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Conserved domains on  [gi|2469828359|ref|WP_277135658|]
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TlpA disulfide reductase family protein [Bacteroides congonensis]

Protein Classification

TlpA disulfide reductase family protein( domain architecture ID 10626239)

TlpA disulfide reductase family protein belonging to the thioredoxin superfamily, similar to 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; contains a DUF4369 domain

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

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, ...
 238-381 4.92e-43

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 146.76  E-value: 4.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 238 MKAlaPGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYkdKGLKVVGISMDNSKAAWMK 317
Cdd:COG0526     1 MKA--VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDENPEAVKA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2469828359 318 SIDKIQIPWLHVSSLKGmkrcPVAELYQVYAIPKLYIIDKEGKIVDK---DLRGEDLKKKVDGLFAR 381
Cdd:COG0526    77 FLKELGLPYPVLLDPDG----ELAKAYGVRGIPTTVLIDKDGKIVARhvgPLSPEELEEALEKLLAK 139
DUF4369 pfam14289
Domain of unknown function (DUF4369); This domain family is found in bacteria, and is ...
 25-109 1.22e-04

Domain of unknown function (DUF4369); This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00578. LPAM signal peptide sequence is found in some family members.


:

Pssm-ID: 433842  Cd Length: 92  Bit Score: 40.41  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359  25 YQIEGKWaTGI--GKKVYLSNfpaDTPEAVTIDSTIVApDGSYKLSGKLDKMQLLSLTHEGSKGFRPLMGDGKPANILIR 102
Cdd:pfam14289   1 YTIEGTI-KGLkdGTKVYLSY---DGGGLVKLDSAVVK-NGKFTFKGKVDEPPMAYLLIDDKSGALPFFLENGTITIKLD 75


                  ....*..
gi 2469828359 103 DMEYSYK 109
Cdd:pfam14289  76 PGDFIAK 82
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 238-381 4.92e-43

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 146.76  E-value: 4.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 238 MKAlaPGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYkdKGLKVVGISMDNSKAAWMK 317
Cdd:COG0526     1 MKA--VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDENPEAVKA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2469828359 318 SIDKIQIPWLHVSSLKGmkrcPVAELYQVYAIPKLYIIDKEGKIVDK---DLRGEDLKKKVDGLFAR 381
Cdd:COG0526    77 FLKELGLPYPVLLDPDG----ELAKAYGVRGIPTTVLIDKDGKIVARhvgPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 249-364 2.32e-36

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: 128.12  E-value: 2.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 249 DFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMD-NSKAAWMKSIDKIQIPWL 327
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDdDDPAAVKAFLKKYGITFP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2469828359 328 HVSSLKGmkrcPVAELYQVYAIPKLYIIDKEGKIVDK 364
Cdd:cd02966    81 VLLDPDG----ELAKAYGVRGLPTTFLIDRDGRIRAR 113
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 243-364 3.99e-28

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: 106.92  E-value: 3.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 243 PGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWAS-WCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDN--SKAAWmksI 319
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSpeSHKAF---A 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2469828359 320 DKIQIPWLHVSSLKGmkrcPVAELYQVY------AIPKLYIIDKEGKIVDK 364
Cdd:pfam00578  78 EKYGLPFPLLSDPDG----EVARAYGVLneeeggALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
235-363 2.40e-24

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 98.15  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 235 IAKMKALAPGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDNSKAA 314
Cdd:PRK03147   29 FADKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELA 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2469828359 315 WMKSIDKIQIPWlHVSSLKGMKrcpVAELYQVYAIPKLYIIDKEGKIVD 363
Cdd:PRK03147  109 VKNFVNRYGLTF-PVAIDKGRQ---VIDAYGVGPLPTTFLIDKDGKVVK 153
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 216-361 3.76e-12

