NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|505246868|ref|WP_015433970|]
View 

DsbE family thiol:disulfide interchange protein [Azoarcus sp. KH32C]

Protein Classification

DsbE family thiol:disulfide interchange protein( domain architecture ID 10122405)

DsbE family thiol:disulfide interchange protein such as DsbE, which catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 37-184 2.14e-66

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: 199.73  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  37 KPAPAFRVPQLQSPDKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELSRNSPVPIIGLNYKEVRgdselegksmdap 116
Cdd:cd03010    1 KPAPAFSLPALPGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQGRVPIYGINYKDNP------------- 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505246868 117 telrlatDRARQWLVQHgGDPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALR 184
Cdd:cd03010   68 -------ENALAWLARH-GNPYAAVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPLTPEVWE 127
 
Name Accession Description Interval E-value
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 37-184 2.14e-66

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: 199.73  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  37 KPAPAFRVPQLQSPDKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELSRNSPVPIIGLNYKEVRgdselegksmdap 116
Cdd:cd03010    1 KPAPAFSLPALPGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQGRVPIYGINYKDNP------------- 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505246868 117 telrlatDRARQWLVQHgGDPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALR 184
Cdd:cd03010   68 -------ENALAWLARH-GNPYAAVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPLTPEVWE 127
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 26-191 2.68e-50

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: 160.33  E-value: 2.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868   26 NPREVPSPLIDKPAPAFRVPQLQSPDKTISPDDL-KGRVWLLNVWASWCVSCRQEHPLLVELSRNSpVPIIGLNYKEVRg 104
Cdd:TIGR00385  27 DPKALPSALIGKPVPAFRLASLDEPGQFYTADVLtQGKPVLLNVWASWCPPCRAEHPYLNELAKQG-LPIVGVDYKDDR- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  105 dselegksmdaptelrlatDRARQWLVQHGgDPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALR 184
Cdd:TIGR00385 105 -------------------QNAIKFLKELG-NPYQLSLFDPDGMLGLDLGVYGAPETFLVDGNGVIRYRHAGPLNPEVWT 164


                  ....*..
gi 505246868  185 DVLLPKI 191
Cdd:TIGR00385 165 EEFLPLW 171
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 35-193 1.20e-40

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 134.82  E-value: 1.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  35 IDKPAPAFRVPQLQspDKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELS-RNSPVPIIGLNYKEvrgdselegksm 113
Cdd:COG0526    4 VGKPAPDFTLTDLD--GKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAeEYGGVVFVGVDVDE------------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868 114 daptelrlATDRARQWLVQHGgDPYTVtAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALRDVLLPKIAE 193
Cdd:COG0526   70 --------NPEAVKAFLKELG-LPYPV-LLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 26-189 7.86e-37

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 126.65  E-value: 7.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  26 NPREVPSPLIDKPAPAFRVPQLQSPDKTISPDDL-KGRVWLLNVWASWCVSCRQEHPLLVELSRNSpVPIIGLNYKEVRg 104
Cdd:PRK15412  32 DPTNLESALIGKPVPKFRLESLENPGQFYQADVLtQGKPVLLNVWATWCPTCRAEHQYLNQLSAQG-IRVVGMNYKDDR- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868 105 dselegksmdaptelrlatDRARQWLvQHGGDPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALR 184
Cdd:PRK15412 110 -------------------QKAISWL-KELGNPYALSLFDGDGMLGLDLGVYGAPETFLIDGNGIIRYRHAGDLNPRVWE 169


                 ....*
gi 505246868 185 DVLLP 189
Cdd:PRK15412 170 SEIKP 174
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 37-186 2.18e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 67.01  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868   37 KPAPAFRVPQLQSPDKTISPDDLKGRVWLLNVWAS-WCVSCRQEHPLLVELSR---NSPVPIIGLNYKEvrgdselegks 112
Cdd:pfam08534   4 DKAPDFTLPDAATDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNElykEKGVDVVAVNSDN----------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  113 mDAPTelrlatdrARQWLVQHgGDPYTVTAmDLDGRIGIDYGV---------YGVPETFVVDKAGVIRYKHIGPLTVEAL 183
Cdd:pfam08534  73 -DAFF--------VKRFWGKE-GLPFPFLS-DGNAAFTKALGLpieedasagLRSPRYAVIDEDGKVVYLFVGPEPGVDV 141


                  ...
gi 505246868  184 RDV 186
Cdd:pfam08534 142 SDA 144
 
Name Accession Description Interval E-value
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 37-184 2.14e-66

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: 199.73  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  37 KPAPAFRVPQLQSPDKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELSRNSPVPIIGLNYKEVRgdselegksmdap 116
Cdd:cd03010    1 KPAPAFSLPALPGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQGRVPIYGINYKDNP------------- 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505246868 117 telrlatDRARQWLVQHgGDPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALR 184
Cdd:cd03010   68 -------ENALAWLARH-GNPYAAVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPLTPEVWE 127
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 26-191 2.68e-50

