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Conserved domains on  [gi|1817133494|ref|WP_164025356|]
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DsbE family thiol:disulfide interchange protein [Rhizobium leguminosarum]

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 ...
 22-195 5.27e-81

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 TIGR00385:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 173  Bit Score: 238.52  E-value: 5.27e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  22 LLPLVVFGGIAAtAAKMLYDQDFHGKNIAEIPSALIGTKAPALNLPPLDGaDLPALT-DVAIKGKLTLVNVFASWCLPCR 100
Cdd:TIGR00385   2 LLPLIIFLGIAA-ALLWQLARNAEGDDPKALPSALIGKPVPAFRLASLDE-PGQFYTaDVLTQGKPVLLNVWASWCPPCR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 101 DEHPILKELAKDGrLNIVAINYKDQSDNALRFLGELGNPFRAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPF 180
Cdd:TIGR00385  80 AEHPYLNELAKQG-LPIVGVDYKDDRQNAIKFLKELGNPYQLSLFDPDGMLGLDLGVYGAPETFLVDGNGVIRYRHAGPL 158

                         170
                  ....*....|....*
gi 1817133494 181 DDISLKEGLFPAMEK 195
Cdd:TIGR00385 159 NPEVWTEEFLPLWEK 173
 
Name Accession Description Interval E-value
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 22-195 5.27e-81

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 238.52  E-value: 5.27e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  22 LLPLVVFGGIAAtAAKMLYDQDFHGKNIAEIPSALIGTKAPALNLPPLDGaDLPALT-DVAIKGKLTLVNVFASWCLPCR 100
Cdd:TIGR00385   2 LLPLIIFLGIAA-ALLWQLARNAEGDDPKALPSALIGKPVPAFRLASLDE-PGQFYTaDVLTQGKPVLLNVWASWCPPCR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 101 DEHPILKELAKDGrLNIVAINYKDQSDNALRFLGELGNPFRAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPF 180
Cdd:TIGR00385  80 AEHPYLNELAKQG-LPIVGVDYKDDRQNAIKFLKELGNPYQLSLFDPDGMLGLDLGVYGAPETFLVDGNGVIRYRHAGPL 158

                         170
                  ....*....|....*
gi 1817133494 181 DDISLKEGLFPAMEK 195
Cdd:TIGR00385 159 NPEVWTEEFLPLWEK 173
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 61-182 1.80e-60

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 184.70  E-value: 1.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  61 APALNLPPLDGADlPALTDVAIKGKLTLVNVFASWCLPCRDEHPILKELAKDGRLNIVAINYKDQSDNALRFLGELGNPF 140
Cdd:cd03010     3 APAFSLPALPGPD-KTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQGRVPIYGINYKDNPENALAWLARHGNPY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1817133494 141 RAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPFDD 182
Cdd:cd03010    82 AAVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPLTP 123
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 57-195 7.43e-42

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 137.90  E-value: 7.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  57 IGTKAPALNLPPLDGAdlpALTDVAIKGKLTLVNVFASWCLPCRDEHPILKELAKD-GRLNIVAINYKDQSDNALRFLGE 135
Cdd:COG0526     4 VGKPAPDFTLTDLDGK---PLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEyGGVVFVGVDVDENPEAVKAFLKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 136 LGNPFRaIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPFDDISLKEGLFPAMEK 195
Cdd:COG0526    81 LGLPYP-VLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 22-195 1.51e-33

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 118.17  E-value: 1.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  22 LLPLVVFGGIAATAAKMLYdQDFHGKNIAEIPSALIGTKAPALNLPPLDGADLPALTDVAIKGKLTLVNVFASWCLPCRD 101
Cdd:PRK15412    7 LIPLIIFLAIAAALLWQLA-RNAEGDDPTNLESALIGKPVPKFRLESLENPGQFYQADVLTQGKPVLLNVWATWCPTCRA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 102 EHPILKELAKDGrLNIVAINYKDQSDNALRFLGELGNPFRAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPFD 181
Cdd:PRK15412   86 EHQYLNQLSAQG-IRVVGMNYKDDRQKAISWLKELGNPYALSLFDGDGMLGLDLGVYGAPETFLIDGNGIIRYRHAGDLN 164

