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Conserved domains on  [gi|495652454|ref|WP_008377033|]
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MULTISPECIES: thiol peroxidase [Enterococcus]

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];
1-161 7.01e-71

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441680  Cd Length: 168  Bit Score: 211.10  E-value: 7.01e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   1 MQVTRKETVYEMPGNQPKVGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVT 80
Cdd:COG2077    2 ATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  81 ISNNTKEEQAQWCGQEGVD-MIMLHDPAN-TFGEAYQIMIPD---FGHFARAIFVLDREGVIQHVEIVPEISHEPDYQAA 155
Cdd:COG2077   82 ISADLPFAQKRFCGAEGIDnVVTLSDFRDrSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDAA 161

                 ....*.
gi 495652454 156 IDAAKA 161
Cdd:COG2077  162 LAALKA 167
 
Name Accession Description Interval E-value
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-161 7.01e-71

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 211.10  E-value: 7.01e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   1 MQVTRKETVYEMPGNQPKVGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVT 80
Cdd:COG2077    2 ATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  81 ISNNTKEEQAQWCGQEGVD-MIMLHDPAN-TFGEAYQIMIPD---FGHFARAIFVLDREGVIQHVEIVPEISHEPDYQAA 155
Cdd:COG2077   82 ISADLPFAQKRFCGAEGIDnVVTLSDFRDrSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDAA 161

                 ....*.
gi 495652454 156 IDAAKA 161
Cdd:COG2077  162 LAALKA 167
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
18-158 7.24e-60

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: 182.40  E-value: 7.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  18 KVGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVTISNNTKEEQAQWCGQEG 97
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495652454  98 VD-MIMLHDPA-NTFGEAYQIMIPDFGHFARAIFVLDREGVIQHVEIVPEISHEPDYQAAIDA 158
Cdd:cd03014   81 VDnVTTLSDFRdHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
tpx PRK00522
thiol peroxidase;
1-161 3.04e-53

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 166.23  E-value: 3.04e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   1 MQVTRKETVYEMPGNQPKVGDKAADFRL--KSLEDKeyTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINF 78
Cdd:PRK00522   2 ATVTFKGNPVTVAGSLPQVGDKAPDFTLvaNDLSDV--SLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  79 VTISNNTKEEQAQWCGQEGVD-MIMLHD-PANTFGEAYQIMI---PDFGHFARAIFVLDREGVIQHVEIVPEISHEPDYQ 153
Cdd:PRK00522  80 LCISADLPFAQKRFCGAEGLEnVITLSDfRDHSFGKAYGVAIaegPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYD 159

                 ....*...
gi 495652454 154 AAIDAAKA 161
Cdd:PRK00522 160 AALAALKA 167
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
19-140 1.86e-24

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: 91.52  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   19 VGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINF--VTISNNTKEEQAQWCGQE 96
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVevLGVSVDSPESHKAFAEKY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 495652454   97 GVDMIMLHDPANTFGEAYQIMIPDFGHFARAIFVLDREGVIQHV 140
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
1-161 7.01e-71

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 211.10  E-value: 7.01e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   1 MQVTRKETVYEMPGNQPKVGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVT 80
Cdd:COG2077    2 ATVTLKGNPVTLVGNLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVPSLDTPVCATSTRKFNEEAAKLDNVVVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  81 ISNNTKEEQAQWCGQEGVD-MIMLHDPAN-TFGEAYQIMIPD---FGHFARAIFVLDREGVIQHVEIVPEISHEPDYQAA 155
Cdd:COG2077   82 ISADLPFAQKRFCGAEGIDnVVTLSDFRDrSFGKDYGVLIKEgplLGLLARAVFVLDENGKVVYTELVPEITDEPDYDAA 161

                 ....*.
gi 495652454 156 IDAAKA 161
Cdd:COG2077  162 LAALKA 167
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
18-158 7.24e-60

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: 182.40  E-value: 7.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  18 KVGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVTISNNTKEEQAQWCGQEG 97
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPVCATQTKRFNKEAAKLDNTVVLTISADLPFAQKRWCGAEG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495652454  98 VD-MIMLHDPA-NTFGEAYQIMIPDFGHFARAIFVLDREGVIQHVEIVPEISHEPDYQAAIDA 158
Cdd:cd03014   81 VDnVTTLSDFRdHSFGKAYGVLIKDLGLLARAVFVIDENGKVIYVELVPEITDEPDYEAALAA 143
tpx PRK00522
thiol peroxidase;
1-161 3.04e-53

