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Conserved domains on  [gi|1786822|gb|AAC73706|]
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alkyl hydroperoxide reductase, AhpC component [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

peroxiredoxin( domain architecture ID 11484690)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-187 1.01e-148

alkyl hydroperoxide reductase subunit C; Provisional


:

Pssm-ID: 182423  Cd Length: 187  Bit Score: 409.76  E-value: 1.01e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     1 MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:PRK10382   1 MSLINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160
Cdd:PRK10382  81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160

                        170       180
                 ....*....|....*....|....*..
gi 1786822   161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
Cdd:PRK10382 161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
 
Name Accession Description Interval E-value
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-187 1.01e-148

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 409.76  E-value: 1.01e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     1 MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:PRK10382   1 MSLINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160
Cdd:PRK10382  81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160

                        170       180
                 ....*....|....*....|....*..
gi 1786822   161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
Cdd:PRK10382 161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 1-187 5.56e-139

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: 384.83  E-value: 5.56e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822      1 MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:TIGR03137   1 MSLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160
Cdd:TIGR03137  81 AWHDTSEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|....*..
gi 1786822    161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
Cdd:TIGR03137 161 HPGEVCPAKWKEGAETLKPSLDLVGKI 187
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-187 1.51e-106

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 303.15  E-value: 1.51e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    1 MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:COG0450   2 MPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   81 AWHSSSE---TIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQY 157
Cdd:COG0450  82 AWHETIKekgGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQF 161

                       170       180       190
                ....*....|....*....|....*....|
gi 1786822  158 VASHpGEVCPAKWKEGEATLAPSLDLVGKI 187
Cdd:COG0450 162 VDKH-GEVCPANWKPGDKVIIPPPDLVGKA 190
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-173 2.72e-90

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: 261.29  E-value: 2.72e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    4 INTKIKPFKNQA-FKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAW 82
Cdd:cd03015   1 VGKKAPDFKATAvVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   83 HSSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVA 159
Cdd:cd03015  81 RNTPRKeggLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|....
gi 1786822  160 SHpGEVCPAKWKEG 173
Cdd:cd03015 161 EH-GEVCPANWKPG 173
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
11-187 2.59e-57

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 179.86  E-value: 2.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    11 FKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAW--HSSSET 88
Cdd:NF040737  45 FTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMWndEELSKM 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    89 I-AKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYV-ASHPGEVC 166
Cdd:NF040737 125 VtGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHVrETKGTEAT 204

                        170       180
                 ....*....|....*....|.
gi 1786822   167 PAKWKEGEATLAPSLDLVGKI 187
Cdd:NF040737 205 PSGWQPGKPTLKPGPDLVGKV 225
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-134 2.52e-42

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: 138.13  E-value: 2.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822      4 INTKIKPFKNqafKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWH 83
Cdd:pfam00578   1 VGDKAPDFEL---PDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1786822     84 SSSEtiakIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAI 134
Cdd:pfam00578  78 EKYG----LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-187 1.01e-148

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 409.76  E-value: 1.01e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     1 MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:PRK10382   1 MSLINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160
Cdd:PRK10382  81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160

                        170       180
                 ....*....|....*....|....*..
gi 1786822   161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
Cdd:PRK10382 161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 1-187 5.56e-139

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: 384.83  E-value: 5.56e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822      1 MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:TIGR03137   1 MSLINTEIKPFKATAYHNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFVHK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     81 AWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAS 160
Cdd:TIGR03137  81 AWHDTSEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYVAA 160

                         170       180
                  ....*....|....*....|....*..
gi 1786822    161 HPGEVCPAKWKEGEATLAPSLDLVGKI 187
Cdd:TIGR03137 161 HPGEVCPAKWKEGAETLKPSLDLVGKI 187
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-187 1.51e-106

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 303.15  E-value: 1.51e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    1 MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:COG0450   2 MPLIGDKAPDFTAEATHGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFSHK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   81 AWHSSSE---TIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQY 157
Cdd:COG0450  82 AWHETIKekgGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDALQF 161

                       170       180       190
                ....*....|....*....|....*....|
gi 1786822  158 VASHpGEVCPAKWKEGEATLAPSLDLVGKI 187
Cdd:COG0450 162 VDKH-GEVCPANWKPGDKVIIPPPDLVGKA 190
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-173 2.72e-90