                         170
                  ....*....|....
gi 1817133494 182 DISLKEGLFPAMEK 195
Cdd:PRK15412  165 PRVWESEIKPLWEK 178
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 57-175 9.97e-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: 64.94  E-value: 9.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  57 IGTKAPALNLPPLDGADLpALTDvaIKGKLTLVNVFAS-WCLPCRDEHP----ILKELAKDGrLNIVAINyKDQSDNALR 131
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTV-SLSD--YRGKWVVLFFYPAdWTPVCTTELPaladLYEEFKKLG-VEVLGVS-VDSPESHKA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1817133494 132 FLGELGNPFRaIGIDPNGKAAIDWGVY------GIPESYLVGPDGTILYK 175
Cdd:pfam00578  76 FAEKYGLPFP-LLSDPDGEVARAYGVLneeeggALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 22-195 5.27e-81

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 238.52  E-value: 5.27e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  22 LLPLVVFGGIAAtAAKMLYDQDFHGKNIAEIPSALIGTKAPALNLPPLDGaDLPALT-DVAIKGKLTLVNVFASWCLPCR 100
Cdd:TIGR00385   2 LLPLIIFLGIAA-ALLWQLARNAEGDDPKALPSALIGKPVPAFRLASLDE-PGQFYTaDVLTQGKPVLLNVWASWCPPCR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 101 DEHPILKELAKDGrLNIVAINYKDQSDNALRFLGELGNPFRAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPF 180
Cdd:TIGR00385  80 AEHPYLNELAKQG-LPIVGVDYKDDRQNAIKFLKELGNPYQLSLFDPDGMLGLDLGVYGAPETFLVDGNGVIRYRHAGPL 158

                         170
                  ....*....|....*
gi 1817133494 181 DDISLKEGLFPAMEK 195
Cdd:TIGR00385 159 NPEVWTEEFLPLWEK 173
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 61-182 1.80e-60

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 184.70  E-value: 1.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  61 APALNLPPLDGADlPALTDVAIKGKLTLVNVFASWCLPCRDEHPILKELAKDGRLNIVAINYKDQSDNALRFLGELGNPF 140
Cdd:cd03010     3 APAFSLPALPGPD-KTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQGRVPIYGINYKDNPENALAWLARHGNPY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1817133494 141 RAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPFDD 182
Cdd:cd03010    82 AAVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPLTP 123
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 57-195 7.43e-42

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 137.90  E-value: 7.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  57 IGTKAPALNLPPLDGAdlpALTDVAIKGKLTLVNVFASWCLPCRDEHPILKELAKD-GRLNIVAINYKDQSDNALRFLGE 135
Cdd:COG0526     4 VGKPAPDFTLTDLDGK---PLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEyGGVVFVGVDVDENPEAVKAFLKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 136 LGNPFRaIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPFDDISLKEGLFPAMEK 195
Cdd:COG0526    81 LGLPYP-VLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 22-195 1.51e-33

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 118.17  E-value: 1.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  22 LLPLVVFGGIAATAAKMLYdQDFHGKNIAEIPSALIGTKAPALNLPPLDGADLPALTDVAIKGKLTLVNVFASWCLPCRD 101
Cdd:PRK15412    7 LIPLIIFLAIAAALLWQLA-RNAEGDDPTNLESALIGKPVPKFRLESLENPGQFYQADVLTQGKPVLLNVWATWCPTCRA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 102 EHPILKELAKDGrLNIVAINYKDQSDNALRFLGELGNPFRAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPFD 181
Cdd:PRK15412   86 EHQYLNQLSAQG-IRVVGMNYKDDRQKAISWLKELGNPYALSLFDGDGMLGLDLGVYGAPETFLIDGNGIIRYRHAGDLN 164

                         170
                  ....*....|....
gi 1817133494 182 DISLKEGLFPAMEK 195
Cdd:PRK15412  165 PRVWESEIKPLWEK 178
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 61-178 2.96e-33

