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Conserved domains on  [gi|445974926|ref|WP_000052781|]
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MULTISPECIES: alkyl hydroperoxide reductase subunit C [Staphylococcus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AhpC super family cl29162
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 1-189 6.01e-129

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]


The actual alignment was detected with superfamily member TIGR03137:

Pssm-ID: 211789  Cd Length: 187  Bit Score: 359.79  E-value: 6.01e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926    1 MSLINKEILPFTAQAFdpKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:TIGR03137   1 MSLINTEIKPFKATAY--HNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   81 HKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:TIGR03137  79 HKAWHDTSEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYV 158

                         170       180
                  ....*....|....*....|....*....
gi 445974926  161 RKNPGEVCPAKWEEGAKTLQPGLDLVGKI 189
Cdd:TIGR03137 159 AAHPGEVCPAKWKEGAETLKPSLDLVGKI 187
 
Name Accession Description Interval E-value
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 1-189 6.01e-129

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: 359.79  E-value: 6.01e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926    1 MSLINKEILPFTAQAFdpKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:TIGR03137   1 MSLINTEIKPFKATAY--HNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   81 HKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:TIGR03137  79 HKAWHDTSEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYV 158

                         170       180
                  ....*....|....*....|....*....
gi 445974926  161 RKNPGEVCPAKWEEGAKTLQPGLDLVGKI 189
Cdd:TIGR03137 159 AAHPGEVCPAKWKEGAETLKPSLDLVGKI 187
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-189 3.57e-107

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 304.60  E-value: 3.57e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   1 MSLINKEILPFTAQAFdpKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:PRK10382   1 MSLINTKIKPFKNQAF--KNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  81 HKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:PRK10382  79 HKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYV 158

                        170       180
                 ....*....|....*....|....*....
gi 445974926 161 RKNPGEVCPAKWEEGAKTLQPGLDLVGKI 189
Cdd:PRK10382 159 ASHPGEVCPAKWKEGEATLAPSLDLVGKI 187
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-189 4.35e-100

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 286.97  E-value: 4.35e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   1 MSLINKEILPFTAQAFdpKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:COG0450    2 MPLIGDKAPDFTAEAT--HGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  81 HKAWHDHS---DAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAA 157
Cdd:COG0450   80 HKAWHETIkekGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDAL 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 445974926 158 QYVRKNpGEVCPAKWEEGAKTLQPGLDLVGKI 189
Cdd:COG0450  160 QFVDKH-GEVCPANWKPGDKVIIPPPDLVGKA 190
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-175 4.54e-89

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: 258.20  E-value: 4.54e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   4 INKEILPFTAQAFDPKKDqFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKA 83
Cdd:cd03015    1 VGKKAPDFKATAVVPNGE-FKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  84 WHDHSDA---ISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:cd03015   80 WRNTPRKeggLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFV 159

                        170
                 ....*....|....*
gi 445974926 161 RKNpGEVCPAKWEEG 175
Cdd:cd03015  160 EEH-GEVCPANWKPG 173
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 13-136 2.33e-43

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: 140.82  E-value: 2.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   13 AQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHsdaiS 92
Cdd:pfam00578   5 APDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK----Y 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 445974926   93 KITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQAS 136
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
AhpC TIGR03137
peroxiredoxin; This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one ...
 1-189 6.01e-129

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: 359.79  E-value: 6.01e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926    1 MSLINKEILPFTAQAFdpKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:TIGR03137   1 MSLINTEIKPFKATAY--HNGEFVEVTDEDVKGKWSVFFFYPADFTFVCPTELEDLADNYAELKKLGVEVYSVSTDTHFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   81 HKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:TIGR03137  79 HKAWHDTSEAIGKITYPMLGDPTGVLTRNFGVLIEEAGLADRGTFVIDPEGVIQAVEIHDNGIGRDASELLRKIKAAQYV 158

                         170       180
                  ....*....|....*....|....*....
gi 445974926  161 RKNPGEVCPAKWEEGAKTLQPGLDLVGKI 189
Cdd:TIGR03137 159 AAHPGEVCPAKWKEGAETLKPSLDLVGKI 187
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 1-189 3.57e-107

