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Conserved domains on  [gi|889054078|emb|CMI37781|]
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thioredoxin protein [Mycobacterium tuberculosis]

Protein Classification

TlpA disulfide reductase family protein( domain architecture ID 10121831)

TlpA disulfide reductase family protein such as Bradyrhizobium japonicum thiol:disulfide interchange protein TlpA, an unusual thioredoxin which has been implicated in the biogenesis of cytochrome aa3 and also characterized as a reductant for the copper metallochaperone ScoI

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  9099998|10049365|15558583
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 54-174 7.65e-35

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: 119.26  E-value: 7.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  54 PLSGPELADpaRSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRGAGVSFLGIDVRDNNRQAPQDFINDRHVT 133
Cdd:cd02966    1 DFSLPDLDG--KPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGIT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 889054078 134 YPSIYDPAMRTLIAFGGkyptSVIPSTLVLDRQHRVAAVFL 174
Cdd:cd02966   79 FPVLLDPDGELAKAYGV----RGLPTTFLIDRDGRIRARHV 115
 
Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 54-174 7.65e-35

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: 119.26  E-value: 7.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  54 PLSGPELADpaRSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRGAGVSFLGIDVRDNNRQAPQDFINDRHVT 133
Cdd:cd02966    1 DFSLPDLDG--KPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGIT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 889054078 134 YPSIYDPAMRTLIAFGGkyptSVIPSTLVLDRQHRVAAVFL 174
Cdd:cd02966   79 FPVLLDPDGELAKAYGV----RGLPTTFLIDRDGRIRARHV 115
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 49-192 2.76e-33

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 115.94  E-value: 2.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  49 RGRPGPLSGPELADPA-RSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRgaGVSFLGIDVrDNNRQAPQDFI 127
Cdd:COG0526    2 KAVGKPAPDFTLTDLDgKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDV-DENPEAVKAFL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889054078 128 NDRHVTYPSIYDPAMRTLIAFGgkypTSVIPSTLVLDRQHRVAAVFLRELLAADLQPVVERVAEE 192
Cdd:COG0526   79 KELGLPYPVLLDPDGELAKAYG----VRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 55-174 1.49e-16

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 73.17  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078   55 LSGPELADPARSVSLDDFPGQVVVVNVW-GQWCGPCRAEVSQLQRVYDATRGAGVSFLGIdVRDNNRQAPQDFINDRHVT 133
Cdd:pfam08534   9 FTLPDAATDGNTVSLSDFKGKKVVLNFWpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAV-NSDNDAFFVKRFWGKEGLP 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 889054078  134 YPSIYDPAMRTLIAFGGKYPTSV-----IPSTLVLDRQHRVAAVFL 174
Cdd:pfam08534  88 FPFLSDGNAAFTKALGLPIEEDAsaglrSPRYAVIDEDGKVVYLFV 133
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
65-155 3.70e-11

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 59.25  E-value: 3.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  65 RSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRGAGVSFLGIDVrDNNRQAPQDFINDRHVTYPSIYDPAMRT 144
Cdd:PRK03147  52 KKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNV-DETELAVKNFVNRYGLTFPVAIDKGRQV 130

                         90
                 ....*....|..
gi 889054078 145 LIAFG-GKYPTS 155
Cdd:PRK03147 131 IDAYGvGPLPTT 142
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 45-188 1.80e-09

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: 54.78  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078   45 PPASRGRPGPLSG-PELADPARSVSLDDFP-GQVVVVNVWGQWCGPCRAEVSQLQRVydATRgaGVSFLGIDVRDnNRQA 122
Cdd:TIGR00385  32 PSALIGKPVPAFRlASLDEPGQFYTADVLTqGKPVLLNVWASWCPPCRAEHPYLNEL--AKQ--GLPIVGVDYKD-DRQN 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 889054078  123 PQDFINDRHVTYP-SIYDPAMRTLIAFGgkypTSVIPSTLVLDRQ----HRVAAVFLRELLAADLQPVVER 188
Cdd:TIGR00385 107 AIKFLKELGNPYQlSLFDPDGMLGLDLG----VYGAPETFLVDGNgvirYRHAGPLNPEVWTEEFLPLWEK 173
 
Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 54-174 7.65e-35

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: 119.26  E-value: 7.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  54 PLSGPELADpaRSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRGAGVSFLGIDVRDNNRQAPQDFINDRHVT 133
Cdd:cd02966    1 DFSLPDLDG--KPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGIT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 889054078 134 YPSIYDPAMRTLIAFGGkyptSVIPSTLVLDRQHRVAAVFL 174
Cdd:cd02966   79 FPVLLDPDGELAKAYGV----RGLPTTFLIDRDGRIRARHV 115
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 49-192 2.76e-33

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 115.94  E-value: 2.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  49 RGRPGPLSGPELADPA-RSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRgaGVSFLGIDVrDNNRQAPQDFI 127
Cdd:COG0526    2 KAVGKPAPDFTLTDLDgKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDV-DENPEAVKAFL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889054078 128 NDRHVTYPSIYDPAMRTLIAFGgkypTSVIPSTLVLDRQHRVAAVFLRELLAADLQPVVERVAEE 192
Cdd:COG0526   79 KELGLPYPVLLDPDGELAKAYG----VRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
65-194 5.55e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 94.55  E-value: 5.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  65 RSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRGAGVSFLGIDVRDNNRQapQDFINDRHVTYPSIYDPAMRT 144
Cdd:COG1225   12 KTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAH--KKFAEKYGLPFPLLSDPDGEV 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 889054078 145 LIAFGgkypTSVIPSTLVLDRQHRVAAVFLREL-LAADLQPVVERVAEEEP 194
Cdd:COG1225   90 AKAYG----VRGTPTTFLIDPDGKIRYVWVGPVdPRPHLEEVLEALLAELK 136
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 55-174 1.49e-16

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 73.17  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078   55 LSGPELADPARSVSLDDFPGQVVVVNVW-GQWCGPCRAEVSQLQRVYDATRGAGVSFLGIdVRDNNRQAPQDFINDRHVT 133
Cdd:pfam08534   9 FTLPDAATDGNTVSLSDFKGKKVVLNFWpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAV-NSDNDAFFVKRFWGKEGLP 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 889054078  134 YPSIYDPAMRTLIAFGGKYPTSV-----IPSTLVLDRQHRVAAVFL 174
Cdd:pfam08534  88 FPFLSDGNAAFTKALGLPIEEDAsaglrSPRYAVIDEDGKVVYLFV 133
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 51-169 1.90e-16

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: 72.23  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  51 RPGP-LSGPELADPARSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVydATRGaGVSFLGIDVRDnNRQAPQDFIND 129
Cdd:cd03010    1 KPAPaFSLPALPGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMAL--ARQG-RVPIYGINYKD-NPENALAWLAR 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 889054078 130 RHVTY-PSIYDPAMRTLIAFGgkyptsVI--PSTLVLDRQHRV 169
Cdd:cd03010   77 HGNPYaAVGFDPDGRVGIDLG------VYgvPETFLIDGDGII 113
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 65-172 1.09e-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: 67.25  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078   65 RSVSLDDFPGQVVVVNVW-GQWCGPCRAEVSQLQRVYDATRGAGVSFLGIDVrdNNRQAPQDFINDRHVTYPSIYDPAMR 143
Cdd:pfam00578  16 GTVSLSDYRGKWVVLFFYpADWTPVCTTELPALADLYEEFKKLGVEVLGVSV--DSPESHKAFAEKYGLPFPLLSDPDGE 93

                          90       100       110
                  ....*....|....*....|....*....|.
gi 889054078  144 TLIAFGGKYP--TSVIPSTLVLDRQHRVAAV 172
Cdd:pfam00578  94 VARAYGVLNEeeGGALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
65-155 3.70e-11

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 59.25  E-value: 3.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  65 RSVSLDDFPGQVVVVNVWGQWCGPCRAEVSQLQRVYDATRGAGVSFLGIDVrDNNRQAPQDFINDRHVTYPSIYDPAMRT 144
Cdd:PRK03147  52 KKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNV-DETELAVKNFVNRYGLTFPVAIDKGRQV 130

                         90
                 ....*....|..
gi 889054078 145 LIAFG-GKYPTS 155
Cdd:PRK03147 131 IDAYGvGPLPTT 142
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 45-188 1.80e-09