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: 160.33  E-value: 2.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868   26 NPREVPSPLIDKPAPAFRVPQLQSPDKTISPDDL-KGRVWLLNVWASWCVSCRQEHPLLVELSRNSpVPIIGLNYKEVRg 104
Cdd:TIGR00385  27 DPKALPSALIGKPVPAFRLASLDEPGQFYTADVLtQGKPVLLNVWASWCPPCRAEHPYLNELAKQG-LPIVGVDYKDDR- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  105 dselegksmdaptelrlatDRARQWLVQHGgDPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALR 184
Cdd:TIGR00385 105 -------------------QNAIKFLKELG-NPYQLSLFDPDGMLGLDLGVYGAPETFLVDGNGVIRYRHAGPLNPEVWT 164


                  ....*..
gi 505246868  185 DVLLPKI 191
Cdd:TIGR00385 165 EEFLPLW 171
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 35-193 1.20e-40

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 134.82  E-value: 1.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  35 IDKPAPAFRVPQLQspDKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELS-RNSPVPIIGLNYKEvrgdselegksm 113
Cdd:COG0526    4 VGKPAPDFTLTDLD--GKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAeEYGGVVFVGVDVDE------------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868 114 daptelrlATDRARQWLVQHGgDPYTVtAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALRDVLLPKIAE 193
Cdd:COG0526   70 --------NPEAVKAFLKELG-LPYPV-LLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 26-189 7.86e-37

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 126.65  E-value: 7.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  26 NPREVPSPLIDKPAPAFRVPQLQSPDKTISPDDL-KGRVWLLNVWASWCVSCRQEHPLLVELSRNSpVPIIGLNYKEVRg 104
Cdd:PRK15412  32 DPTNLESALIGKPVPKFRLESLENPGQFYQADVLtQGKPVLLNVWATWCPTCRAEHQYLNQLSAQG-IRVVGMNYKDDR- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868 105 dselegksmdaptelrlatDRARQWLvQHGGDPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALR 184
Cdd:PRK15412 110 -------------------QKAISWL-KELGNPYALSLFDGDGMLGLDLGVYGAPETFLIDGNGIIRYRHAGDLNPRVWE 169


                 ....*
gi 505246868 185 DVLLP 189
Cdd:PRK15412 170 SEIKP 174
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 41-176 1.58e-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: 113.10  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  41 AFRVPQLQspDKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELSR---NSPVPIIGLNYKEVRgdselegksmdapt 117
Cdd:cd02966    1 DFSLPDLD--GKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKeykDDGVEVVGVNVDDDD-------------- 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505246868 118 elrlaTDRARQWLVQHGgdPYTVTAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIG 176
Cdd:cd02966   65 -----PAAVKAFLKKYG--ITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
39-195 1.80e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 95.70  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  39 APAFRVPQLQspDKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELS---RNSPVPIIGLnykevrgdselegkSMDA 115
Cdd:COG1225    1 APDFTLPDLD--GKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYeefKDKGVEVLGV--------------SSDS 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868 116 PtelrlatDRARQWLVQHGgDPYTVtAMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTV-EALRDVLLPKIAEL 194
Cdd:COG1225   65 D-------EAHKKFAEKYG-LPFPL-LSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPrPHLEEVLEALLAEL 135


                 .
gi 505246868 195 Q 195
Cdd:COG1225  136 K 136
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 37-186 2.18e-14

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 67.01  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868   37 KPAPAFRVPQLQSPDKTISPDDLKGRVWLLNVWAS-WCVSCRQEHPLLVELSR---NSPVPIIGLNYKEvrgdselegks 112
Cdd:pfam08534   4 DKAPDFTLPDAATDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNElykEKGVDVVAVNSDN----------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  113 mDAPTelrlatdrARQWLVQHgGDPYTVTAmDLDGRIGIDYGV---------YGVPETFVVDKAGVIRYKHIGPLTVEAL 183
Cdd:pfam08534  73 -DAFF--------VKRFWGKE-GLPFPFLS-DGNAAFTKALGLpieedasagLRSPRYAVIDEDGKVVYLFVGPEPGVDV 141


                  ...
gi 505246868  184 RDV 186
Cdd:pfam08534 142 SDA 144
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
37-187 1.29e-11

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 60.40  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  37 KPAPAFRVPQLQSpdKTISPDDLKGRVWLLNVWASWCVSCRQEHPLLVELS---RNSPVPIIGLNYKEvrgdselegksm 113
Cdd:PRK03147  39 KEAPNFVLTDLEG--KKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYpkyKEKGVEIIAVNVDE------------ 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505246868 114 dapTELrlatdrarqwLVQHGGDPYTVT---AMDLDGRIGIDYGVYGVPETFVVDKAGVIRYKHIGPLTVEALRDVL 187
Cdd:PRK03147 105 ---TEL----------AVKNFVNRYGLTfpvAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLEEYL 168
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 35-173 8.85e-11