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 304.60  E-value: 3.57e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   1 MSLINKEILPFTAQAFdpKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:PRK10382   1 MSLINTKIKPFKNQAF--KNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  81 HKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:PRK10382  79 HKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYV 158

                        170       180
                 ....*....|....*....|....*....
gi 445974926 161 RKNPGEVCPAKWEEGAKTLQPGLDLVGKI 189
Cdd:PRK10382 159 ASHPGEVCPAKWKEGEATLAPSLDLVGKI 187
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
1-189 4.35e-100

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 286.97  E-value: 4.35e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   1 MSLINKEILPFTAQAFdpKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:COG0450    2 MPLIGDKAPDFTAEAT--HGGEFKKISLSDYKGKWVVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  81 HKAWHDHS---DAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAA 157
Cdd:COG0450   80 HKAWHETIkekGGIVKIKFPIIADPTGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEVYPLSVGRNVDEILRVVDAL 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 445974926 158 QYVRKNpGEVCPAKWEEGAKTLQPGLDLVGKI 189
Cdd:COG0450  160 QFVDKH-GEVCPANWKPGDKVIIPPPDLVGKA 190
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 4-175 4.54e-89

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: 258.20  E-value: 4.54e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   4 INKEILPFTAQAFDPKKDqFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKA 83
Cdd:cd03015    1 VGKKAPDFKATAVVPNGE-FKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHFSHLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  84 WHDHSDA---ISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:cd03015   80 WRNTPRKeggLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITVNDLPVGRSVDETLRVLDALQFV 159

                        170
                 ....*....|....*
gi 445974926 161 RKNpGEVCPAKWEEG 175
Cdd:cd03015  160 EEH-GEVCPANWKPG 173
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 12-150 2.65e-47

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: 151.16  E-value: 2.65e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  12 TAQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWhdhSDAI 91
Cdd:cd02971    1 KAPDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAW---AEKE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445974926  92 SKITYTMIGDPSQTITRNFDVLDEA---TGLAQRGTFIIDPDGVVQASEINADGIGRDASTL 150
Cdd:cd02971   78 GGLNFPLLSDPDGEFAKAYGVLIEKsagGGLAARATFIIDPDGKIRYVEVEPLPTGRNAEEL 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 13-136 2.33e-43

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: 140.82  E-value: 2.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   13 AQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHsdaiS 92
Cdd:pfam00578   5 APDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEK----Y 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 445974926   93 KITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQAS 136
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 4-181 2.41e-40

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 135.42  E-value: 2.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   4 INKEILPFTAQAFDPKkDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKA 83
Cdd:PTZ00253   8 INHPAPSFEEVALMPN-GSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  84 W---HDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYV 160
Cdd:PTZ00253  87 WtlqERKKGGLGTMAIPMLADKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQFV 166

                        170       180
                 ....*....|....*....|.
gi 445974926 161 RKNpGEVCPAKWEEGAKTLQP 181
Cdd:PTZ00253 167 EKH-GEVCPANWKKGDPTMKP 186
PRK15000 PRK15000
peroxiredoxin C;
1-188 4.66e-34

peroxiredoxin C;


Pssm-ID: 184962  Cd Length: 200  Bit Score: 119.39  E-value: 4.66e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   1 MSLINKEILPFTAQAF-----DPKKDQFKEVTQedlkGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVST 75
Cdd:PRK15000   1 MVLVTRQAPDFTAAAVlgsgeIVDKFNFKQHTN----GKTTVLFFWPMDFTFVCPSELIAFDKRYEEFQKRGVEVVGVSF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  76 DTHFVHKAWHD---HSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAH 152
Cdd:PRK15000  77 DSEFVHNAWRNtpvDKGGIGPVKYAMVADVKREIQKAYGIEHPDEGVALRGSFLIDANGIVRHQVVNDLPLGRNIDEMLR 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 445974926 153 KIKAAQYvRKNPGEVCPAKWEEGAKTLQPGLDLVGK 188
Cdd:PRK15000 157 MVDALQF-HEEHGDVCPAQWEKGKEGMNASPDGVAK 191
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 2-181 1.79e-27