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: 54.78  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078   45 PPASRGRPGPLSG-PELADPARSVSLDDFP-GQVVVVNVWGQWCGPCRAEVSQLQRVydATRgaGVSFLGIDVRDnNRQA 122
Cdd:TIGR00385  32 PSALIGKPVPAFRlASLDEPGQFYTADVLTqGKPVLLNVWASWCPPCRAEHPYLNEL--AKQ--GLPIVGVDYKD-DRQN 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 889054078  123 PQDFINDRHVTYP-SIYDPAMRTLIAFGgkypTSVIPSTLVLDRQ----HRVAAVFLRELLAADLQPVVER 188
Cdd:TIGR00385 107 AIKFLKELGNPYQlSLFDPDGMLGLDLG----VYGAPETFLVDGNgvirYRHAGPLNPEVWTEEFLPLWEK 173
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 74-169 1.43e-07

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: 47.69  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078   74 GQVVVVNVWGQWCGPCRAEVSQLQRVYDATR-GAGVSFLGIDVrDNNRQAPQDFINDRHVTYPSIY--DPAMRTLIAfgg 150
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKkKKNVEIVFVSL-DRDLEEFKDYLKKMPKDWLSVPfdDDERNELKR--- 76

                          90
                  ....*....|....*....
gi 889054078  151 KYPTSVIPSTLVLDRQHRV 169
Cdd:pfam13905  77 KYGVNAIPTLVLLDPNGEV 95
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 74-164 2.35e-06

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: 44.98  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  74 GQVVVVNVWGQWCGPCRAEVSQLQRVYDAtrgagVSFLGIDVRDNNRQAPQDFINDRHVTYPSIYDPAMrtliAFGGKYP 153
Cdd:cd03011   20 GKPVLVYFWATWCPVCRFTSPTVNQLAAD-----YPVVSVALRSGDDGAVARFMQKKGYGFPVINDPDG----VISARWG 90

                         90
                 ....*....|.
gi 889054078 154 TSVIPSTLVLD 164
Cdd:cd03011   91 VSVTPAIVIVD 101
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 74-126 3.68e-05

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: 41.00  E-value: 3.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 889054078  74 GQVVVVNVWGQWCGPCRAevsqLQRVYD--ATRGAGVSFLGIDVrDNNRQAPQDF 126
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKA----IAPVLEelAEEYPKVKFVKVDV-DENPELAEEY 59
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 50-122 6.00e-05

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 41.90  E-value: 6.00e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889054078  50 GRPGPLSGPE-LADPARSVSLDDFP-GQVVVVNVWGQWCGPCRAEVSQLQRVydatRGAGVSFLGIDVRDNNRQA 122
Cdd:PRK15412  42 GKPVPKFRLEsLENPGQFYQADVLTqGKPVLLNVWATWCPTCRAEHQYLNQL----SAQGIRVVGMNYKDDRQKA 112
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 74-126 1.41e-04

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: 39.80  E-value: 1.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 889054078  74 GQVVVVNVWGQWCGPCRAEVSQLQRVYDATRGAgVSFLGIDVrDNNRQAPQDF 126
Cdd:COG3118   18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDV-DENPELAAQF 68
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 78-100 2.91e-04

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: 38.86  E-value: 2.91e-04
                         10        20
                 ....*....|....*....|...
gi 889054078  78 VVNVWGQWCGPCRAEVSQLQRVY 100
Cdd:cd02948   21 VVDVYQEWCGPCKAVVSLFKKIK 43
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 76-124 4.60e-03

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: 35.34  E-value: 4.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 889054078   76 VVVVNVWGQWCGPCRAEVSQLQRVyDATRGAGVSFLGIDVRDNNRQAPQ 124
Cdd:TIGR01068  16 PVLVDFWAPWCGPCKMIAPILEEL-AKEYEGKVKFVKLNVDENPDIAAK 63
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 65-149 6.82e-03

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: 35.80  E-value: 6.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889054078  65 RSVSLDDFPGQ--VVVVNVWGQWCGPCRAEVSQLQRVYDATRGAGVSFLGI--DVRDNNRQAPQDFindrHVTYPSIYDP 140
Cdd:cd02970   13 ETVTLSALLGEgpVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVgpESPEKLEAFDKGK----FLPFPVYADP 88


                 ....*....
gi 889054078 141 AMRTLIAFG 149
Cdd:cd02970   89 DRKLYRALG 97
 
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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