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Conserved domains on  [gi|2224847472|ref|WP_245261597|]
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TlpA disulfide reductase family protein [Ancylobacter sp. FA202]

Protein Classification

TlpA family protein disulfide reductase( domain architecture ID 10001660)

TlpA family protein disulfide reductase 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, and similar to ResA and DsbE, which are essential proteins in cytochrome c maturation

CATH:  3.40.30.10
Gene Ontology:  GO:0016491
PubMed:  11531338|15667290

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 107-248 3.83e-33

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 117.87  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 107 TEKPTRIPDLAFLAPDGQPTRLSQVGGDGLkLVNIWATWCVPCRKEMPALDELQATLGskggdgapGFEVITVNIDtRDP 186
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPV-LVNFWATWCPPCRAEMPVLKELAEEYG--------GVVFVGVDVD-ENP 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2224847472 187 AKPKTFFTETGLTHlALYTDPKAQAFQDLRVvgrgFGLPTTMLIDAQGCELGHIAGPAEWAS 248
Cdd:COG0526    72 EAVKAFLKELGLPY-PVLLDPDGELAKAYGV----RGIPTTVLIDKDGKIVARHVGPLSPEE 128
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 107-248 3.83e-33

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 117.87  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 107 TEKPTRIPDLAFLAPDGQPTRLSQVGGDGLkLVNIWATWCVPCRKEMPALDELQATLGskggdgapGFEVITVNIDtRDP 186
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPV-LVNFWATWCPPCRAEMPVLKELAEEYG--------GVVFVGVDVD-ENP 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2224847472 187 AKPKTFFTETGLTHlALYTDPKAQAFQDLRVvgrgFGLPTTMLIDAQGCELGHIAGPAEWAS 248
Cdd:COG0526    72 EAVKAFLKELGLPY-PVLLDPDGELAKAYGV----RGIPTTVLIDKDGKIVARHVGPLSPEE 128
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 115-242 9.41e-32

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: 113.49  E-value: 9.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 115 DLAFLAPDGQPTRLSQVGGDGLkLVNIWATWCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDTRDPAKPKTFFT 194
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVV-LVNFWASWCPPCRAEMPELEALAKEYKDD------GVEVVGVNVDDDDPAAVKAFLK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2224847472 195 ETGLTHLALYtDPKAQAFQDLRVVgrgfGLPTTMLIDAQGCELGHIAG 242
Cdd:cd02966    74 KYGITFPVLL-DPDGELAKAYGVR----GLPTTFLIDRDGRIRARHVG 116
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 112-234 2.81e-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: 64.94  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 112 RIPDLAFLAPDGQPTRLSQVGGDGLkLVNIWAT-WCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDTrdPAKPK 190
Cdd:pfam00578   4 KAPDFELPDGDGGTVSLSDYRGKWV-VLFFYPAdWTPVCTTELPALADLYEEFKKL------GVEVLGVSVDS--PESHK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2224847472 191 TFFTETGLThLALYTDPKAQAFQDLRVV--GRGFGLPTTMLIDAQG 234
Cdd:pfam00578  75 AFAEKYGLP-FPLLSDPDGEVARAYGVLneEEGGALRATFVIDPDG 119
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
114-234 1.10e-11

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 61.94  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 114 PDLAFLAPDGQPTRLSQVGGDGLKLvNIWATWCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDTRDPAKpKTFF 193
Cdd:PRK03147   42 PNFVLTDLEGKKIELKDLKGKGVFL-NFWGTWCKPCEKEMPYMNELYPKYKEK------GVEIIAVNVDETELAV-KNFV 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2224847472 194 TETGLTH-LALYTDpkaqafqdlRVVGRGFG---LPTTMLIDAQG 234
Cdd:PRK03147  114 NRYGLTFpVAIDKG---------RQVIDAYGvgpLPTTFLIDKDG 149
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 135-243 4.40e-11

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: 60.18  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 135 GLKLVNIWATWCVPCRKEMPALDELQAtlgskggDGAPgfeviTVNIDTRDPA-KPKTFFTETGLTHLALYTDPKAQAFQ 213
Cdd:TIGR00385  64 KPVLLNVWASWCPPCRAEHPYLNELAK-------QGLP-----IVGVDYKDDRqNAIKFLKELGNPYQLSLFDPDGMLGL 131

                          90       100       110
                  ....*....|....*....|....*....|
gi 2224847472 214 DLRVvgrgFGLPTTMLIDAQGCELGHIAGP 243
Cdd:TIGR00385 132 DLGV----YGAPETFLVDGNGVIRYRHAGP 157
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 107-248 3.83e-33

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 117.87  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 107 TEKPTRIPDLAFLAPDGQPTRLSQVGGDGLkLVNIWATWCVPCRKEMPALDELQATLGskggdgapGFEVITVNIDtRDP 186
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPV-LVNFWATWCPPCRAEMPVLKELAEEYG--------GVVFVGVDVD-ENP 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2224847472 187 AKPKTFFTETGLTHlALYTDPKAQAFQDLRVvgrgFGLPTTMLIDAQGCELGHIAGPAEWAS 248
Cdd:COG0526    72 EAVKAFLKELGLPY-PVLLDPDGELAKAYGV----RGIPTTVLIDKDGKIVARHVGPLSPEE 128
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 115-242 9.41e-32

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: 113.49  E-value: 9.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 115 DLAFLAPDGQPTRLSQVGGDGLkLVNIWATWCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDTRDPAKPKTFFT 194
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVV-LVNFWASWCPPCRAEMPELEALAKEYKDD------GVEVVGVNVDDDDPAAVKAFLK 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2224847472 195 ETGLTHLALYtDPKAQAFQDLRVVgrgfGLPTTMLIDAQGCELGHIAG 242
Cdd:cd02966    74 KYGITFPVLL-DPDGELAKAYGVR----GLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
113-234 3.93e-20

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 83.76  E-value: 3.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 113 IPDLAFLAPDGQPTRLSQVGGDGLkLVNIWATWCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDtrDPAKPKTF 192
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPV-VLYFYATWCPGCTAELPELRDLYEEFKDK------GVEVLGVSSD--SDEAHKKF 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2224847472 193 FTETGLThLALYTDPKAQAFQDLRVvgrgFGLPTTMLIDAQG 234
Cdd:COG1225    72 AEKYGLP-FPLLSDPDGEVAKAYGV----RGTPTTFLIDPDG 108
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 109-243 4.63e-14

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: 67.22  E-value: 4.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 109 KPtrIPDLAFLAPDGQPTRLSQVG-GDGLKLVNIWATWCVPCRKEMPALDELQAtlgskggdgAPGFEVITVNI-DTRDP 186
Cdd:cd03010     1 KP--APAFSLPALPGPDKTLTSADlKGKPYLLNVWASWCAPCREEHPVLMALAR---------QGRVPIYGINYkDNPEN 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2224847472 187 AkpKTFFTETGLTHLALYTDPKAQAFQDLRVVgrgfGLPTTMLIDAQGCELGHIAGP 243
Cdd:cd03010    70 A--LAWLARHGNPYAAVGFDPDGRVGIDLGVY----GVPETFLIDGDGIIRYKHVGP 120
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 112-234 2.81e-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: 64.94  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 112 RIPDLAFLAPDGQPTRLSQVGGDGLkLVNIWAT-WCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDTrdPAKPK 190
Cdd:pfam00578   4 KAPDFELPDGDGGTVSLSDYRGKWV-VLFFYPAdWTPVCTTELPALADLYEEFKKL------GVEVLGVSVDS--PESHK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2224847472 191 TFFTETGLThLALYTDPKAQAFQDLRVV--GRGFGLPTTMLIDAQG 234
Cdd:pfam00578  75 AFAEKYGLP-FPLLSDPDGEVARAYGVLneEEGGALRATFVIDPDG 119
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 112-235 4.27e-13

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 65.08  E-value: 4.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 112 RIPDLAF--LAPDGQPTRLSQVGGdGLKLVNIWAT-WCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDTrDPAK 188
Cdd:pfam08534   5 KAPDFTLpdAATDGNTVSLSDFKG-KKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEK------GVDVVAVNSDN-DAFF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2224847472 189 PKTFFTETGLTHLALYtDPKAQAFQDL-----RVVGRGFGLPTTMLIDAQGC 235
Cdd:pfam08534  77 VKRFWGKEGLPFPFLS-DGNAAFTKALglpieEDASAGLRSPRYAVIDEDGK 127
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
114-234 1.10e-11

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 61.94  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 114 PDLAFLAPDGQPTRLSQVGGDGLKLvNIWATWCVPCRKEMPALDELQATLGSKggdgapGFEVITVNIDTRDPAKpKTFF 193
Cdd:PRK03147   42 PNFVLTDLEGKKIELKDLKGKGVFL-NFWGTWCKPCEKEMPYMNELYPKYKEK------GVEIIAVNVDETELAV-KNFV 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2224847472 194 TETGLTH-LALYTDpkaqafqdlRVVGRGFG---LPTTMLIDAQG 234
Cdd:PRK03147  114 NRYGLTFpVAIDKG---------RQVIDAYGvgpLPTTFLIDKDG 149
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 135-243 4.40e-11

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: 60.18  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 135 GLKLVNIWATWCVPCRKEMPALDELQAtlgskggDGAPgfeviTVNIDTRDPA-KPKTFFTETGLTHLALYTDPKAQAFQ 213
Cdd:TIGR00385  64 KPVLLNVWASWCPPCRAEHPYLNELAK-------QGLP-----IVGVDYKDDRqNAIKFLKELGNPYQLSLFDPDGMLGL 131

                          90       100       110
                  ....*....|....*....|....*....|
gi 2224847472 214 DLRVvgrgFGLPTTMLIDAQGCELGHIAGP 243
Cdd:TIGR00385 132 DLGV----YGAPETFLVDGNGVIRYRHAGP 157
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 138-234 2.89e-08

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: 50.38  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 138 LVNIWATWCVPCRKEMPALDELQATLGSKggdgaPGFEVITVNIDtRDPAKPKTFFTETGLTHLALYT-DPKAQAFQD-L 215
Cdd:pfam13905   5 LLYFGASWCKPCRRFTPLLKELYEKLKKK-----KNVEIVFVSLD-RDLEEFKDYLKKMPKDWLSVPFdDDERNELKRkY 78

                          90
                  ....*....|....*....
gi 2224847472 216 RVVgrgfGLPTTMLIDAQG 234
Cdd:pfam13905  79 GVN----AIPTLVLLDPNG 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 131-182 3.99e-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: 47.51  E-value: 3.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2224847472 131 VGGDGLKLVNIWATWCVPCRKEMPALDELQATLGSKggdgapgFEVITVNID 182
Cdd:COG3118    15 LESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-------VKFVKVDVD 59
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 129-182 4.63e-07

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: 46.78  E-value: 4.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2224847472 129 SQVGGDGLKLVNIWATWCVPCRKEMPALDELQATlgskggdgAPGFEVITVNID 182
Cdd:cd02947     5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE--------YPKVKFVKVDVD 50
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 138-234 1.24e-06

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 47.68  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 138 LVNIWATWCVPCRKEMPALDELQATlgskggdgapGFEVITVNIDTrDPAKPKTFFTETGLTHLALYTDPKAQAFQDLRV 217
Cdd:PRK15412   72 LLNVWATWCPTCRAEHQYLNQLSAQ----------GIRVVGMNYKD-DRQKAISWLKELGNPYALSLFDGDGMLGLDLGV 140

                          90
                  ....*....|....*..
gi 2224847472 218 vgrgFGLPTTMLIDAQG 234
Cdd:PRK15412  141 ----YGAPETFLIDGNG 153
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 133-187 2.78e-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: 2.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2224847472 133 GDGLKLVNIWATWCVPCRKEMPALDELQATLGSKggdgapgFEVITVNIDT-RDPA 187
Cdd:TIGR01068  13 SDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGK-------VKFVKLNVDEnPDIA 61
trxA PRK09381
thioredoxin TrxA;
133-211 9.79e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 40.82  E-value: 9.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2224847472 133 GDGLKLVNIWATWCVPCRKEMPALDELQATLGSKggdgapgFEVITVNIDTRDPAKPKtfFTETGLTHLALYTDPKAQA 211
Cdd:PRK09381   20 ADGAILVDFWAEWCGPCKMIAPILDEIADEYQGK-------LTVAKLNIDQNPGTAPK--YGIRGIPTLLLFKNGEVAA 89
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 119-234 1.82e-03

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 37.65  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 119 LAPDGQPTRLSQVGGdglKLVNIW--ATWCVPCRKEMPALDELQATLGSKGGDgapgFEVITVNIDtRDPAKPKTFFTEt 196
Cdd:cd03009     4 LRNDGGKVPVSSLEG---KTVGLYfsASWCPPCRAFTPKLVEFYEKLKESGKN----FEIVFISWD-RDEESFNDYFSK- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2224847472 197 gLTHLAL-YTDPKAQafQDLRvvgRGF---GLPTTMLIDAQG 234
Cdd:cd03009    75 -MPWLAVpFSDRERR--SRLN---RTFkieGIPTLIILDADG 110
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 138-234 7.77e-03

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: 35.74  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2224847472 138 LVNIWATWCVPCRKEMPALDELQATlgskggdgapgFEVITVNIDTRDPAKPKTFFTETGL--THLAlytDPKAqafqdl 215
Cdd:cd03011    24 LVYFWATWCPVCRFTSPTVNQLAAD-----------YPVVSVALRSGDDGAVARFMQKKGYgfPVIN---DPDG------ 83

                          90       100
                  ....*....|....*....|..
gi 2224847472 216 rVVGRGFG---LPTTMLIDAQG 234
Cdd:cd03011    84 -VISARWGvsvTPAIVIVDPGG 104
 
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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