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 104.26  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   2 SLINKEILPFTAQAFdpKKDQFKEVTQED-LKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFV 80
Cdd:PTZ00137  68 SLVGKLMPSFKGTAL--LNDDLVQFNSSDyFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFS 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  81 HKAWHD---HSDAISKITYTMIGDPSQTITRNFDVLdEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAA 157
Cdd:PTZ00137 146 HKAWKEldvRQGGVSPLKFPLFSDISREVSKSFGLL-RDEGFSHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAV 224

                        170       180
                 ....*....|....*....|....
gi 445974926 158 QYVRKNpGEVCPAKWEEGAKTLQP 181
Cdd:PTZ00137 225 QFAEKT-GNVCPVNWKQGDQAMKP 247
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 11-146 7.91e-27

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


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 99.27  E-value: 7.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  11 FTAQAFDPKKDQFKEVTQEDLKGSWSVV-CFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHsd 89
Cdd:cd03018    5 DKAPDFELPDQNGQEVRLSEFRGRKPVVlVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWAEE-- 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 445974926  90 aiSKITYTMIGD--PSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRD 146
Cdd:cd03018   83 --NGLTFPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVSDDGEPRD 139
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 26-181 1.37e-26

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 100.31  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  26 VTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAW-HDHSDAIS-KITYTMIGDPS 103
Cdd:PRK13190  20 IDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSIYSHIAWlRDIEERFGiKIPFPVIADID 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926 104 QTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQ--YVRKnpgEVCPAKWEEGAKTLQP 181
Cdd:PRK13190 100 KELAREYNLIDENSGATVRGVFIIDPNQIVRWMIYYPAETGRNIDEIIRITKALQvnWKRK---VATPANWQPGQEGIVP 176
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 30-175 1.17e-21

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: 87.21  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  30 DLKG-SWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWhdhSDAI-----SKITYTMIGDPS 103
Cdd:cd03016   21 DYLGdSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKW---IEDIeeytgVEIPFPIIADPD 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445974926 104 QTITRNFDVLDEATGLAQ--RGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNPGeVCPAKWEEG 175
Cdd:cd03016   98 REVAKLLGMIDPDAGSTLtvRAVFIIDPDKKIRLILYYPATTGRNFDEILRVVDALQLTDKHKV-ATPANWKPG 170
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 13-151 5.28e-20

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: 81.44  E-value: 5.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  13 AQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWhdhsdaIS 92
Cdd:cd03017    3 APDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKF------AE 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445974926  93 K--ITYTMIGDPSQTITRNFDVLDE---ATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLA 151
Cdd:cd03017   77 KygLPFPLLSDPDGKLAKAYGVWGEkkkKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
24-135 8.08e-20

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 80.68  E-value: 8.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  24 KEVTQEDLKGSWSVVCFYpADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHSDaiskITYTMIGDPS 103
Cdd:COG1225   12 KTVSLSDLRGKPVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYG----LPFPLLSDPD 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 445974926 104 QTITRNFDVldeatgLAQRGTFIIDPDGVVQA 135
Cdd:COG1225   87 GEVAKAYGV------RGTPTTFLIDPDGKIRY 112
PRK13189 PRK13189
peroxiredoxin; Provisional
 29-175 5.30e-19

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 80.80  E-value: 5.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  29 EDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAW----HDHSDAisKITYTMIGDPSQ 104
Cdd:PRK13189  31 DDYKGKWFVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWvewiKEKLGV--EIEFPIIADDRG 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445974926 105 TITRNFDVLDEATG-LAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNpGEVCPAKWEEG 175
Cdd:PRK13189 109 EIAKKLGMISPGKGtNTVRAVFIIDPKGIIRAILYYPQEVGRNMDEILRLVKALQTSDEK-GVATPANWPPN 179
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 29-181 6.45e-17

