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Conserved domains on  [gi|356515995|ref|XP_003526682|]
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uncharacterized protein LOC100806693 [Glycine max]

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. ...
 65-240 1.47e-96

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: 279.51  E-value: 1.47e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  65 GFRTPQFQLPEPLTGTtWTLDDFEAYPALLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHPQDGPEF 144
Cdd:cd02969    1 GSPAPDFSLPDTDGKT-YSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995 145 MAEDAKLFGYPFPYLYDESQDVAQHFGAVCTPEFYLFKKDGRrpfeLVYHGQFDDSRPSNNVPVTGRDLSLAIDRVLSGQ 224
Cdd:cd02969   80 MKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGK----LVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGK 155

                        170
                 ....*....|....*.
gi 356515995 225 PVPSEQKPSVGCSIKW 240
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. ...
 65-240 1.47e-96

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: 279.51  E-value: 1.47e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  65 GFRTPQFQLPEPLTGTtWTLDDFEAYPALLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHPQDGPEF 144
Cdd:cd02969    1 GSPAPDFSLPDTDGKT-YSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995 145 MAEDAKLFGYPFPYLYDESQDVAQHFGAVCTPEFYLFKKDGRrpfeLVYHGQFDDSRPSNNVPVTGRDLSLAIDRVLSGQ 224
Cdd:cd02969   80 MKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGK----LVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGK 155

                        170
                 ....*....|....*.
gi 356515995 225 PVPSEQKPSVGCSIKW 240
Cdd:cd02969  156 PVPVPQTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-201 1.67e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 97.24  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  69 PQFQLPEpLTGTTWTLDDFEAYPaLLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHpqdgpefmAED 148
Cdd:COG1225    2 PDFTLPD-LDGKTVSLSDLRGKP-VVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAH--------KKF 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 356515995 149 AKLFGYPFPYLYDESQDVAQHFGAVCTPEFYLFKKDGRrpFELVYHGQFDDSR 201
Cdd:COG1225   72 AEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGK--IRYVWVGPVDPRP 122
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 69-185 6.81e-14

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: 66.09  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995   69 PQFQLPEpLTGTTWTLDDFEAYPALLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHPQdgpeFMAED 148
Cdd:pfam00578   6 PDFELPD-GDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKA----FAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 356515995  149 aklfGYPFPYLYDESQDVAQHFGA------VCTPEFYLFKKDG 185
Cdd:pfam00578  81 ----GLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDG 119
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 65-240 1.47e-96

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: 279.51  E-value: 1.47e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  65 GFRTPQFQLPEPLTGTtWTLDDFEAYPALLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHPQDGPEF 144
Cdd:cd02969    1 GSPAPDFSLPDTDGKT-YSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995 145 MAEDAKLFGYPFPYLYDESQDVAQHFGAVCTPEFYLFKKDGRrpfeLVYHGQFDDSRPSNNVPVTGRDLSLAIDRVLSGQ 224
Cdd:cd02969   80 MKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGK----LVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGK 155

                        170
                 ....*....|....*.
gi 356515995 225 PVPSEQKPSVGCSIKW 240
Cdd:cd02969  156 PVPVPQTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-201 1.67e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 97.24  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  69 PQFQLPEpLTGTTWTLDDFEAYPaLLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHpqdgpefmAED 148
Cdd:COG1225    2 PDFTLPD-LDGKTVSLSDLRGKP-VVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAH--------KKF 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 356515995 149 AKLFGYPFPYLYDESQDVAQHFGAVCTPEFYLFKKDGRrpFELVYHGQFDDSR 201
Cdd:COG1225   72 AEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGK--IRYVWVGPVDPRP 122
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 69-185 6.81e-14

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: 66.09  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995   69 PQFQLPEpLTGTTWTLDDFEAYPALLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHPQdgpeFMAED 148
Cdd:pfam00578   6 PDFELPD-GDGGTVSLSDYRGKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKA----FAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 356515995  149 aklfGYPFPYLYDESQDVAQHFGA------VCTPEFYLFKKDG 185
Cdd:pfam00578  81 ----GLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDG 119
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 69-186 2.19e-13

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 65.10  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  69 PQFQLPePLTGTTWTLDDFEAYPaLLVMFICNHCPFVKHLKKDIVKLTKFYmeKGLAVIAISSNsvathpqDGPEFMAED 148
Cdd:COG0526    9 PDFTLT-DLDGKPLSLADLKGKP-VLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVD-------ENPEAVKAF 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 356515995 149 AKLFGYPFPYLYDESQDVAQHFGAVCTPEFYLFKKDGR 186
Cdd:COG0526   78 LKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGK 115
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 70-186 5.71e-13

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: 63.41  E-value: 5.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  70 QFQLPePLTGTTWTLDDFEAYPALLVMFI--CNHC----PFVKHLKKDivkltkfYMEKGLAVIAISSNSvaTHPQDGPE 143
Cdd:cd02966    1 DFSLP-DLDGKPVSLSDLKGKVVLVNFWAswCPPCraemPELEALAKE-------YKDDGVEVVGVNVDD--DDPAAVKA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 356515995 144 FMAEdaklFGYPFPYLYDESQDVAQHFGAVCTPEFYLFKKDGR 186
Cdd:cd02966   71 FLKK----YGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGR 109
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 69-186 1.59e-11

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 60.46  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995   69 PQFQLPEPLT-GTTWTLDDFEAYPALLVMFICNHCPFVKHLKKDIVKLTKFYMEKGLAVIAISSNSVATHPQdgpEFMAE 147
Cdd:pfam08534   7 PDFTLPDAATdGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVK---RFWGK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 356515995  148 DaklfGYPFPYLYDESQDVAQHFGA---------VCTPEFYLFKKDGR 186
Cdd:pfam08534  84 E----GLPFPFLSDGNAAFTKALGLpieedasagLRSPRYAVIDEDGK 127
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 67-173 2.85e-04

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: 40.03  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356515995  67 RTPQFQLPEpLTGTTWTLDDFEAYPALLVMFICN-HCPFVKHLKKDIVKLTKFYMEKGLAVIAISsnsvathpQDGPEFM 145
Cdd:cd02970    1 TAPDFELPD-AGGETVTLSALLGEGPVVVVFYRGfGCPFCREYLRALSKLLPELDALGVELVAVG--------PESPEKL 71

                         90       100
                 ....*....|....*....|....*...
gi 356515995 146 AEDAKLFGYPFPYLYDESQDVAQHFGAV 173
Cdd:cd02970   72 EAFDKGKFLPFPVYADPDRKLYRALGLV 99
 
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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