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: 64.03  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 216 NGMGEKAKKTPKGIELKESIAKMKALAPGakapdfTLPTVTGEEFSlaslQGHIVILDFWASWCAPCIAEMPTVKEIYAk 295
Cdd:TIGR00385  22 NAEGDDPKALPSALIGKPVPAFRLASLDE------PGQFYTADVLT----QGKPVLLNVWASWCPPCRAEHPYLNELAK- 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2469828359 296 ykdKGLKVVGISM-DNSKAAwMKSIDKIQIPW-LHVSSLKGMkrcpVAELYQVYAIPKLYIIDKEGKI 361
Cdd:TIGR00385  91 ---QGLPIVGVDYkDDRQNA-IKFLKELGNPYqLSLFDPDGM----LGLDLGVYGAPETFLVDGNGVI 150
DUF4369 pfam14289
Domain of unknown function (DUF4369); This domain family is found in bacteria, and is ...
 25-109 1.22e-04

Domain of unknown function (DUF4369); This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00578. LPAM signal peptide sequence is found in some family members.


Pssm-ID: 433842  Cd Length: 92  Bit Score: 40.41  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359  25 YQIEGKWaTGI--GKKVYLSNfpaDTPEAVTIDSTIVApDGSYKLSGKLDKMQLLSLTHEGSKGFRPLMGDGKPANILIR 102
Cdd:pfam14289   1 YTIEGTI-KGLkdGTKVYLSY---DGGGLVKLDSAVVK-NGKFTFKGKVDEPPMAYLLIDDKSGALPFFLENGTITIKLD 75


                  ....*..
gi 2469828359 103 DMEYSYK 109
Cdd:pfam14289  76 PGDFIAK 82
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 238-381 4.92e-43

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 146.76  E-value: 4.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 238 MKAlaPGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYkdKGLKVVGISMDNSKAAWMK 317
Cdd:COG0526     1 MKA--VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDENPEAVKA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2469828359 318 SIDKIQIPWLHVSSLKGmkrcPVAELYQVYAIPKLYIIDKEGKIVDK---DLRGEDLKKKVDGLFAR 381
Cdd:COG0526    77 FLKELGLPYPVLLDPDG----ELAKAYGVRGIPTTVLIDKDGKIVARhvgPLSPEELEEALEKLLAK 139
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
247-380 1.62e-42

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 145.01  E-value: 1.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 247 APDFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDnSKAAWMKSIDKIQIPW 326
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSD-SDEAHKKFAEKYGLPF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2469828359 327 LHVSSLKGmkrcPVAELYQVYAIPKLYIIDKEGKIVDKDLRGEDLKKKVDGLFA 380
Cdd:COG1225    80 PLLSDPDG----EVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 249-364 2.32e-36

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: 128.12  E-value: 2.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 249 DFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMD-NSKAAWMKSIDKIQIPWL 327
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDdDDPAAVKAFLKKYGITFP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2469828359 328 HVSSLKGmkrcPVAELYQVYAIPKLYIIDKEGKIVDK 364
Cdd:cd02966    81 VLLDPDG----ELAKAYGVRGLPTTFLIDRDGRIRAR 113
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 243-364 3.99e-28

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: 106.92  E-value: 3.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 243 PGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWAS-WCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDN--SKAAWmksI 319
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSpeSHKAF---A 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2469828359 320 DKIQIPWLHVSSLKGmkrcPVAELYQVY------AIPKLYIIDKEGKIVDK 364
Cdd:pfam00578  78 EKYGLPFPLLSDPDG----EVARAYGVLneeeggALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
235-363 2.40e-24

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 98.15  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 235 IAKMKALAPGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDNSKAA 314
Cdd:PRK03147   29 FADKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELA 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2469828359 315 WMKSIDKIQIPWlHVSSLKGMKrcpVAELYQVYAIPKLYIIDKEGKIVD 363
Cdd:PRK03147  109 VKNFVNRYGLTF-PVAIDKGRQ---VIDAYGVGPLPTTFLIDKDGKVVK 153
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 242-380 1.60e-19