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 75.27  E-value: 6.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  29 EDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHD--HSDAISKITYTMIGDPSQTI 106
Cdd:PRK13191  29 DDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWVMwiEKNLKVEVPFPIIADPMGNV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926 107 TRNFDVLD-EATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNpGEVCPAKWEE----GAKTLQP 181
Cdd:PRK13191 109 AKRLGMIHaESSTATVRAVFIVDDKGTVRLILYYPMEIGRNIDEILRAIRALQLVDKA-GVVTPANWPNneliGDKVINP 187
PRK13599 PRK13599
peroxiredoxin;
29-172 6.12e-13

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 64.35  E-value: 6.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  29 EDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHD--HSDAISKITYTMIGDPSQTI 106
Cdd:PRK13599  24 EDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEwiKDNTNIAIPFPVIADDLGKV 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445974926 107 TRNFDVLDEATGLAQ-RGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNpGEVCPAKW 172
Cdd:PRK13599 104 SNQLGMIHPGKGTNTvRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTADQY-GVALPEKW 169
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 24-138 6.21e-13

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 63.16  E-value: 6.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   24 KEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVST--DTHFVHKAWHDHSdaiskITYTMIGD 101
Cdd:pfam08534  19 NTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSdnDAFFVKRFWGKEG-----LPFPFLSD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 445974926  102 PSQTITRNFDV---LDEATGLAQRGTFIIDPDGVVQASEI 138
Cdd:pfam08534  94 GNAAFTKALGLpieEDASAGLRSPRYAVIDEDGKVVYLFV 133
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-157 6.75e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.30  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   1 MSLINKEILPFTAQAFDPKkdqfkEVTQEDLKGSWSVVCFYpADFSFVCPTELEDLQNQYEELQklGVNVFSVSTDTHF- 79
Cdd:COG0526    1 MKAVGKPAPDFTLTDLDGK-----PLSLADLKGKPVLVNFW-ATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDENPe 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  80 -VHKAWHDHsdaisKITYTMIGDPSQTITRNFDVldeatglaqRG---TFIIDPDGVVQASEINAdgigRDASTLAHKIK 155
Cdd:COG0526   73 aVKAFLKEL-----GLPYPVLLDPDGELAKAYGV---------RGiptTVLIDKDGKIVARHVGP----LSPEELEEALE 134


                 ..
gi 445974926 156 AA 157
Cdd:COG0526  135 KL 136
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 24-156 5.92e-07

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 47.20  E-value: 5.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  24 KEVTQEDLKGSWSVVcfypaDFSF-----VCPTELEDLQNQYEELQKLG---VNVFSVSTD-------------THFVHK 82
Cdd:COG1999   11 KPVTLADLRGKPVLV-----FFGYtscpdVCPTTLANLAQVQEALGEDGgddVQVLFISVDperdtpevlkayaEAFGAP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  83 AWHdhsdaiskityTMIGDPSQT--ITRNFDVLDEATGLAQR------GTFIIDPDGVVQASeINAdgiGRDASTLAHKI 154
Cdd:COG1999   86 RWI-----------GLTGDPEEIaaLAKAFGVYYEKVPDGDYtfdhsaAVYLVDPDGRLRGY-YPA---GEDPEELAADL 150


                 ..
gi 445974926 155 KA 156
Cdd:COG1999  151 KA 152
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 22-136 4.46e-06

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 43.76  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  22 QFKEVTQEDLKGSWSVVCFY-----PadfsfvCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAwhdhSDAISK--I 94
Cdd:cd02966    8 DGKPVSLSDLKGKVVLVNFWaswcpP------CRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAV----KAFLKKygI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 445974926  95 TYTMIGDPSQTITRNFDVldeatglaqRG---TFIIDPDGVVQAS 136
Cdd:cd02966   78 TFPVLLDPDGELAKAYGV---------RGlptTFLIDRDGRIRAR 113
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 29-138 1.44e-05