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: 261.29  E-value: 2.72e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    4 INTKIKPFKNQA-FKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAW 82
Cdd:cd03015   1 VGKKAPDFKATAvVPNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   83 HSSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVA 159
Cdd:cd03015  81 RNTPRKeggLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFVE 160

                       170
                ....*....|....
gi 1786822  160 SHpGEVCPAKWKEG 173
Cdd:cd03015 161 EH-GEVCPANWKPG 173
peroxi_PrxU NF040737
thioredoxin-dependent peroxiredoxin;
11-187 2.59e-57

thioredoxin-dependent peroxiredoxin;


Pssm-ID: 468701  Cd Length: 233  Bit Score: 179.86  E-value: 2.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    11 FKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAW--HSSSET 88
Cdd:NF040737  45 FTAPAYYKGGFTNVKLSDYLGKWVVLCFYPGDFTFVUATEISAVAEKHDEFQKLGVEVLSMSTDSVFVHKMWndEELSKM 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    89 I-AKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYV-ASHPGEVC 166
Cdd:NF040737 125 VtGGVPFPMLSDGGGKIGKAYGVYDEAAGVDIRGRFIIDPDGVIQAMEVLTPPVGRNVSETIRQIQAFQHVrETKGTEAT 204

                        170       180
                 ....*....|....*....|.
gi 1786822   167 PAKWKEGEATLAPSLDLVGKI 187
Cdd:NF040737 205 PSGWQPGKPTLKPGPDLVGKV 225
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 7-149 6.23e-46

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 147.69  E-value: 6.23e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    7 KIKPFKnqaFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWhssS 86
Cdd:cd02971   1 KAPDFT---LPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAW---A 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786822   87 ETIAKIKYAMIGDPTGALTRNFDNMREDE---GLADRATFVVDPQGIIQAIEVTAEGIGRDASDLL 149
Cdd:cd02971  75 EKEGGLNFPLLSDPDGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGRNAEELL 140
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 4-179 8.79e-44

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 144.28  E-value: 8.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     4 INTKIKPFKNQAF-KNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAW 82
Cdd:PTZ00253   8 INHPAPSFEEVALmPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQW 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    83 HSSSET---IAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVA 159
Cdd:PTZ00253  88 TLQERKkggLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFVE 167

                        170       180
                 ....*....|....*....|
gi 1786822   160 SHpGEVCPAKWKEGEATLAP 179
Cdd:PTZ00253 168 KH-GEVCPANWKKGDPTMKP 186
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-134 2.52e-42

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: 138.13  E-value: 2.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822      4 INTKIKPFKNqafKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWH 83
Cdd:pfam00578   1 VGDKAPDFEL---PDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1786822     84 SSSEtiakIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAI 134
Cdd:pfam00578  78 EKYG----LPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PRK15000 PRK15000
peroxiredoxin C;
1-186 1.53e-37

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 128.25  E-value: 1.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     1 MSLINTKIKPFKNQA-FKNGEFIEIT--EKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHF 77
Cdd:PRK15000   1 MVLVTRQAPDFTAAAvLGSGEIVDKFnfKQHTNGKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSFDSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    78 THKAWHSS---SETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKA 154
Cdd:PRK15000  81 VHNAWRNTpvdKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLRMVDA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 1786822   155 AQYVASHpGEVCPAKWKEGEATLAPSLDLVGK 186
Cdd:PRK15000 161 LQFHEEH-GDVCPAQWEKGKEGMNASPDGVAK 191
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 2-186 2.60e-33

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 119.28  E-value: 2.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     2 SLINTKIKPFKNQAFKNGEFIEITEKDT-EGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHK 80
Cdd:PTZ00137  68 SLVGKLMPSFKGTALLNDDLVQFNSSDYfKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHK 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    81 AWHS---SSETIAKIKYAMIGDPTGALTRNFDNMReDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQY 157
Cdd:PTZ00137 148 AWKEldvRQGGVSPLKFPLFSDISREVSKSFGLLR-DEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQF 226

                        170       180
                 ....*....|....*....|....*....
gi 1786822   158 vASHPGEVCPAKWKEGEATLAPSLDLVGK 186
Cdd:PTZ00137 227 -AEKTGNVCPVNWKQGDQAMKPDSQSVKQ 254
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 33-179 6.23e-33

