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Conserved domains on  [gi|498485492|ref|WP_010787218|]
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thiol peroxidase [Glaesserella parasuis]

Protein Classification

peroxiredoxin( domain architecture ID 10792015)

atypical 2-Cys peroxiredoxin

EC:  1.11.1.24
Gene Ontology:  GO:0008379
PubMed:  12517450

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tpx PRK00522
thiol peroxidase;
1-166 1.73e-108

thiol peroxidase;


:

Pssm-ID: 179055  Cd Length: 167  Bit Score: 306.06  E-value: 1.73e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   1 MSQVTLAGNAIEVTGQFPQAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELANTVVL 80
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  81 CISADLPFAQARFCGAEGIANTQTLSTFRNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKQEPDYAA 160
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEGPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ....*.
gi 498485492 161 ALAVLK 166
Cdd:PRK00522 161 ALAALK 166
 
Name Accession Description Interval E-value
tpx PRK00522
thiol peroxidase;
1-166 1.73e-108

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 306.06  E-value: 1.73e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   1 MSQVTLAGNAIEVTGQFPQAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELANTVVL 80
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  81 CISADLPFAQARFCGAEGIANTQTLSTFRNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKQEPDYAA 160
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEGPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ....*.
gi 498485492 161 ALAVLK 166
Cdd:PRK00522 161 ALAALK 166
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-166 5.68e-102

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 289.68  E-value: 5.68e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   1 MSQVTLAGNAIEVTGQFPQAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELANTVVL 80
Cdd:COG2077    1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  81 CISADLPFAQARFCGAEGIANTQTLSTFRNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKQEPDYAA 160
Cdd:COG2077   81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEGPLLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                 ....*.
gi 498485492 161 ALAVLK 166
Cdd:COG2077  161 ALAALK 166
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 19-164 6.94e-73

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: 215.14  E-value: 6.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  19 QAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELANTVVLCISADLPFAQARFCGAEG 98
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498485492  99 IANTQTLSTFRNKAFHQAVGVDIATgplAGLTARAVIVLDENNKVLHSELVPEIKQEPDYAAALAV 164
Cdd:cd03014   81 VDNVTTLSDFRDHSFGKAYGVLIKD---LGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 19-162 1.16e-34

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 118.63  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   19 QAGSSVADFTL--VSNGLENVSLSDFAEKRKVLNIFPSIDTGICATS---VRVFNKEAAELANTVVLCISADLPFAQARF 93
Cdd:pfam08534   1 KAGDKAPDFTLpdAATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEhpyLEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   94 CGAEGIANTQTLStfRNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKQE-PDYAAAL 162
Cdd:pfam08534  81 WGKEGLPFPFLSD--GNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDvSDAEAVL 148
 
Name Accession Description Interval E-value
tpx PRK00522
thiol peroxidase;
1-166 1.73e-108

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 306.06  E-value: 1.73e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   1 MSQVTLAGNAIEVTGQFPQAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELANTVVL 80
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  81 CISADLPFAQARFCGAEGIANTQTLSTFRNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKQEPDYAA 160
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEGPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ....*.
gi 498485492 161 ALAVLK 166
Cdd:PRK00522 161 ALAALK 166
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-166 5.68e-102

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 289.68  E-value: 5.68e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   1 MSQVTLAGNAIEVTGQFPQAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELANTVVL 80
Cdd:COG2077    1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  81 CISADLPFAQARFCGAEGIANTQTLSTFRNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKQEPDYAA 160
Cdd:COG2077   81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEGPLLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                 ....*.
gi 498485492 161 ALAVLK 166
Cdd:COG2077  161 ALAALK 166
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 19-164 6.94e-73

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: 215.14  E-value: 6.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  19 QAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELANTVVLCISADLPFAQARFCGAEG 98
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498485492  99 IANTQTLSTFRNKAFHQAVGVDIATgplAGLTARAVIVLDENNKVLHSELVPEIKQEPDYAAALAV 164
Cdd:cd03014   81 VDNVTTLSDFRDHSFGKAYGVLIKD---LGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 26-162 2.97e-38

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: 127.28  E-value: 2.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  26 DFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELA--NTVVLCISADLPFAQARFCGAEGIANTQ 103
Cdd:cd02971    4 DFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAkgGAEVLGVSVDSPFSHKAWAEKEGGLNFP 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498485492 104 TLSTFrNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKqEPDYAAAL 162
Cdd:cd02971   84 LLSDP-DGEFAKAYGVLIEKSAGGGLAARATFIIDPDGKIRYVEVEPLPT-GRNAEELL 140
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 19-162 1.16e-34

