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Conserved domains on  [gi|1956496185|ref|WP_200376727|]
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redoxin domain-containing protein [Thiocystis violacea]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 32-206 2.70e-52

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02969:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 171  Bit Score: 165.88  E-value: 2.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  32 GQPAPAFSVSDTSGKVWTLETLAGRPA-ILEWTNHDCPFVVKHYGAGNMQALQAEAKdaGYVWLSVVSSAPGKQGHVSPS 110
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFADGKAlVVMFICNHCPYVKAIEDRLNRLAKEYGAK--GVAVVAINSNDIEAYPEDSPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185 111 EADDLTQRRSAvPTAVLLDSDGVMGRTYGAMTTPHMYVIDAGGTLAYMGGIDDRPTTNpaDIQGATNHVRAAMTDLAAGQ 190
Cdd:cd02969    79 NMKAKAKEHGY-PFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGN--DPPVTGRDLRAALDALLAGK 155

                         170
                  ....*....|....*.
gi 1956496185 191 AVGTPLTRPYGCSVKY 206
Cdd:cd02969   156 PVPVPQTPSIGCSIKW 171
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 32-206 2.70e-52

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: 165.88  E-value: 2.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  32 GQPAPAFSVSDTSGKVWTLETLAGRPA-ILEWTNHDCPFVVKHYGAGNMQALQAEAKdaGYVWLSVVSSAPGKQGHVSPS 110
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFADGKAlVVMFICNHCPYVKAIEDRLNRLAKEYGAK--GVAVVAINSNDIEAYPEDSPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185 111 EADDLTQRRSAvPTAVLLDSDGVMGRTYGAMTTPHMYVIDAGGTLAYMGGIDDRPTTNpaDIQGATNHVRAAMTDLAAGQ 190
Cdd:cd02969    79 NMKAKAKEHGY-PFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGN--DPPVTGRDLRAALDALLAGK 155

                         170
                  ....*....|....*.
gi 1956496185 191 AVGTPLTRPYGCSVKY 206
Cdd:cd02969   156 PVPVPQTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
35-191 9.16e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 94.16  E-value: 9.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  35 APAFSVSDTSGKVWTLETLAGRPAILEWTNHDCPFVVKHygAGNMQALQAEAKDAGYVWLSvvssapgkqghVSPSEADD 114
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAE--LPELRDLYEEFKDKGVEVLG-----------VSSDSDEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185 115 LTQ--RRSAVPTAVLLDSDGVMGRTYGAMTTPHMYVIDAGGTLAY--MGGIDDRPttnpadiqgatnHVRAAMTDLAAGQ 190
Cdd:COG1225    68 HKKfaEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYvwVGPVDPRP------------HLEEVLEALLAEL 135


                  .
gi 1956496185 191 A 191
Cdd:COG1225   136 K 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 31-158 5.63e-13

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 63.01  E-value: 5.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  31 VGQPAPAFSVSDTSGKVWTLETLAGRPAILE-WTNHDCPFVVKHYGAgnMQALQAEAKDAGYVWLSVvsSAPGKQGHVSP 109
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFfYPADWTPVCTTELPA--LADLYEEFKKLGVEVLGV--SVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1956496185 110 SEADDLtqrrsavPTAVLLDSDGVMGRTYGAMTTPHM------YVIDAGGTLAYM 158
Cdd:pfam00578  77 AEKYGL-------PFPLLSDPDGEVARAYGVLNEEEGgalratFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 32-206 2.70e-52

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: 165.88  E-value: 2.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  32 GQPAPAFSVSDTSGKVWTLETLAGRPA-ILEWTNHDCPFVVKHYGAGNMQALQAEAKdaGYVWLSVVSSAPGKQGHVSPS 110
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFADGKAlVVMFICNHCPYVKAIEDRLNRLAKEYGAK--GVAVVAINSNDIEAYPEDSPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185 111 EADDLTQRRSAvPTAVLLDSDGVMGRTYGAMTTPHMYVIDAGGTLAYMGGIDDRPTTNpaDIQGATNHVRAAMTDLAAGQ 190
Cdd:cd02969    79 NMKAKAKEHGY-PFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGN--DPPVTGRDLRAALDALLAGK 155

                         170
                  ....*....|....*.
gi 1956496185 191 AVGTPLTRPYGCSVKY 206
Cdd:cd02969   156 PVPVPQTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
35-191 9.16e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 94.16  E-value: 9.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  35 APAFSVSDTSGKVWTLETLAGRPAILEWTNHDCPFVVKHygAGNMQALQAEAKDAGYVWLSvvssapgkqghVSPSEADD 114
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAE--LPELRDLYEEFKDKGVEVLG-----------VSSDSDEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185 115 LTQ--RRSAVPTAVLLDSDGVMGRTYGAMTTPHMYVIDAGGTLAY--MGGIDDRPttnpadiqgatnHVRAAMTDLAAGQ 190
Cdd:COG1225    68 HKKfaEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYvwVGPVDPRP------------HLEEVLEALLAEL 135


                  .
gi 1956496185 191 A 191
Cdd:COG1225   136 K 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 31-158 5.63e-13

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 63.01  E-value: 5.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  31 VGQPAPAFSVSDTSGKVWTLETLAGRPAILE-WTNHDCPFVVKHYGAgnMQALQAEAKDAGYVWLSVvsSAPGKQGHVSP 109
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFfYPADWTPVCTTELPA--LADLYEEFKKLGVEVLGV--SVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1956496185 110 SEADDLtqrrsavPTAVLLDSDGVMGRTYGAMTTPHM------YVIDAGGTLAYM 158
Cdd:pfam00578  77 AEKYGL-------PFPLLSDPDGEVARAYGVLNEEEGgalratFVIDPDGKVRYI 124
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 31-162 2.09e-12

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 62.01  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  31 VGQPAPAFSVSDTSGKVWTLETLAGRPAILEWTNHDCPFVVKHygAGNMQALQAEAKDAGYVWLSVVSSAPGKQGHVsps 110
Cdd:COG0526     4 VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAE--MPVLKELAEEYGGVVFVGVDVDENPEAVKAFL--- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1956496185 111 eaddltqRRSAVPTAVLLDSDGVMGRTYGAMTTPHMYVIDAGGTLAY--MGGID 162
Cdd:COG0526    79 -------KELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVArhVGPLS 125
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 37-157 1.31e-09

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: 53.78  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496185  37 AFSVSDTSGKVWTLETLAGRPAILE-WTnHDCPFVVKHygAGNMQALQAEAKDAGYVWLSVvssapgkqgHVSPSEADDL 115
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNfWA-SWCPPCRAE--MPELEALAKEYKDDGVEVVGV---------NVDDDDPAAV 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1956496185 116 TQ--RRSAVPTAVLLDSDGVMGRTYGAMTTPHMYVIDAGGTLAY 157
Cdd:cd02966    69 KAflKKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRA 112
 
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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