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Conserved domains on  [gi|516407906|ref|WP_017797304|]
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MULTISPECIES: thiol peroxidase [Oceanobacillus]

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];
1-164 7.76e-103

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441680  Cd Length: 168  Bit Score: 291.99  E-value: 7.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   1 MSNVTFKNDPVTLLGVEKKVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFDNVQIL 80
Cdd:COG2077    1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  81 TISMDLPFAQKRWCAANGIDKVDTLSDHRAADFGEKYGVLIKE---LRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEA 157
Cdd:COG2077   81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                 ....*..
gi 516407906 158 VLSHLNK 164
Cdd:COG2077  161 ALAALKA 167
 
Name Accession Description Interval E-value
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-164 7.76e-103

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 291.99  E-value: 7.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   1 MSNVTFKNDPVTLLGVEKKVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFDNVQIL 80
Cdd:COG2077    1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  81 TISMDLPFAQKRWCAANGIDKVDTLSDHRAADFGEKYGVLIKE---LRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEA 157
Cdd:COG2077   81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                 ....*..
gi 516407906 158 VLSHLNK 164
Cdd:COG2077  161 ALAALKA 167
tpx PRK00522
thiol peroxidase;
1-159 2.34e-96

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 275.63  E-value: 2.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   1 MSNVTFKNDPVTLLGVEKKVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFDNVQIL 80
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  81 TISMDLPFAQKRWCAANGIDKVDTLSDHRAADFGEKYGVLIKE---LRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEA 157
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEgplKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ..
gi 516407906 158 VL 159
Cdd:PRK00522 161 AL 162
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 19-159 3.65e-78

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: 228.62  E-value: 3.65e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  19 KVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFDNVQILTISMDLPFAQKRWCAANG 98
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516407906  99 IDKVDTLSDHRAADFGEKYGVLIKELRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEAVL 159
Cdd:cd03014   81 VDNVTTLSDFRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPEITDEPDYEAAL 141
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 19-159 2.90e-31

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 109.77  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   19 KVGDSAPDFTV--LANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQT---RRFNEEASNFDNVQILTISMDLPFAQKRW 93
Cdd:pfam08534   1 KAGDKAPDFTLpdAATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHpylEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   94 CAANGIdKVDTLSDhRAADFGEKYGVLIKE---LRLLSRAVFVVDENDKITYVEYLSE-VSNHPDYEAVL 159
Cdd:pfam08534  81 WGKEGL-PFPFLSD-GNAAFTKALGLPIEEdasAGLRSPRYAVIDEDGKVVYLFVGPEpGVDVSDAEAVL 148
 
Name Accession Description Interval E-value
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-164 7.76e-103

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 291.99  E-value: 7.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   1 MSNVTFKNDPVTLLGVEKKVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFDNVQIL 80
Cdd:COG2077    1 MATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  81 TISMDLPFAQKRWCAANGIDKVDTLSDHRAADFGEKYGVLIKE---LRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEA 157
Cdd:COG2077   81 TISADLPFAQKRFCGAEGIDNVVTLSDFRDRSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDA 160


                 ....*..
gi 516407906 158 VLSHLNK 164
Cdd:COG2077  161 ALAALKA 167
tpx PRK00522
thiol peroxidase;
1-159 2.34e-96

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 275.63  E-value: 2.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   1 MSNVTFKNDPVTLLGVEKKVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFDNVQIL 80
Cdd:PRK00522   1 MATVTFKGNPVTVAGSLPQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  81 TISMDLPFAQKRWCAANGIDKVDTLSDHRAADFGEKYGVLIKE---LRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEA 157
Cdd:PRK00522  81 CISADLPFAQKRFCGAEGLENVITLSDFRDHSFGKAYGVAIAEgplKGLLARAVFVLDENNKVVYSELVPEITNEPDYDA 160


                 ..
gi 516407906 158 VL 159
Cdd:PRK00522 161 AL 162
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 19-159 3.65e-78