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 118.63  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   19 QAGSSVADFTL--VSNGLENVSLSDFAEKRKVLNIFPSIDTGICATS---VRVFNKEAAELANTVVLCISADLPFAQARF 93
Cdd:pfam08534   1 KAGDKAPDFTLpdAATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEhpyLEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   94 CGAEGIANTQTLStfRNKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHSELVPEIKQE-PDYAAAL 162
Cdd:pfam08534  81 WGKEGLPFPFLSD--GNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFVGPEPGVDvSDAEAVL 148
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 21-146 8.39e-13

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: 61.47  E-value: 8.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492   21 GSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELA--NTVVLCISADLPFAQARFCGAEG 98
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKklGVEVLGVSVDSPESHKAFAEKYG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 498485492   99 IantqtlsTF-----RNKAFHQAVGVDIatgPLAGLTARAVIVLDENNKVLHS 146
Cdd:pfam00578  82 L-------PFpllsdPDGEVARAYGVLN---EEEGGALRATFVIDPDGKVRYI 124
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 21-164 1.65e-12

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: 61.52  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  21 GSSVADFTLVSNGLENVSLSDFAEKRKVLNIF-PSIDTGICATSVRVFNKEAAEL--ANTVVLCISADLPFAQARFCGAE 97
Cdd:cd03018    4 GDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFfPLAFTPVCTKELCALRDSLELFeaAGAEVLGISVDSPFSLRAWAEEN 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498485492  98 GIaNTQTLSTFrnkAFHQAV----GVDIatgPLAGLTARAVIVLDENNKVLHSElVPEIKQ---EPDYAAALAV 164
Cdd:cd03018   84 GL-TFPLLSDF---WPHGEVakayGVFD---EDLGVAERAVFVIDRDGIIRYAW-VSDDGEprdLPDYDEALDA 149
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 26-146 1.47e-09

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: 53.32  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  26 DFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAEL--ANTVVLCISADLPFAQARFCGAEGIantq 103
Cdd:cd03017    5 DFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFkaLGAVVIGVSPDSVESHAKFAEKYGL---- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 498485492 104 tlsTFR-----NKAFHQAVGVDIATGPLAGLTARAVIVLDENNKVLHS 146
Cdd:cd03017   81 ---PFPllsdpDGKLAKAYGVWGEKKKKYMGIERSTFLIDPDGKIVKV 125
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
26-165 2.36e-08

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 49.86  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  26 DFTLVSNGLENVSLSDFAEKRKVLNIFPSiDTGICATSVRVFNKEAAELA--NTVVLCISADLPFAQARFCGAEGIaNTQ 103
Cdd:COG1225    3 DFTLPDLDGKTVSLSDLRGKPVVLYFYAT-WCPGCTAELPELRDLYEEFKdkGVEVLGVSSDSDEAHKKFAEKYGL-PFP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498485492 104 TLSTFrNKAFHQAVGVdiatgplagLTARAVIVLDENNKVLHSElVPEIKQEPDYAAALAVL 165
Cdd:COG1225   81 LLSDP-DGEVAKAYGV---------RGTPTTFLIDPDGKIRYVW-VGPVDPRPHLEEVLEAL 131
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 19-94 2.44e-04

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 39.15  E-value: 2.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498485492  19 QAGSSVADFTLVSNGLENVSLSDFAEKRKVLNIFPSIDTGIC---ATSVRVfNKEAAELANTVVLCISADLPFAQARFC 94
Cdd:PRK09437   5 KAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCtvqACGLRD-NMDELKKAGVVVLGISTDKPEKLSRFA 82
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 21-147 4.07e-03

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: 35.94  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485492  21 GSSVADFTL---VSNG-LENVSLSDFAEKRKVLNIFPSIDTGICATSVRVFNKEAAELA--NTVVLCISADLPFAQARFC 94
Cdd:cd03015    2 GKKAPDFKAtavVPNGeFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKklNAEVLGVSTDSHFSHLAWR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498485492  95 GAE----GIANTQ--TLSTFrNKAFHQAVGVDIATgplAGLTARAVIVLDENNKVLHSE 147
Cdd:cd03015   82 NTPrkegGLGKINfpLLADP-KKKISRDYGVLDEE---EGVALRGTFIIDPEGIIRHIT 136
 
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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