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: 56.85  E-value: 8.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868   35 IDKPAPAFRVPQLQspDKTISPDDLKGRVWLLNVWAS-WCVSCRQEHPLLVEL-----SRNspVPIIGLnykevrgdsel 108
Cdd:pfam00578   1 VGDKAPDFELPDGD--GGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLyeefkKLG--VEVLGV----------- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505246868  109 egkSMDAPTELRlatdrarQWLVQHGgDPYTVTAmDLDGRIGIDYGVY------GVPETFVVDKAGVIRYK 173
Cdd:pfam00578  66 ---SVDSPESHK-------AFAEKYG-LPFPLLS-DPDGEVARAYGVLneeeggALRATFVIDPDGKVRYI 124
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 38-188 3.57e-06

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They 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 TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 44.85  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  38 PAPAFRVPQlqSPDKTISPDDLKGRVWLLNVwaswcvscrqeHPLLvelsrNSPV-P--IIGLN--YKE-VRGDSELEGK 111
Cdd:cd02971    1 KAPDFTLPA--TDGGEVSLSDFKGKWVVLFF-----------YPKD-----FTPVcTteLCAFRdlAEEfAKGGAEVLGV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868 112 SMDAPTELRlatdrarQWLVQHGGDPYTVTAmDLDGRIGIDYGVYGVPE---------TFVVDKAGVIRYKHIGPLTVEA 182
Cdd:cd02971   63 SVDSPFSHK-------AWAEKEGGLNFPLLS-DPDGEFAKAYGVLIEKSaggglaaraTFIIDPDGKIRYVEVEPLPTGR 134


                 ....*.
gi 505246868 183 LRDVLL 188
Cdd:cd02971  135 NAEELL 140
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 47-169 2.00e-05

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: 42.29  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  47 LQSPDKTISPDDLKGRVW-----LLNVWASWCVSCRQEHPLLVELSRNspVPIIGLnykevrgdselegkSMDAPTELRL 121
Cdd:cd03011    1 PLFTATTLDGEQFDLESLsgkpvLVYFWATWCPVCRFTSPTVNQLAAD--YPVVSV--------------ALRSGDDGAV 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 505246868 122 AtdrarQWLVQHGgdpYTVTAM-DLDGRIGIDYGVYGVPETFVVDKAGV 169
Cdd:cd03011   65 A-----RFMQKKG---YGFPVInDPDGVISARWGVSVTPAIVIVDPGGI 105
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 61-170 9.15e-05

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: 39.98  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868   61 GRVWLLNVWASWCVSCRQEHPLLVELSR----NSPVPIIGLNYkevrgDSELEgksmdaptelrlatdrarQW---LVQH 133
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEklkkKKNVEIVFVSL-----DRDLE------------------EFkdyLKKM 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 505246868  134 GGDPYTVTAMD-LDGRIGIDYGVYGVPETFVVDKAGVI 170
Cdd:pfam13905  58 PKDWLSVPFDDdERNELKRKYGVNAIPTLVLLDPNGEV 95
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 65-187 2.93e-04

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: 38.31  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  65 LLNVWASWCVSCRQEHPLLVELSRNSP-VPIIGLNYKEVRgdselegksmdaptelrlatdrarqwlvqhggdpytvtam 143
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEEYPkVKFVKVDVDENP---------------------------------------- 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505246868 144 dldgRIGIDYGVYGVPeTFVVDKAGVIRYKHIGPLTVEALRDVL 187
Cdd:cd02947   54 ----ELAEEYGVRSIP-TFLFFKNGKEVDRVVGADPKEELEEFL 92
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 144-184 2.97e-03

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 36.71  E-value: 2.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505246868 144 DLDGRIGIDYGVY----GVPE--TFVVDKAGVIRYKHIGPLTV-----EALR 184
Cdd:cd03015  100 DPKKKISRDYGVLdeeeGVALrgTFIIDPEGIIRHITVNDLPVgrsvdETLR 151
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 147-185 3.64e-03

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective 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. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 36.48  E-value: 3.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505246868 147 GRIGIDYGVY----GVPE--TFVVDKAGVIRYKHIG--------PLTVEALRD 185
Cdd:cd03018   97 GEVAKAYGVFdedlGVAEraVFVIDRDGIIRYAWVSddgeprdlPDYDEALDA 149
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
32-184 3.73e-03

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 36.59  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  32 SPLIDKPAPAFRVPQLQSPD-KTISPDDLKGrvwllnvwaSWCV--ScrqeHPL---------LVELSRNSP------VP 93
Cdd:COG0450    2 MPLIGDKAPDFTAEATHGGEfKKISLSDYKG---------KWVVlfF----HPAdftfvcpteLGAFAKRYEefkklgVE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505246868  94 IIGLnykevrgdselegkSMDaptelRLATDRA-RQWLVQHGGD---PYTVTAmDLDGRIGIDYGVY----GVPE--TFV 163
Cdd:COG0450   69 VIGL--------------SVD-----SVFSHKAwHETIKEKGGIvkiKFPIIA-DPTGKIARAYGMLhpedGVAVrgVFI 128

                        170       180
                 ....*....|....*....|....*.
gi 505246868 164 VDKAGVIRYKHIGPLTV-----EALR 184
Cdd:COG0450  129 IDPDGKIRAIEVYPLSVgrnvdEILR 154
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH