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Conserved domains on  [gi|1650118718|gb|QCQ37863|]
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thiol peroxidase [Bacteroides fragilis]

Protein Classification

peroxiredoxin( domain architecture ID 10005271)

atypical 2-Cys peroxiredoxin similar to thioredoxin-dependent thiol peroxidase (Tpx), a thiol-specific antioxidant (TSA) protein with substrate specificity toward alkyl hydroperoxides over hydrogen peroxide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-166 4.44e-106

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441680  Cd Length: 168  Bit Score: 300.08  E-value: 4.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718   1 MATTNFKGQPVKLIGEFIQVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKDTVVL 80
Cdd:COG2077     1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  81 AISKDLPFAQGRFCTTEGIENVIPLSDFRFSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITQEPDYEK 160
Cdd:COG2077    81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEGPLLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                  ....*.
gi 1650118718 161 ALAAVK 166
Cdd:COG2077   161 ALAALK 166
 
Name Accession Description Interval E-value
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-166 4.44e-106

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 300.08  E-value: 4.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718   1 MATTNFKGQPVKLIGEFIQVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKDTVVL 80
Cdd:COG2077     1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  81 AISKDLPFAQGRFCTTEGIENVIPLSDFRFSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITQEPDYEK 160
Cdd:COG2077    81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEGPLLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                  ....*.
gi 1650118718 161 ALAAVK 166
Cdd:COG2077   161 ALAALK 166
tpx PRK00522
thiol peroxidase;
1-166 9.24e-102

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 289.11  E-value: 9.24e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718   1 MATTNFKGQPVKLIGEFIQVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKDTVVL 80
Cdd:PRK00522    1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  81 AISKDLPFAQGRFCTTEGIENVIPLSDFRFSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITQEPDYEK 160
Cdd:PRK00522   81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEGPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                  ....*.
gi 1650118718 161 ALAAVK 166
Cdd:PRK00522  161 ALAALK 166
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 19-164 1.26e-77

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: 227.47  E-value: 1.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  19 QVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKDTVVLAISKDLPFAQGRFCTTEG 98
Cdd:cd03014     1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1650118718  99 IENVIPLSDFRFSDFDESYGVRMADgplAGLLARAVVVIGKDGKVAYTELVPEITQEPDYEKALAA 164
Cdd:cd03014    81 VDNVTTLSDFRDHSFGKAYGVLIKD---LGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 19-162 3.91e-33

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 114.77  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  19 QVGKVAPDFELVK--SDLSSFSLKDLKGKNIVLNIFPSMDTGVCATS---VRKFNKMAAGLKDTVVLAISKDLPFAQGRF 93
Cdd:pfam08534   1 KAGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEhpyLEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  94 CTTEGIENVIPLSdfRFSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITQE-PDYEKAL 162
Cdd:pfam08534  81 WGKEGLPFPFLSD--GNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDvSDAEAVL 148
 
Name Accession Description Interval E-value
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-166 4.44e-106

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 300.08  E-value: 4.44e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718   1 MATTNFKGQPVKLIGEFIQVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKDTVVL 80
Cdd:COG2077     1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  81 AISKDLPFAQGRFCTTEGIENVIPLSDFRFSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITQEPDYEK 160
Cdd:COG2077    81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEGPLLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                  ....*.
gi 1650118718 161 ALAAVK 166
Cdd:COG2077   161 ALAALK 166
tpx PRK00522
thiol peroxidase;
1-166 9.24e-102

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 289.11  E-value: 9.24e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718   1 MATTNFKGQPVKLIGEFIQVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKDTVVL 80
Cdd:PRK00522    1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  81 AISKDLPFAQGRFCTTEGIENVIPLSDFRFSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITQEPDYEK 160
Cdd:PRK00522   81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEGPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                  ....*.
gi 1650118718 161 ALAAVK 166
Cdd:PRK00522  161 ALAALK 166
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 19-164 1.26e-77

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: 227.47  E-value: 1.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  19 QVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKDTVVLAISKDLPFAQGRFCTTEG 98
Cdd:cd03014     1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1650118718  99 IENVIPLSDFRFSDFDESYGVRMADgplAGLLARAVVVIGKDGKVAYTELVPEITQEPDYEKALAA 164
Cdd:cd03014    81 VDNVTTLSDFRDHSFGKAYGVLIKD---LGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 24-162 1.90e-41

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: 135.37  E-value: 1.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  24 APDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLK--DTVVLAISKDLPFAQGRFCTTEGIEN 101
Cdd:cd02971     2 APDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAkgGAEVLGVSVDSPFSHKAWAEKEGGLN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1650118718 102 VIPLSDFRfSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITqEPDYEKAL 162
Cdd:cd02971    82 FPLLSDPD-GEFAKAYGVLIEKSAGGGLAARATFIIDPDGKIRYVEVEPLPT-GRNAEELL 140
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 19-162 3.91e-33

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 114.77  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  19 QVGKVAPDFELVK--SDLSSFSLKDLKGKNIVLNIFPSMDTGVCATS---VRKFNKMAAGLKDTVVLAISKDLPFAQGRF 93
Cdd:pfam08534   1 KAGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEhpyLEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  94 CTTEGIENVIPLSdfRFSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAYTELVPEITQE-PDYEKAL 162
Cdd:pfam08534  81 WGKEGLPFPFLSD--GNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDvSDAEAVL 148
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 20-145 1.55e-21

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: 84.20  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  20 VGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLKD--TVVLAISKDLPFAQGRFCTTE 97
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKlgVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1650118718  98 GIENVIpLSDFRfSDFDESYGVRmadGPLAGLLARAVVVIGKDGKVAY 145
Cdd:pfam00578  81 GLPFPL-LSDPD-GEVARAYGVL---NEEEGGALRATFVIDPDGKVRY 123
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 18-164 2.44e-20

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: 81.94  E-value: 2.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  18 IQVGKVAPDFELVKSDLSSFSLKDLKG-KNIVLNIFPSMDTGVCATSVRKFNKMAAGLKD--TVVLAISKDLPFAQGRFC 94
Cdd:cd03018     1 LEVGDKAPDFELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAagAEVLGISVDSPFSLRAWA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1650118718  95 TTEGIEnvIPLsdfrFSDFD------ESYGVRMADgplAGLLARAVVVIGKDGKVAYTElVPEITQ---EPDYEKALAA 164
Cdd:cd03018    81 EENGLT--FPL----LSDFWphgevaKAYGVFDED---LGVAERAVFVIDRDGIIRYAW-VSDDGEprdLPDYDEALDA 149
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
24-165 2.18e-18

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 76.44  E-value: 2.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  24 APDFELVKSDLSSFSLKDLKGKNIVLNIFPSMdTGVCATSVRKFNKMAAGLKD--TVVLAISKDLPFAQGRFCTTEGIEn 101
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATW-CPGCTAELPELRDLYEEFKDkgVEVLGVSSDSDEAHKKFAEKYGLP- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1650118718 102 vIPLsdfrFSDFD----ESYGVRMadgplagllARAVVVIGKDGKVAYtELVPEITQEPDYEKALAAV 165
Cdd:COG1225    79 -FPL----LSDPDgevaKAYGVRG---------TPTTFLIDPDGKIRY-VWVGPVDPRPHLEEVLEAL 131
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 24-145 8.81e-16

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: 69.88  E-value: 8.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  24 APDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSVRKFNKMAAGLK--DTVVLAISKDLPFAQGRFCTTEGIeN 101
Cdd:cd03017     3 APDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKalGAVVIGVSPDSVESHAKFAEKYGL-P 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1650118718 102 VIPLSDFRfSDFDESYGVRMADGPLAGLLARAVVVIGKDGKVAY 145
Cdd:cd03017    82 FPLLSDPD-GKLAKAYGVWGEKKKKYMGIERSTFLIDPDGKIVK 124
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 20-147 7.09e-12

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: 60.21  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  20 VGKVAPDFELV----KSDLSSFSLKDLKGKNIVLNIFPsMD-TGVCATSVRKFNKMAAGLKD--TVVLAISKDLPFAQGR 92
Cdd:cd03015     1 VGKKAPDFKATavvpNGEFKEISLSDYKGKWVVLFFYP-LDfTFVCPTEIIAFSDRYEEFKKlnAEVLGVSTDSHFSHLA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1650118718  93 FCTTE----GIENV-IPLsdfrFSDFD----ESYGVRMADgplAGLLARAVVVIGKDGKVAYTE 147
Cdd:cd03015    80 WRNTPrkegGLGKInFPL----LADPKkkisRDYGVLDEE---EGVALRGTFIIDPEGIIRHIT 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 19-165 2.53e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 47.38  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  19 QVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFpSMDTGVCATSVRKFNKMAAGLKDTVVLAIS-KDLPFAQGRFCTTE 97
Cdd:COG0526     3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFW-ATWCPPCRAEMPVLKELAEEYGGVVFVGVDvDENPEAVKAFLKEL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1650118718  98 GIENVIpLSDfRFSDFDESYGVRMAdgPlagllarAVVVIGKDGKVAYTeLVPEITQEpDYEKALAAV 165
Cdd:COG0526    82 GLPYPV-LLD-PDGELAKAYGVRGI--P-------TTVLIDKDGKIVAR-HVGPLSPE-ELEEALEKL 136
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
18-147 3.01e-07

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 47.76  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  18 IQVGKVAPDFEL---VKSDLSSFSLKDLKGKNIVLNIFPsMD-TGVCATSVRKFNKMAAGLK--DTVVLAISKDLPFAQG 91
Cdd:COG0450     3 PLIGDKAPDFTAeatHGGEFKKISLSDYKGKWVVLFFHP-ADfTFVCPTELGAFAKRYEEFKklGVEVIGLSVDSVFSHK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1650118718  92 RFCTTegIENVIPLSDFRF---SDFD----ESYGVRMADGPLAgllARAVVVIGKDGKVAYTE 147
Cdd:COG0450    82 AWHET--IKEKGGIVKIKFpiiADPTgkiaRAYGMLHPEDGVA---VRGVFIIDPDGKIRAIE 139
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 18-107 1.29e-04

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 39.92  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650118718  18 IQVGKVAPDFELVKSDLSSFSLKDLKGKNIVLNIFPSMDTGVCATSvrkfnkmAAGLKD---------TVVLAISKDLPF 88
Cdd:PRK09437    4 LKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQ-------ACGLRDnmdelkkagVVVLGISTDKPE 76

                          90
                  ....*....|....*....
gi 1650118718  89 AQGRFCTTEGIeNVIPLSD 107
Cdd:PRK09437   77 KLSRFAEKELL-NFTLLSD 94
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
16-50 1.59e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 39.99  E-value: 1.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1650118718  16 EFIQVGKVAPDFELVKSDLSSFSLKDLKGKNIVLN 50
Cdd:PRK03147   33 EKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLN 67
 
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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