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: 116.49  E-value: 6.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   33 WSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIK--YAMIGDPTGALTRNFDN 110
Cdd:cd03016  27 WGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEDIEEYTGVEipFPIIADPDREVAKLLGM 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786822  111 MREDEG--LADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGeVCPAKWKEGEATLAP 179
Cdd:cd03016 107 IDPDAGstLTVRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTDKHKV-ATPANWKPGDDVIVP 176
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 24-179 3.90e-27

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 101.47  E-value: 3.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    24 ITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETI--AKIKYAMIGDPT 101
Cdd:PRK13190  20 IDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWLRDIEERfgIKIPFPVIADID 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786822   102 GALTRNFDNMREDEGLADRATFVVDPQGIIQ-AIEVTAEgIGRDASDLLRKIKAAQyVASHPGEVCPAKWKEGEATLAP 179
Cdd:PRK13190 100 KELAREYNLIDENSGATVRGVFIIDPNQIVRwMIYYPAE-TGRNIDEIIRITKALQ-VNWKRKVATPANWQPGQEGIVP 176
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 35-154 1.58e-26

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 98.50  E-value: 1.58e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   35 VFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSetiaKIKYAMIGD--PTGALTRNFDNMR 112
Cdd:cd03018  32 VLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWAEEN----GLTFPLLSDfwPHGEVAKAYGVFD 107

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 1786822  113 EDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKA 154
Cdd:cd03018 108 EDLGVAERAVFVIDRDGIIRYAWVSDDGEPRDLPDYDEALDA 149
PRK13189 PRK13189
peroxiredoxin; Provisional
 28-174 1.58e-26

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 100.44  E-value: 1.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    28 DTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWhssSETI-----AKIKYAMIGDPTG 102
Cdd:PRK13189  32 DYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKW---VEWIkeklgVEIEFPIIADDRG 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786822   103 ALTRNFDNMREDEG-LADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQyVASHPGEVCPAKWKEGE 174
Cdd:PRK13189 109 EIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQ-TSDEKGVATPANWPPND 180
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 28-174 6.18e-26

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 98.77  E-value: 6.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    28 DTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETIAK--IKYAMIGDPTGALT 105
Cdd:PRK13191  30 DYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMWIEKNLKveVPFPIIADPMGNVA 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   106 RNFDNMREDEGLAD-RATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHpGEVCPAKWKEGE 174
Cdd:PRK13191 110 KRLGMIHAESSTATvRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKA-GVVTPANWPNNE 178
PRK13599 PRK13599
peroxiredoxin;
27-170 2.87e-21

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 86.69  E-value: 2.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    27 KDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHS--SSETIAKIKYAMIGDPTGAL 104
Cdd:PRK13599  24 EDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEwiKDNTNIAIPFPVIADDLGKV 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786822   105 TRNFDNMREDEGLAD-RATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQyVASHPGEVCPAKW 170
Cdd:PRK13599 104 SNQLGMIHPGKGTNTvRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQ-TADQYGVALPEKW 169
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 23-134 5.90e-21

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: 83.75  E-value: 5.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   23 EITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWhsssetIAK--IKYAMIGDP 100
Cdd:cd03017  15 TVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKF------AEKygLPFPLLSDP 88

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 1786822  101 TGALTRNFDNMREDE---GLADRATFVVDPQGIIQAI 134
Cdd:cd03017  89 DGKLAKAYGVWGEKKkkyMGIERSTFLIDPDGKIVKV 125
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
28-156 1.19e-18

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 77.60  E-value: 1.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   28 DTEGRWSVFFFYpADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWhsssetIAK--IKYAMIGDPTGALT 105
Cdd:COG1225  18 DLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKF------AEKygLPFPLLSDPDGEVA 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 1786822  106 RNFDNMREdegladRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQ 156
Cdd:COG1225  91 KAYGVRGT------PTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLAEL 135
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 18-152 1.20e-09

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 54.30  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     18 NGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVST--DTHFTHKAWHSssetiAKIKYA 95
Cdd:pfam08534  15 ATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSdnDAFFVKRFWGK-----EGLPFP 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822     96 MIGDPTGALTRNFDN-MRED--EGLADRATFVVDPQGIIQAIEVTAEgIGRDASDLLRKI 152
Cdd:pfam08534  90 FLSDGNAAFTKALGLpIEEDasAGLRSPRYAVIDEDGKVVYLFVGPE-PGVDVSDAEAVL 148
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 9-154 2.63e-07

