGV--------RGIpttVLIDKDGKIVA 118
tpx PRK00522
thiol peroxidase;
34-167 1.08e-09

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 55.29  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  34 PKVQKPAPDFSataVVNGEFNQLKLSDFTGKYVVLFFYP-LDfTFVCPTELIAFSDKAKDFAGIdcQVIGVSTDSEFSHL 112
Cdd:PRK00522  18 PQVGDKAPDFT---LVANDLSDVSLADFAGKRKVLNIFPsID-TGVCATSVRKFNQEAAELDNT--VVLCISADLPFAQK 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 113 AWINTPrkdgGLGKMeIPLLADYKKQISKDYDVLLDDGfALRGL-----FIIDRNGTLRH 167
Cdd:PRK00522  92 RFCGAE----GLENV-ITLSDFRDHSFGKAYGVAIAEG-PLKGLlaravFVLDENNKVVY 145
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 42-167 6.72e-07

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: 46.46  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  42 DFSATAVvngEFNQLKLSDFTGKYVVLFFY-----PldftfvCPTELIAFSDKAKDFAGIDCQVIGVSTDsEFSHLAWIN 116
Cdd:cd02966    1 DFSLPDL---DGKPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVD-DDDPAAVKA 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 114052210 117 TPRKDGglgkMEIPLLADYKKQISKDYDVllddgfalRGL---FIIDRNGTLRH 167
Cdd:cd02966   71 FLKKYG----ITFPVLLDPDGELAKAYGV--------RGLpttFLIDRDGRIRA 112
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 39-166 4.24e-05

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: 42.20  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  39 PAPDFSataVVNGEFNQLKLSDFTGKYVVLFFYpldFTF---VCPTELIAFS---DKAKDFAGIDCQVIGVSTDSEF--- 109
Cdd:cd02968    1 IGPDFT---LTDQDGRPVTLSDLKGKPVLVYFG---YTHcpdVCPTTLANLAqalKQLGADGGDDVQVVFISVDPERdtp 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114052210 110 SHL-AWINT--PRKDGGLGKMEI--PLLADYKKQISKDYDVLLDDGFA-LRGLFIIDRNGTLR 166
Cdd:cd02968   75 EVLkAYAKAfgPGWIGLTGTPEEieALAKAFGVYYEKVPEDDGDYLVDhSAAIYLVDPDGKLV 137
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 35-107 5.83e-05

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 41.85  E-value: 5.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114052210  35 KVQKPAPDFSataVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDS 107
Cdd:PRK09437   5 KAGDIAPKFS---LPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDK 74
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 58-188 7.69e-04

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 38.73  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210  58 LSDFTGKYVVLFFyplDFTF---VCPTELIAFS---DKAKDFAGIDCQVIGVSTDSEF-------SHLAWINTPRKDGGL 124
Cdd:COG1999   15 LADLRGKPVLVFF---GYTScpdVCPTTLANLAqvqEALGEDGGDDVQVLFISVDPERdtpevlkAYAEAFGAPRWIGLT 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114052210 125 GKME-IPLLAD-----YKKQISKDYDVLLDDGFalrglFIIDRNGTLRHMsvndLPVGRSVDETLRLVKA 188
Cdd:COG1999   92 GDPEeIAALAKafgvyYEKVPDGDYTFDHSAAV-----YLVDPDGRLRGY----YPAGEDPEELAADLKA 152
 
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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