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Conserved domains on  [gi|586175985|gb|EWP81973|]
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thiol peroxidase [Staphylococcus aureus M1209]

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;
1-163 7.63e-103

thiol peroxidase;


:

Pssm-ID: 179055  Cd Length: 167  Bit Score: 291.80  E-value: 7.63e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   1 MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEG-IVL 79
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNtVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  80 TISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEE---LRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDA 156
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEgplKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ....*..
gi 586175985 157 ALAAYKN 163
Cdd:PRK00522 161 ALAALKA 167
 
Name Accession Description Interval E-value
tpx PRK00522
thiol peroxidase;
1-163 7.63e-103

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 291.80  E-value: 7.63e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   1 MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEG-IVL 79
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNtVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  80 TISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEE---LRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDA 156
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEgplKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ....*..
gi 586175985 157 ALAAYKN 163
Cdd:PRK00522 161 ALAALKA 167
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-164 9.38e-99

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 281.59  E-value: 9.38e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   1 MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEGI-VL 79
Cdd:COG2077    1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVvVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  80 TISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEE---LRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDA 156
Cdd:COG2077   81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                 ....*...
gi 586175985 157 ALAAYKNI 164
Cdd:COG2077  161 ALAALKAL 168
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 21-160 4.74e-76

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: 223.23  E-value: 4.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  21 GDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEGI-VLTISADLPFAQKRWCASAGLD 99
Cdd:cd03014    3 GDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTvVLTISADLPFAQKRWCGAEGVD 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586175985 100 NVITLSDHRDLSFGENYGVVMEELRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDAALAA 160
Cdd:cd03014   83 NVTTLSDFRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 20-158 7.57e-30

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 106.30  E-value: 7.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   20 EGDFAPDFTVLD--NDLNQVTLADYAGKKKLISVVPSIDTGVCDQQT---RKFNSEASKEE-GIVLTISADLPFAQKRWC 93
Cdd:pfam08534   2 AGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHpylEKLNELYKEKGvDVVAVNSDNDAFFVKRFW 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586175985   94 ASAGLDNVITLSdhRDLSFGENYGVVMEE---LRLLARAVFVLDVDNKVVYKEIVSE-GTDFPDFDAAL 158
Cdd:pfam08534  82 GKEGLPFPFLSD--GNAAFTKALGLPIEEdasAGLRSPRYAVIDEDGKVVYLFVGPEpGVDVSDAEAVL 148
 
Name Accession Description Interval E-value
tpx PRK00522
thiol peroxidase;
1-163 7.63e-103

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 291.80  E-value: 7.63e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   1 MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEG-IVL 79
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNtVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  80 TISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEE---LRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDA 156
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEgplKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ....*..
gi 586175985 157 ALAAYKN 163
Cdd:PRK00522 161 ALAALKA 167
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-164 9.38e-99

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 281.59  E-value: 9.38e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   1 MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEGI-VL 79
Cdd:COG2077    1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVvVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  80 TISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEE---LRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDA 156
Cdd:COG2077   81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                 ....*...
gi 586175985 157 ALAAYKNI 164
Cdd:COG2077  161 ALAALKAL 168
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 21-160 4.74e-76

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: 223.23  E-value: 4.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  21 GDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASKEEGI-VLTISADLPFAQKRWCASAGLD 99
Cdd:cd03014    3 GDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTvVLTISADLPFAQKRWCGAEGVD 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586175985 100 NVITLSDHRDLSFGENYGVVMEELRLLARAVFVLDVDNKVVYKEIVSEGTDFPDFDAALAA 160
Cdd:cd03014   83 NVTTLSDFRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 24-158 1.38e-36

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: 123.04  E-value: 1.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  24 APDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEASK-EEGI--VLTISADLPFAQKRWCASAGLDN 100
Cdd:cd02971    2 APDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEfAKGGaeVLGVSVDSPFSHKAWAEKEGGLN 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586175985 101 VITLSDHrDLSFGENYGVVMEEL---RLLARAVFVLDVDNKVVYKEIVSEGTDfPDFDAAL 158
Cdd:cd02971   82 FPLLSDP-DGEFAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTG-RNAEELL 140
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 20-158 7.57e-30

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 106.30  E-value: 7.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   20 EGDFAPDFTVLD--NDLNQVTLADYAGKKKLISVVPSIDTGVCDQQT---RKFNSEASKEE-GIVLTISADLPFAQKRWC 93
Cdd:pfam08534   2 AGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHpylEKLNELYKEKGvDVVAVNSDNDAFFVKRFW 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586175985   94 ASAGLDNVITLSdhRDLSFGENYGVVMEE---LRLLARAVFVLDVDNKVVYKEIVSE-GTDFPDFDAAL 158
Cdd:pfam08534  82 GKEGLPFPFLSD--GNAAFTKALGLPIEEdasAGLRSPRYAVIDEDGKVVYLFVGPEpGVDVSDAEAVL 148
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 18-160 2.55e-24