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: 228.62  E-value: 3.65e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  19 KVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFDNVQILTISMDLPFAQKRWCAANG 98
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516407906  99 IDKVDTLSDHRAADFGEKYGVLIKELRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEAVL 159
Cdd:cd03014   81 VDNVTTLSDFRDHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPEITDEPDYEAAL 141
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 24-159 4.42e-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: 134.60  E-value: 4.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  24 APDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKRWCAANGIDK 101
Cdd:cd02971    2 APDFTLPATDGGEVSLSDFKGKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAkgGAEVLGVSVDSPFSHKAWAEKEGGLN 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516407906 102 VDTLSDHRAAdFGEKYGVLIKEL---RLLSRAVFVVDENDKITYVEYLSEVSNHpDYEAVL 159
Cdd:cd02971   82 FPLLSDPDGE-FAKAYGVLIEKSaggGLAARATFIIDPDGKIRYVEVEPLPTGR-NAEELL 140
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 19-159 2.90e-31

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 109.77  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   19 KVGDSAPDFTV--LANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQT---RRFNEEASNFDNVQILTISMDLPFAQKRW 93
Cdd:pfam08534   1 KAGDKAPDFTLpdAATDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHpylEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   94 CAANGIdKVDTLSDhRAADFGEKYGVLIKE---LRLLSRAVFVVDENDKITYVEYLSE-VSNHPDYEAVL 159
Cdd:pfam08534  81 WGKEGL-PFPFLSD-GNAAFTKALGLPIEEdasAGLRSPRYAVIDEDGKVVYLFVGPEpGVDVSDAEAVL 148
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 19-159 9.57e-30

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: 105.82  E-value: 9.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  19 KVGDSAPDFTVLANDLSEKHLSDYKGNVKVISV-VPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKRWCA 95
Cdd:cd03018    2 EVGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVfFPLAFTPVCTKELCALRDSLELFEaaGAEVLGISVDSPFSLRAWAE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516407906  96 ANGIDkVDTLSD---HRAAdfGEKYGVLIKELRLLSRAVFVVDENDKITYVEY--LSEVSNHPDYEAVL 159
Cdd:cd03018   82 ENGLT-FPLLSDfwpHGEV--AKAYGVFDEDLGVAERAVFVIDRDGIIRYAWVsdDGEPRDLPDYDEAL 147
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 20-143 5.17e-25

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: 93.06  E-value: 5.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906   20 VGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNF--DNVQILTISMDLPFAQKRWCAAN 97
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFkkLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 516407906   98 GIdKVDTLSDhRAADFGEKYGVLIKELRLLSRAVFVVDENDKITYV 143
Cdd:pfam00578  81 GL-PFPLLSD-PDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
24-162 1.33e-15

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 69.12  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  24 APDFTVLANDLSEKHLSDYKGNVKVISVVPSiDTGVCSEQTRRFNEEASNF--DNVQILTISMDLPFAQKRWCAANGIDk 101
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYAT-WCPGCTAELPELRDLYEEFkdKGVEVLGVSSDSDEAHKKFAEKYGLP- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516407906 102 VDTLSDhRAADFGEKYGVLIKelrllsRAVFVVDENDKITYVeYLSEVSNHPDYEAVLSHL 162
Cdd:COG1225   79 FPLLSD-PDGEVAKAYGVRGT------PTTFLIDPDGKIRYV-WVGPVDPRPHLEEVLEAL 131
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 22-154 6.22e-15

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: 67.57  E-value: 6.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  22 DSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKRWCAANGI 99
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKalGAVVIGVSPDSVESHAKFAEKYGL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516407906 100 dKVDTLSDHRAAdFGEKYGVL---IKELRLLSRAVFVVDENDKITYVEYLSEVSNHPD 154
Cdd:cd03017   81 -PFPLLSDPDGK-LAKAYGVWgekKKKYMGIERSTFLIDPDGKIVKVWRKVKPKGHAE 136
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 20-144 1.43e-11

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: 59.44  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  20 VGDSAPDFTVLA----NDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKRW 93
Cdd:cd03015    1 VGKKAPDFKATAvvpnGEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKklNAEVLGVSTDSHFSHLAW 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516407906  94 CAA----NGIDKVD--TLSDhRAADFGEKYGVLIKELRLLSRAVFVVDENDKITYVE 144
Cdd:cd03015   81 RNTprkeGGLGKINfpLLAD-PKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHIT 136
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
19-145 6.86e-08

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 49.69  E-value: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  19 KVGDSAPDFTVLA---NDLSEKHLSDYKGNVKVISVVPSiD-TGVC-SEQTRrFNEEASNFD--NVQILTISMDLPFAQK 91
Cdd:COG0450    4 LIGDKAPDFTAEAthgGEFKKISLSDYKGKWVVLFFHPA-DfTFVCpTELGA-FAKRYEEFKklGVEVIGLSVDSVFSHK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  92 RWCAA----NGIDKVD--TLSDHrAADFGEKYGVLIKELRLLSRAVFVVDENDKITYVEY 145
Cdd:COG0450   82 AWHETikekGGIVKIKfpIIADP-TGKIARAYGMLHPEDGVAVRGVFIIDPDGKIRAIEV 140
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 19-164 3.81e-06

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 44.16  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  19 KVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLP-----FAQK 91
Cdd:PRK09437   5 KAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKkaGVVVLGISTDKPeklsrFAEK 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516407906  92 RwcAANgidkVDTLSD--HRAAD----FGEKyGVLIKELRLLSRAVFVVDENDKITYVEYLSEVSNHpdYEAVLSHLNK 164
Cdd:PRK09437  85 E--LLN----FTLLSDedHQVAEqfgvWGEK-KFMGKTYDGIHRISFLIDADGKIEHVFDKFKTSNH--HDVVLDYLKE 154
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 19-137 2.26e-05

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 42.58  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  19 KVGDSAPDFTVLA----NDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKR 92
Cdd:PTZ00253   7 KINHPAPSFEEVAlmpnGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNelNCEVLACSMDSEYAHLQ 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516407906  93 WCAAN------GIDKVDTLSDhRAADFGEKYGVLIKELRLLSRAVFVVDEN 137
Cdd:PTZ00253  87 WTLQErkkgglGTMAIPMLAD-KTKSIARSYGVLEEEQGVAYRGLFIIDPK 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 18-162 9.08e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.44  E-value: 9.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  18 KKVGDSAPDFTVLANDLSEKHLSDYKGNVKVISV-----VPsidtgvCSEQTRRFNEEASNFDNVQILTISMD-LPFAQK 91
Cdd:COG0526    2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFwatwcPP------CRAEMPVLKELAEEYGGVVFVGVDVDeNPEAVK 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516407906  92 RWCAANGIDKVdTLSDhRAADFGEKYGVlikelrllsRAV---FVVDENDKITYVeyLSEVSNHPDYEAVLSHL 162
Cdd:COG0526   76 AFLKELGLPYP-VLLD-PDGELAKAYGV---------RGIpttVLIDKDGKIVAR--HVGPLSPEELEEALEKL 136
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 19-145 2.16e-04

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 39.84  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  19 KVGDSAPDFTVLANDlSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKRWCaa 96
Cdd:PRK13190   3 KLGQKAPDFTVNTTK-GPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSRRYEDFKklGVELVGLSVDSIYSHIAWL-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516407906  97 ngidkvdtlsdhraADFGEKYGVLI---------KEL-RLLS----------RAVFVVDENDKITYVEY 145
Cdd:PRK13190  80 --------------RDIEERFGIKIpfpviadidKELaREYNlidensgatvRGVFIIDPNQIVRWMIY 134
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 20-93 3.12e-04

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 39.54  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  20 VGDSAPDF---TVLANDLSEKHLSDYKGNVKVISVVPSID-TGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKRW 93
Cdd:PTZ00137  70 VGKLMPSFkgtALLNDDLVQFNSSDYFKDSYGLLVFYPLDfTFVCPSELLGFSERLKEFEerGVKVLGVSVDSPFSHKAW 149
PRK13599 PRK13599
peroxiredoxin;
18-145 4.09e-03

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 36.23  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407906  18 KKVGDSAPDFTVLANDLSEKHLSDYKGNVKVISVVPSIDTGVCSEQTRRFNEEASNFD--NVQILTISMDLPFAQKRWca 95
Cdd:PRK13599   2 KLLGEKFPSMEVVTTQGVKRLPEDYAGKWFVLFSHPADFTPVCTTEFVEFARKANDFKelNTELIGLSVDQVFSHIKW-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516407906  96 angidkVDTLSDHRAAD-----FGEKYGVLIKELRLLS--------RAVFVVDENDKITYVEY 145
Cdd:PRK13599  80 ------VEWIKDNTNIAipfpvIADDLGKVSNQLGMIHpgkgtntvRAVFIVDDKGTIRLIMY 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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