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 47.97  E-value: 2.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822    9 KPFKNQafkNGEfiEITEKDTEGRWS-VFFFYpadfTF---VCPTELGDVADHYEELQKLG---VDVYAVSTD------- 74
Cdd:COG1999   3 RTLTDQ---DGK--PVTLADLRGKPVlVFFGY----TScpdVCPTTLANLAQVQEALGEDGgddVQVLFISVDperdtpe 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   75 ------THFTHKAWH---SSSETIAkikyamigdptgALTRNFDNMREDEGLADR------ATFVVDPQGIIQAIEVTae 139
Cdd:COG1999  74 vlkayaEAFGAPRWIgltGDPEEIA------------ALAKAFGVYYEKVPDGDYtfdhsaAVYLVDPDGRLRGYYPA-- 139

                       170
                ....*....|....*
gi 1786822  140 giGRDASDLLRKIKA 154
Cdd:COG1999 140 --GEDPEELAADLKA 152
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 47-134 2.36e-05

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: 41.84  E-value: 2.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   47 CPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAwhssSETIAK--IKYAMIGDPTGALTRNFDNMredeGLAdrATFV 124
Cdd:cd02966  34 CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAV----KAFLKKygITFPVLLDPDGELAKAYGVR----GLP--TTFL 103

                        90
                ....*....|
gi 1786822  125 VDPQGIIQAI 134
Cdd:cd02966 104 IDRDGRIRAR 113
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 18-72 5.50e-05

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 41.01  E-value: 5.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1786822     18 NGEfiEITEKDTEGRWSVFFFYpadFTF---VCPTELGDVADHYEELQKLGVDVYAVS 72
Cdd:pfam02630  10 DGK--AVTEADFEGRPSLVFFG---FTHcpdVCPTTLPNMAQVLDALGEEGIDVQPVF 62
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 154-179 2.74e-04

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: 37.18  E-value: 2.74e-04
                          10        20
                  ....*....|....*....|....*.
gi 1786822    154 AAQYVASHpGEVCPAKWKEGEATLAP 179
Cdd:pfam10417   1 ALQFVDKH-GVVCPANWRPGDKVIVP 25
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 23-134 5.94e-04

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: 38.35  E-value: 5.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   23 EITEKDTEGRWS-VFFFYpadfTF---VCPTELGDVADHYEELQKLG---VDVYAVSTD------------THFTHKAWH 83
Cdd:cd02968  14 PVTLSDLKGKPVlVYFGY----THcpdVCPTTLANLAQALKQLGADGgddVQVVFISVDperdtpevlkayAKAFGPGWI 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786822   84 sssetiakikyAMIGDP--TGALTRNFDNMREDEGLADR--------ATFVVDPQGIIQAI 134
Cdd:cd02968  90 -----------GLTGTPeeIEALAKAFGVYYEKVPEDDGdylvdhsaAIYLVDPDGKLVRY 139
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 25-136 1.16e-03

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: 37.54  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   25 TEKDTEGRWSVFFFYPADFTFVC-----PtelGDVAdHYEELQKLGVD-VYAVSTDTHFTHKAWHSSSETIAKIKyaMIG 98
Cdd:cd03013  23 LSELFKGKKVVIFGVPGAFTPTCsaqhlP---GYVE-NADELKAKGVDeVICVSVNDPFVMKAWGKALGAKDKIR--FLA 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 1786822   99 DPTGALTRNFDnMREDEGLAD------RATFVVDpQGIIQAIEV 136
Cdd:cd03013  97 DGNGEFTKALG-LTLDLSAAGggirskRYALIVD-DGKVKYLFV 138
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 29-136 2.99e-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: 36.57  E-value: 2.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786822   29 TEGRWSVFFFYPadfTFVCP---TELGDVADHYEELQKLGVDVYAVSTDTHftHKAWHSSSETIAkiKYAMIGDPTGALT 105
Cdd:cd02970  21 LGEGPVVVVFYR---GFGCPfcrEYLRALSKLLPELDALGVELVAVGPESP--EKLEAFDKGKFL--PFPVYADPDRKLY 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 1786822  106 R-----------------------NFDNMREDEGLADRATFVVDPQGIIQAIEV 136
Cdd:cd02970  94 RalglvrslpwsntpralwknaaiGFRGNDEGDGLQLPGVFVIGPDGTILFAHV 147
 
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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