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 166.23  E-value: 3.04e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   1 MQVTRKETVYEMPGNQPKVGDKAADFRL--KSLEDKeyTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINF 78
Cdd:PRK00522   2 ATVTFKGNPVTVAGSLPQVGDKAPDFTLvaNDLSDV--SLADFAGKRKVLNIFPSIDTGVCATSVRKFNQEAAELDNTVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  79 VTISNNTKEEQAQWCGQEGVD-MIMLHD-PANTFGEAYQIMI---PDFGHFARAIFVLDREGVIQHVEIVPEISHEPDYQ 153
Cdd:PRK00522  80 LCISADLPFAQKRFCGAEGLEnVITLSDfRDHSFGKAYGVAIaegPLKGLLARAVFVLDENNKVVYSELVPEITNEPDYD 159

                 ....*...
gi 495652454 154 AAIDAAKA 161
Cdd:PRK00522 160 AALAALKA 167
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
19-140 1.86e-24

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: 91.52  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   19 VGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINF--VTISNNTKEEQAQWCGQE 96
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVevLGVSVDSPESHKAFAEKY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 495652454   97 GVDMIMLHDPANTFGEAYQIMIPDFGHFARAIFVLDREGVIQHV 140
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLNEEEGGALRATFVIDPDGKVRYI 124
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
18-156 3.25e-21

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 83.96  E-value: 3.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454   18 KVGDKAADFRLKS--LEDKEYTLTDFLGKPTIISVVPDIVTRVCALQT---KRFNQEASQLD-DINFVTISNNTKEeQAQ 91
Cdd:pfam08534   1 KAGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHpylEKLNELYKEKGvDVVAVNSDNDAFF-VKR 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495652454   92 WCGQEGVDMIMLHDPANTFGEAY-QIMIPDFGHF--ARAIFVLDREGVIQHVEIVPEI-SHEPDYQAAI 156
Cdd:pfam08534  80 FWGKEGLPFPFLSDGNAAFTKALgLPIEEDASAGlrSPRYAVIDEDGKVVYLFVGPEPgVDVSDAEAVL 148
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
23-163 1.28e-20

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 82.22  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  23 AADFRLKSLEDKEYTLTDFLGKPTIISVVPDIvTRVCALQTKRFNQEASQLDD--INFVTISNNTKEEQAQWCGQEGVDM 100
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATW-CPGCTAELPELRDLYEEFKDkgVEVLGVSSDSDEAHKKFAEKYGLPF 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495652454 101 IMLHDPANTFGEAYQIMipdfghFARAIFVLDREGVIQHVeIVPEISHEPDYQAAIDAAKANL 163
Cdd:COG1225   80 PLLSDPDGEVAKAYGVR------GTPTTFLIDPDGKIRYV-WVGPVDPRPHLEEVLEALLAEL 135
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
17-158 1.61e-18

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: 76.93  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  17 PKVGDKAADFRLKSLEDKEYTLTDFLG-KPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVT--ISNNTKEEQAQWC 93
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGrKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVlgISVDSPFSLRAWA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495652454  94 GQEGVDMIMLHD--PANTFGEAYQIMIPDFGHFARAIFVLDREGVI--QHVEIVPEISHEPDYQAAIDA 158
Cdd:cd03018   81 EENGLTFPLLSDfwPHGEVAKAYGVFDEDLGVAERAVFVIDRDGIIryAWVSDDGEPRDLPDYDEALDA 149
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
19-142 1.49e-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: 61.75  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  19 VGDKAADFRLKSL----EDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVTI--SNNTKEEQAQW 92
Cdd:cd03015    1 VGKKAPDFKATAVvpngEFKEISLSDYKGKWVVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLgvSTDSHFSHLAW 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495652454  93 C-------GQEGVDMIMLHDPANTFGEAYQIMIPDFGHFARAIFVLDREGVIQHVEI 142
Cdd:cd03015   81 RntprkegGLGKINFPLLADPKKKISRDYGVLDEEEGVALRGTFIIDPEGIIRHITV 137
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
21-140 2.72e-11