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 84.34  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 242 APGAKAPDFTLPTVT--GEEFSLASLQGHIVILDFWAS-WCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDNSKAAWMKS 318
Cdd:pfam08534   1 KAGDKAPDFTLPDAAtdGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2469828359 319 IDKIQIPWLHVSS-----LKGMKRCPVAELYQVYAIPKLYIIDKEGKIVDKDLrGEDLKKKVDGLFA 380
Cdd:pfam08534  81 WGKEGLPFPFLSDgnaafTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLFV-GPEPGVDVSDAEA 146
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 267-361 5.69e-19

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: 80.81  E-value: 5.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 267 GHIVILDFWASWCAPCIAEMPTVKEIYAKYKD-KGLKVVGISMDNSKAAWMKSIDKIQIPWLHVSSLKGmKRCPVAELYQ 345
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKkKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDD-ERNELKRKYG 79

                          90
                  ....*....|....*.
gi 2469828359 346 VYAIPKLYIIDKEGKI 361
Cdd:pfam13905  80 VNAIPTLVLLDPNGEV 95
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 247-364 1.55e-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: 75.31  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 247 APDFTLPTVTGEE--FSLASLQGHIVILDFWASWCAPCIAEMPTVKEIyakYKDKGLKVVGISM-DNSKAA--WMKS--- 318
Cdd:cd03010     3 APAFSLPALPGPDktLTSADLKGKPYLLNVWASWCAPCREEHPVLMAL---ARQGRVPIYGINYkDNPENAlaWLARhgn 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2469828359 319 ------ID---KIQIPWlhvsslkgmkrcpvaelyQVYAIPKLYIIDKEGKIVDK 364
Cdd:cd03010    80 pyaavgFDpdgRVGIDL------------------GVYGVPETFLIDGDGIIRYK 116
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 246-362 3.80e-15

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: 71.81  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 246 KAPDFTLPTVTGEEFSLASLQGHIVILDFWaswcaP------CIAEMPTVKEIYAKYKDKGLKVVGISMDN--SKAAWMK 317
Cdd:cd02971     1 KAPDFTLPATDGGEVSLSDFKGKWVVLFFY-----PkdftpvCTTELCAFRDLAEEFAKGGAEVLGVSVDSpfSHKAWAE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2469828359 318 SIDKIQIPWLhvsSLKGMKrcpVAELYQVYaIPK----------LYIIDKEGKIV 362
Cdd:cd02971    76 KEGGLNFPLL---SDPDGE---FAKAYGVL-IEKsaggglaaraTFIIDPDGKIR 123
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 256-362 6.37e-14

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 67.72  E-value: 6.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 256 TGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISmdNSKAAWMKSIDKIQipwlhvsslKGM 335
Cdd:cd03012    12 TDKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVH--SPEFAFERDLANVK---------SAV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2469828359 336 KRC----PVA--------ELYQVYAIPKLYIIDKEGKIV 362
Cdd:cd03012    81 LRYgityPVAndndyatwRAYGNQYWPALYLIDPTGNVR 119
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 248-363 1.65e-13

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: 66.55  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 248 PDFTLPTVTGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYkdkglKVVGISM----DNSKAAWMKSIDKiq 323
Cdd:cd03011     1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADY-----PVVSVALrsgdDGAVARFMQKKGY-- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2469828359 324 iPWLHVSSLKGMkrcpVAELYQVYAIPKLYIIDKeGKIVD 363
Cdd:cd03011    74 -GFPVINDPDGV----ISARWGVSVTPAIVIVDP-GGIVF 107
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 262-369 1.70e-13

