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Conserved domains on  [gi|445976602|ref|WP_000054457|]
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MULTISPECIES: thioredoxin family protein [Leptospira]

Protein Classification

thioredoxin family protein( domain architecture ID 10121933)

thioredoxin family protein with similarity to peroxiredoxins, may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein thiol or disulfide bonds using an active site disulfide or dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035
PubMed:  15518547|12517450|15558583|10049365|9099998|11441809|12074972|30367780
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-181 2.32e-88

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: 256.40  E-value: 2.32e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  12 GSLLPDFRLADPNGKTYSSDQISGSTGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPNIHPDYPDDSPEMM 91
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  92 LVKIKEWKISFPYLVDETQEVSKKLKAMCTPDIYLYDGEQRLYYHGRMDDNWK-NEKQVSRKELEYAVHQLVKGNPAPIN 170
Cdd:cd02969   81 KAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPgNDPPVTGRDLRAALDALLAGKPVPVP 160

                        170
                 ....*....|.
gi 445976602 171 QMPSMGCSIKW 181
Cdd:cd02969  161 QTPSIGCSIKW 171
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-181 2.32e-88

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: 256.40  E-value: 2.32e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  12 GSLLPDFRLADPNGKTYSSDQISGSTGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPNIHPDYPDDSPEMM 91
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  92 LVKIKEWKISFPYLVDETQEVSKKLKAMCTPDIYLYDGEQRLYYHGRMDDNWK-NEKQVSRKELEYAVHQLVKGNPAPIN 170
Cdd:cd02969   81 KAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPgNDPPVTGRDLRAALDALLAGKPVPVP 160

                        170
                 ....*....|.
gi 445976602 171 QMPSMGCSIKW 181
Cdd:cd02969  161 QTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
16-166 4.74e-26

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 96.86  E-value: 4.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  16 PDFRLADPNGKTYSSDQISGStGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPnihpdypdDSPEMMLVKI 95
Cdd:COG1225    2 PDFTLPDLDGKTVSLSDLRGK-PVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS--------DSDEAHKKFA 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445976602  96 KEWKISFPYLVDETQEVSKKLKAMCTPDIYLYDGEQRLYYH--GRMDDnwknekqvsRKELEYAVHQLVKGNP 166
Cdd:COG1225   73 EKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVwvGPVDP---------RPHLEEVLEALLAELK 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 11-136 5.53e-16

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: 70.33  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602   11 LGSLLPDFRLADPNGKTYSSDQISGSTGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPnihpdypdDSPEM 90
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSV--------DSPES 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 445976602   91 MLVKIKEWKISFPYLVDETQEVSKKLKAM------CTPDIYLYDGEQRLYYH 136
Cdd:pfam00578  73 HKAFAEKYGLPFPLLSDPDGEVARAYGVLneeeggALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-181 2.32e-88

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: 256.40  E-value: 2.32e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  12 GSLLPDFRLADPNGKTYSSDQISGSTGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPNIHPDYPDDSPEMM 91
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  92 LVKIKEWKISFPYLVDETQEVSKKLKAMCTPDIYLYDGEQRLYYHGRMDDNWK-NEKQVSRKELEYAVHQLVKGNPAPIN 170
Cdd:cd02969   81 KAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPgNDPPVTGRDLRAALDALLAGKPVPVP 160

                        170
                 ....*....|.
gi 445976602 171 QMPSMGCSIKW 181
Cdd:cd02969  161 QTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
16-166 4.74e-26

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 96.86  E-value: 4.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  16 PDFRLADPNGKTYSSDQISGStGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPnihpdypdDSPEMMLVKI 95
Cdd:COG1225    2 PDFTLPDLDGKTVSLSDLRGK-PVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS--------DSDEAHKKFA 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445976602  96 KEWKISFPYLVDETQEVSKKLKAMCTPDIYLYDGEQRLYYH--GRMDDnwknekqvsRKELEYAVHQLVKGNP 166
Cdd:COG1225   73 EKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVwvGPVDP---------RPHLEEVLEALLAELK 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 11-136 5.53e-16

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: 70.33  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602   11 LGSLLPDFRLADPNGKTYSSDQISGSTGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPnihpdypdDSPEM 90
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSV--------DSPES 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 445976602   91 MLVKIKEWKISFPYLVDETQEVSKKLKAM------CTPDIYLYDGEQRLYYH 136
Cdd:pfam00578  73 HKAFAEKYGLPFPLLSDPDGEVARAYGVLneeeggALRATFVIDPDGKVRYI 124
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 17-136 1.99e-11

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: 58.02  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  17 DFRLADPNGKTYSSDQISGSTGLL-LIVTCnhCPYAQAIWPRLIRFAGEILSLGVRTVAINpnihpdYPDDSPEMMLVKI 95
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVnFWASW--CPPCRAEMPELEALAKEYKDDGVEVVGVN------VDDDDPAAVKAFL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 445976602  96 KEWKISFPYLVDETQEVSKKLKAMCTPDIYLYDGEQRLYYH 136
Cdd:cd02966   73 KKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRAR 113
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 10-116 8.43e-10

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 54.68  E-value: 8.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602   10 PLGSLLPDFRLADP--NGKTYSSDQISGSTGLLLIVTCNHCPYAQAIWPRLIRFAGEILSLGVRTVAINPNihpdypDDS 87
Cdd:pfam08534   1 KAGDKAPDFTLPDAatDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSD------NDA 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 445976602   88 PEMMlvkiKEWK---ISFPYLVDETQEVSKKL 116
Cdd:pfam08534  75 FFVK----RFWGkegLPFPFLSDGNAAFTKAL 102
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 15-145 1.41e-06

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 45.81  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445976602  15 LPDFRLADPNGKTYSSDQISGSTGLLLIVTCN-HCPYAQAIWPRLIRFAGEILSLGVRTVAINPnihpdypdDSPEMMLV 93
Cdd:cd02970    2 APDFELPDAGGETVTLSALLGEGPVVVVFYRGfGCPFCREYLRALSKLLPELDALGVELVAVGP--------ESPEKLEA 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445976602  94 KIKEWKISFPYLVDETQEVSKKLKAMctpdIYLYDGEQRLYYHGRMDDNWKN 145
Cdd:cd02970   74 FDKGKFLPFPVYADPDRKLYRALGLV----RSLPWSNTPRALWKNAAIGFRG 121
 
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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