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: 43.12  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  29 EDLKGSWSVVCFYPadfSFVCP---TELEDLQNQYEELQKLGVNVFSVSTDThfVHKAwhDHSDAISKITYTMIGDPSQT 105
Cdd:cd02970   19 ALLGEGPVVVVFYR---GFGCPfcrEYLRALSKLLPELDALGVELVAVGPES--PEKL--EAFDKGKFLPFPVYADPDRK 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445974926 106 ITRNFDVL-----------------------DEATGLAQRGTFIIDPDGVVQASEI 138
Cdd:cd02970   92 LYRALGLVrslpwsntpralwknaaigfrgnDEGDGLQLPGVFVIGPDGTILFAHV 147
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
 58-149 5.03e-05

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: 41.78  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  58 NQYEELQKLGV-NVFSVSTDTHFVHKAWHDHSDAISKItyTMIGDPSQTITRNFDVLDEATGL-----AQRGTFIIDpDG 131
Cdd:cd03013   55 ENADELKAKGVdEVICVSVNDPFVMKAWGKALGAKDKI--RFLADGNGEFTKALGLTLDLSAAgggirSKRYALIVD-DG 131

                         90
                 ....*....|....*...
gi 445974926 132 VVQASEINADGIGRDAST 149
Cdd:cd03013  132 KVKYLFVEEDPGDVEVSS 149
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 24-131 1.89e-04

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: 39.86  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926   24 KEVTQEDLKGSWSVVCFypaDFSF---VCPTELEDLQNQYEEL--QKLGVNVFSVS----TDT-----HFVHKawhdHSD 89
Cdd:pfam02630  12 KAVTEADFEGRPSLVFF---GFTHcpdVCPTTLPNMAQVLDALgeEGIDVQPVFITvdpeRDTpevlaEYLEA----FGP 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 445974926   90 AISKITytmiGDPSQT--ITRNFDVLDEATGLA--------QRGTFIIDPDG 131
Cdd:pfam02630  85 RIIGLT----GSPEQIaaAARAFRVYYEKVPDDggdytvdhTASVYLVDPDG 132
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 21-76 1.91e-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: 39.89  E-value: 1.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445974926  21 DQF-KEVTQEDLKGSWSVVcfypaDFSF-----VCPTELEDLQNQYEELQKLG---VNVFSVSTD 76
Cdd:cd02968    9 DQDgRPVTLSDLKGKPVLV-----YFGYthcpdVCPTTLANLAQALKQLGADGgddVQVVFISVD 68
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 21-133 2.93e-04

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 39.54  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  21 DQFKE-VTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDT-----HFVHKawhdhsdaiSKI 94
Cdd:PRK09437  17 DQDGEqVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKpeklsRFAEK---------ELL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 445974926  95 TYTMIGDPSQTITRNFDVLDEAT-------GLaQRGTFIIDPDGVV 133
Cdd:PRK09437  88 NFTLLSDEDHQVAEQFGVWGEKKfmgktydGI-HRISFLIDADGKI 132
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 12-139 2.93e-04

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: 39.10  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445974926  12 TAQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQklGVNVFSVSTDTHFVHKAWHDHSDAI 91
Cdd:cd03014    5 KAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLD--NTVVLTISADLPFAQKRWCGAEGVD 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445974926  92 SKITYtmigdpSQTITRNFD----VLDEATGLAQRGTFIIDPDGVVQASEIN 139
Cdd:cd03014   83 NVTTL------SDFRDHSFGkaygVLIKDLGLLARAVFVIDENGKVIYVELV 128
1-cysPrx_C pfam10417
C-terminal domain of 1-Cys peroxiredoxin; This is the C-terminal domain of 1-Cys peroxiredoxin ...
 156-181 5.68e-03

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: 33.33  E-value: 5.68e-03
                          10        20
                  ....*....|....*....|....*.
gi 445974926  156 AAQYVRKNpGEVCPAKWEEGAKTLQP 181
Cdd:pfam10417   1 ALQFVDKH-GVVCPANWRPGDKVIVP 25
 
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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