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: 57.94  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  21 DKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVT--ISNNTKEEQAQWCGQEGV 98
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVigVSPDSVESHAKFAEKYGL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495652454  99 DMIMLHDPANTFGEAYQIMIPDFGHF---ARAIFVLDREGVIQHV 140
Cdd:cd03017   81 PFPLLSDPDGKLAKAYGVWGEKKKKYmgiERSTFLIDPDGKIVKV 125
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
25-140 1.65e-08

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 49.93  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  25 DFRLKSLEDKEYTLTDFLGKPTIISV-----VPdivtrvCALQTKRFN--QEASQLDDINFVTIS--NNTKEEQAQWCGQ 95
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFwaswcPP------CRAEMPELEalAKEYKDDGVEVVGVNvdDDDPAAVKAFLKK 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 495652454  96 EGVDMIMLHDPANTFGEAYQIM-IPdfghfarAIFVLDREGVIQHV 140
Cdd:cd02966   75 YGITFPVLLDPDGELAKAYGVRgLP-------TTFLIDRDGRIRAR 113
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
20-162 1.88e-06

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 45.31  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  20 GDKAADFRLKSLEDKEYTLTDFLGKPTIISVVpdivtrVCA------LQTKRFNQEASQL--DDINFVTISNNTKEEQaq 91
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMF------ICNhcpyvkAIEDRLNRLAKEYgaKGVAVVAINSNDIEAY-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  92 wcGQEGVDMI------------MLHDPANTFGEAYQIMI-PDFghfaraiFVLDREGVIQ--------HVEIVPEIShEP 150
Cdd:cd02969   73 --PEDSPENMkakakehgypfpYLLDETQEVAKAYGAACtPDF-------FLFDPDGKLVyrgriddsRPGNDPPVT-GR 142
                        170
                 ....*....|..
gi 495652454 151 DYQAAIDAAKAN 162
Cdd:cd02969  143 DLRAALDALLAG 154
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
18-140 3.85e-06

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 44.16  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  18 KVGDKAADFRLKSLEDKEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVT--ISNNTKEEQAQWCGQ 95
Cdd:PRK09437   5 KAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVlgISTDKPEKLSRFAEK 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495652454  96 EGVDMIMLHDPANTFGEAY------QIMIPDFGHFARAIFVLDREGVIQHV 140
Cdd:PRK09437  85 ELLNFTLLSDEDHQVAEQFgvwgekKFMGKTYDGIHRISFLIDADGKIEHV 135
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
35-145 4.06e-05

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 41.90  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  35 EYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDD--INFVTISNNTKEEQAQWCGQE----GVDMIMLHDPAN 108
Cdd:PRK10382  23 EVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKlgVDVYSVSTDTHFTHKAWHSSSetiaKIKYAMIGDPTG 102
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495652454 109 TFGEAYQIMIPDFGHFARAIFVLDREGVIQHVEIVPE 145
Cdd:PRK10382 103 ALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAE 139
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
23-137 7.64e-05

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 40.66  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  23 AADFRLKSLEDKEYTLTDFLGKPTIISVV----PDivtrVCALQTKRFNQ-----EASQLDDINFVTIS----NNTKEEQ 89
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGythcPD----VCPTTLANLAQalkqlGADGGDDVQVVFISvdpeRDTPEVL 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  90 AQWCGQEGVDMIML-------HDPANTFGEAYQ-----IMIPDFGHFArAIFVLDREGVI 137
Cdd:cd02968   78 KAYAKAFGPGWIGLtgtpeeiEALAKAFGVYYEkvpedDGDYLVDHSA-AIYLVDPDGKL 136
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
34-142 2.16e-03

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 37.19  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495652454  34 KEYTLTDFLGKPTIISVVPDIVTRVCALQTKRFNQEASQLDDINFVTISNNTKEEQA--QWCGQE-------GVDMIMLH 104
Cdd:PTZ00253  27 KKISLSSYKGKWVVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAhlQWTLQErkkgglgTMAIPMLA 106
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495652454 105 DPANTFGEAYQIMIPDFGHFARAIFVLDREGVIQHVEI 142
Cdd:PTZ00253 107 DKTKSIARSYGVLEEEQGVAYRGLFIIDPKGMLRQITV 144
 
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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