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: 115.03  E-value: 2.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  61 APALNLPPLDGADLpaltdvaiKGKLTLVNVFASWCLPCRDEHPILKELA---KDGRLNIVAINYKDQS-DNALRFLGEL 136
Cdd:cd02966     4 LPDLDGKPVSLSDL--------KGKVVLVNFWASWCPPCRAEMPELEALAkeyKDDGVEVVGVNVDDDDpAAVKAFLKKY 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1817133494 137 GNPFrAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVG 178
Cdd:cd02966    76 GITF-PVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
61-182 9.85e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 93.78  E-value: 9.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  61 APALNLPPLDGADLpALTDvaIKGKLTLVNVFASWCLPCRDEHPILKELA---KDGRLNIVAINYkDQSDNALRFLGELG 137
Cdd:COG1225     1 APDFTLPDLDGKTV-SLSD--LRGKPVVLYFYATWCPGCTAELPELRDLYeefKDKGVEVLGVSS-DSDEAHKKFAEKYG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1817133494 138 NPFRaIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKRVGPFDD 182
Cdd:COG1225    77 LPFP-LLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDP 120
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 57-175 9.97e-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: 64.94  E-value: 9.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  57 IGTKAPALNLPPLDGADLpALTDvaIKGKLTLVNVFAS-WCLPCRDEHP----ILKELAKDGrLNIVAINyKDQSDNALR 131
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTV-SLSD--YRGKWVVLFFYPAdWTPVCTTELPaladLYEEFKKLG-VEVLGVS-VDSPESHKA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1817133494 132 FLGELGNPFRaIGIDPNGKAAIDWGVY------GIPESYLVGPDGTILYK 175
Cdd:pfam00578  76 FAEKYGLPFP-LLSDPDGEVARAYGVLneeeggALRATFVIDPDGKVRYI 124
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 58-187 3.22e-13

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 64.31  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  58 GTKAPALNLPplDGADLPALTDVAI-KGKLTLVNVFAS-WCLPCRDEHPILK---ELAKDGRLNIVAINYKDQSDNALRF 132
Cdd:pfam08534   3 GDKAPDFTLP--DAATDGNTVSLSDfKGKKVVLNFWPGaFCPTCSAEHPYLEklnELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817133494 133 LGELGNPFRaIGIDPNGKAAIDWGV---------YGIPESYLVGPDGTILYKRVGPFDDISLKE 187
Cdd:pfam08534  81 WGKEGLPFP-FLSDGNAAFTKALGLpieedasagLRSPRYAVIDEDGKVVYLFVGPEPGVDVSD 143
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 62-170 3.89e-12

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 60.77  E-value: 3.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  62 PALNLPPLDGADLPALtdvAIKGKLTLVNVFASWCLPCRDEHPILKELAKDgrLNIVAINYKDQSDNAL-RFLGELGNPF 140
Cdd:cd03011     1 PLFTATTLDGEQFDLE---SLSGKPVLVYFWATWCPVCRFTSPTVNQLAAD--YPVVSVALRSGDDGAVaRFMQKKGYGF 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1817133494 141 RAIGiDPNGKAAIDWGVYGIPESYLVGPDG 170
Cdd:cd03011    76 PVIN-DPDGVISARWGVSVTPAIVIVDPGG 104
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 84-172 1.85e-11

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 58.09  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  84 GKLTLVNVFASWCLPCRDEHPILKEL----AKDGRLNIVAINYkDQSDNALR-FLGELGNPFRAI--GIDPNGKAAIDWG 156
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELyeklKKKKNVEIVFVSL-DRDLEEFKdYLKKMPKDWLSVpfDDDERNELKRKYG 79

                          90
                  ....*....|....*.
gi 1817133494 157 VYGIPESYLVGPDGTI 172
Cdd:pfam13905  80 VNAIPTLVLLDPNGEV 95
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
57-172 7.15e-09

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 53.08  E-value: 7.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  57 IGTKAPALNLPPLDGADLpALTDvaIKGKLTLVNVFASWCLPCRDEHPILKELA---KDGRLNIVAINYKDQSDNALRFL 133
Cdd:PRK03147   37 VGKEAPNFVLTDLEGKKI-ELKD--LKGKGVFLNFWGTWCKPCEKEMPYMNELYpkyKEKGVEIIAVNVDETELAVKNFV 113

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1817133494 134 GELGNPFrAIGIDPNGKAAIDWGVYGIPESYLVGPDGTI 172
Cdd:PRK03147  114 NRYGLTF-PVAIDKGRQVIDAYGVGPLPTTFLIDKDGKV 151
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 78-187 6.63e-07

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 45.97  E-value: 6.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  78 TDVAIKGKLTLVNVFASWCLPCRDEHPILKELAKD--GRLNIVAINykdqsdnalrflgelgnpfraigIDPNGKAAIDW 155
Cdd:COG3118    12 EEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEygGKVKFVKVD-----------------------VDENPELAAQF 68

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1817133494 156 GVYGIPESYLVgPDGTILYKRVGPFDDISLKE 187
Cdd:COG3118    69 GVRSIPTLLLF-KDGQPVDRFVGALPKEQLRE 99
trxA PRK09381
thioredoxin TrxA;
78-189 1.18e-06