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: 91.95  E-value: 2.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  18 INEGDFAPDFTVLDNDLNQVTLADYAGKKK-LISVVPSIDTGVCDQQTRKFNSEASKEEG---IVLTISADLPFAQKRWC 93
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKPvVLVFFPLAFTPVCTKELCALRDSLELFEAagaEVLGISVDSPFSLRAWA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586175985  94 ASAGLdNVITLSD---HRDLSfgENYGVVMEELRLLARAVFVLDVDNKVVYKEI--VSEGTDFPDFDAALAA 160
Cdd:cd03018   81 EENGL-TFPLLSDfwpHGEVA--KAYGVFDEDLGVAERAVFVIDRDGIIRYAWVsdDGEPRDLPDYDEALDA 149
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 21-142 3.43e-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: 83.04  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985   21 GDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNS--EASKEEGI-VLTISADLPFAQKRWCASAG 97
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADlyEEFKKLGVeVLGVSVDSPESHKAFAEKYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 586175985   98 LdNVITLSD-HRDLSfgENYGVVMEELRLLARAVFVLDVDNKVVYK 142
Cdd:pfam00578  82 L-PFPLLSDpDGEVA--RAYGVLNEEEGGALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
24-160 4.33e-15

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 67.58  E-value: 4.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  24 APDFTVLDNDLNQVTLADYAGKKKLISVVPSiDTGVCDQQTRKFNSEAS--KEEGI-VLTISADLPFAQKRWCASAGLdN 100
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYAT-WCPGCTAELPELRDLYEefKDKGVeVLGVSSDSDEAHKKFAEKYGL-P 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985 101 VITLSDhRDLSFGENYGVVMEelrllaRAVFVLDVDNKVVYKeIVSEGTDFPDFDAALAA 160
Cdd:COG1225   79 FPLLSD-PDGEVAKAYGVRGT------PTTFLIDPDGKIRYV-WVGPVDPRPHLEEVLEA 130
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 22-141 7.99e-13

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: 61.80  E-value: 7.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  22 DFAPDFTVLDNDLNQVTLADYAGKKklisVV----PSIDTGVCDQQTRKF--NSEASKEEGI-VLTISADLPFAQKRWCA 94
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKP----VVlyfyPKDDTPGCTKEACDFrdLYEEFKALGAvVIGVSPDSVESHAKFAE 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 586175985  95 SAGLdNVITLSDHrDLSFGENYGVVME---ELRLLARAVFVLDVDNKVVY 141
Cdd:cd03017   77 KYGL-PFPLLSDP-DGKLAKAYGVWGEkkkKYMGIERSTFLIDPDGKIVK 124
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 21-118 5.10e-07

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 46.85  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  21 GDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQT---RKFNSEASKEEGIVLTISADLP-----FAQKRw 92
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQAcglRDNMDELKKAGVVVLGISTDKPeklsrFAEKE- 85

                         90       100
                 ....*....|....*....|....*.
gi 586175985  93 casagLDNVITLSDhRDLSFGENYGV 118
Cdd:PRK09437  86 -----LLNFTLLSD-EDHQVAEQFGV 105
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 21-144 3.41e-05

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: 41.72  E-value: 3.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  21 GDFAPDFTVL----DNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSEAS--KEEGI-VLTISADLPFAQKRWC 93
Cdd:cd03015    2 GKKAPDFKATavvpNGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEefKKLNAeVLGVSTDSHFSHLAWR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 586175985  94 ----ASAGLDNV-ITL-SD-HRDLSfgENYGVVMEELRLLARAVFVLDVDNKVVYKEI 144
Cdd:cd03015   82 ntprKEGGLGKInFPLlADpKKKIS--RDYGVLDEEEGVALRGTFIIDPEGIIRHITV 137
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 20-161 4.04e-03

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 35.82  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586175985  20 EGDFAPDFTVLDNDLNQVTLADYAGKKKLISV-----VPsidtgvCDQQTRKFNSEASKEEGI-VLTISAD-LPFAQKRW 92
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFwatwcPP------CRAEMPVLKELAEEYGGVvFVGVDVDeNPEAVKAF 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586175985  93 CASAGLDNVItLSDhRDLSFGENYGVvmeelrllaRAV---FVLDVDNKVVYKEIvsEGTDFPDFDAALAAY 161
Cdd:COG0526   78 LKELGLPYPV-LLD-PDGELAKAYGV---------RGIpttVLIDKDGKIVARHV--GPLSPEELEEALEKL 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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