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 45.44  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  78 TDVAIKGKLTLVNVFASWCLPCRDEHPILKELAKD--GRLNIVAINykdqsdnalrflgelgnpfraigIDPNGKAAIDW 155
Cdd:PRK09381   15 TDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEyqGKLTVAKLN-----------------------IDQNPGTAPKY 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1817133494 156 GVYGIPeSYLVGPDGTILYKRVGPFDDISLKEGL 189
Cdd:PRK09381   72 GIRGIP-TLLLFKNGEVAATKVGALSKGQLKEFL 104
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 83-187 1.35e-06

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 44.86  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  83 KGKLTLVNVFASWCLPCRDEHPILKELAKD-GRLNIVAINykdqsdnalrflgelgnpfraigIDPNGKAAIDWGVYGIP 161
Cdd:cd02947     9 SAKPVVVDFWAPWCGPCKAIAPVLEELAEEyPKVKFVKVD-----------------------VDENPELAEEYGVRSIP 65

                          90       100
                  ....*....|....*....|....*.
gi 1817133494 162 eSYLVGPDGTILYKRVGPFDDISLKE 187
Cdd:cd02947    66 -TFLFFKNGKEVDRVVGADPKEELEE 90
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 78-132 1.57e-05

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 42.28  E-value: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1817133494  78 TDVAIKGKLTLVNVFASWCLPCRDEHPILKELAKD--GRLNIVAINYKDQSDNALRF 132
Cdd:TIGR01068   8 ETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyeGKVKFVKLNVDENPDIAAKY 64
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 79-121 2.24e-05

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 41.83  E-value: 2.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1817133494  79 DVAIKGKLTLVNVFASWCLPCRDEHPILKELAK----DGRLNIVAIN 121
Cdd:cd02961    10 ELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKelkgDGKVVVAKVD 56
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 81-173 2.47e-05

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 42.21  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  81 AIKGKLTLVNVFASWCLPCRDEHPILKEL-----AKDGRLNIVAINyKDQSDNAL-RFLGELGN----PFRaigiDPNGK 150
Cdd:cd02964    14 ALEGKTVGLYFSASWCPPCRAFTPKLVEFyeklkEEGKNFEIVFVS-RDRSEESFnEYFSEMPPwlavPFE----DEELR 88

                          90       100
                  ....*....|....*....|....*
gi 1817133494 151 AAID--WGVYGIPESYLVGPDGTIL 173
Cdd:cd02964    89 ELLEkqFKVEGIPTLVVLKPDGDVV 113
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 58-202 2.61e-04

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: 39.91  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  58 GTKAPALNLPPLDGaDLPALTDVAiKGKLTLVNVFASWClPCRDEH-PILKELAKD---GRLNIVAIN------YKDQS- 126
Cdd:cd02969     1 GSPAPDFSLPDTDG-KTYSLADFA-DGKALVVMFICNHC-PYVKAIeDRLNRLAKEygaKGVAVVAINsndieaYPEDSp 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494 127 DNALRFLGELGNPFrAIGIDPNGKAAIDWGVYGIPESYLVGPDGTILYKrvGPFDDiSLKEG--------LFPAMEKAL- 197
Cdd:cd02969    78 ENMKAKAKEHGYPF-PYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYR--GRIDD-SRPGNdppvtgrdLRAALDALLa 153


                  ....*
gi 1817133494 198 GKPVS 202
Cdd:cd02969   154 GKPVP 158
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 79-145 2.29e-03

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 36.93  E-value: 2.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817133494  79 DVAI-KGKLTLVNVFASWCLPCRDEHPILKELAKD--GRLNIVAINYkdqsDNAlRFLGELGNpFRAIGI 145
Cdd:cd02950    14 EVALsNGKPTLVEFYADWCTVCQEMAPDVAKLKQKygDQVNFVMLNV----DNP-KWLPEIDR-YRVDGI 77
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 83-133 7.15e-03

TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity.


Pssm-ID: 239246 [Multi-domain]  Cd Length: 102  Bit Score: 34.62  E-value: 7.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1817133494  83 KGKLTLVNVFASWCLPCRDEHPILKELakdgrlnivainYKDQSDNALRFL 133
Cdd:cd02948    16 NKGLTVVDVYQEWCGPCKAVVSLFKKI------------KNELGDDLLHFA 54
 
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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