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: 66.87  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 262 LASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKG--LKVVGISMDNSKAAwMKSIDKIQIPWLHV--SSLKGMKR 337
Cdd:cd02964    12 VSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGknFEIVFVSRDRSEES-FNEYFSEMPPWLAVpfEDEELREL 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2469828359 338 cpVAELYQVYAIPKLYIIDKEGKIVDKDLRGE 369
Cdd:cd02964    91 --LEKQFKVEGIPTLVVLKPDGDVVTTNARDE 120
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 257-377 2.00e-13

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: 66.54  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 257 GEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKG--LKVVGISMDNSKAAWMKSIDKiqIPWLHV--SSL 332
Cdd:cd03009     8 GGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGknFEIVFISWDRDEESFNDYFSK--MPWLAVpfSDR 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2469828359 333 KGMKRcpVAELYQVYAIPKLYIIDKEGKIVDKDLRGEDLKKKVDG 377
Cdd:cd03009    86 ERRSR--LNRTFKIEGIPTLIILDADGEVVTTDARELVLEYGADA 128
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 241-361 3.24e-13

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: 66.53  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 241 LAPGAKAPDFTLPTVTGEEFSLASL--QGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDN--SKAAWM 316
Cdd:cd03018     1 LEVGDKAPDFELPDQNGQEVRLSEFrgRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSpfSLRAWA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2469828359 317 KSiDKIQIPWLHVSSLKGmkrcPVAELYQVY----AIPK--LYIIDKEGKI 361
Cdd:cd03018    81 EE-NGLTFPLLSDFWPHG----EVAKAYGVFdedlGVAEraVFVIDRDGII 126
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 255-364 1.47e-12

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: 63.30  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 255 VTGEEFSLASLQGH-IVILDFWASWCAPCIAEMPTVKEIYAKYKDKgLKVVGISMDNSKAawmksidkiqipwlhvsslk 333
Cdd:COG3118     5 LTDENFEEEVLESDkPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDVDENPE-------------------- 63

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2469828359 334 gmkrcpVAELYQVYAIPKLYIIdKEGKIVDK 364
Cdd:COG3118    64 ------LAAQFGVRSIPTLLLF-KDGQPVDR 87
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 245-362 2.80e-12

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 63.72  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 245 AKAPDFTLPTVTGEEFSLASLQGHIVILDFWaswcaP------CIAEMPTVKEIYAKYKDKGLKVVGISMDNSKAAWmKS 318
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFY-----PkddtpgCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHA-KF 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2469828359 319 IDKIQIPWLHVSSLKGmkrcPVAELYQVYAIPKL---------YIIDKEGKIV 362
Cdd:cd03017    75 AEKYGLPFPLLSDPDG----KLAKAYGVWGEKKKkymgierstFLIDPDGKIV 123
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 216-361 3.76e-12

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: 64.03  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 216 NGMGEKAKKTPKGIELKESIAKMKALAPGakapdfTLPTVTGEEFSlaslQGHIVILDFWASWCAPCIAEMPTVKEIYAk 295
Cdd:TIGR00385  22 NAEGDDPKALPSALIGKPVPAFRLASLDE------PGQFYTADVLT----QGKPVLLNVWASWCPPCRAEHPYLNELAK- 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2469828359 296 ykdKGLKVVGISM-DNSKAAwMKSIDKIQIPW-LHVSSLKGMkrcpVAELYQVYAIPKLYIIDKEGKI 361
Cdd:TIGR00385  91 ---QGLPIVGVDYkDDRQNA-IKFLKELGNPYqLSLFDPDGM----LGLDLGVYGAPETFLVDGNGVI 150
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 244-361 3.82e-10

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: 58.28  E-value: 3.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 244 GAKAPDFTLPTVTG----EEFSLASLQGHIVILDFW-ASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDN--SKAAWM 316
Cdd:cd03015     2 GKKAPDFKATAVVPngefKEISLSDYKGKWVVLFFYpLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDShfSHLAWR 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2469828359 317 KS------IDKIQIPWlhVSSLKGmkrcPVAELYQVY------AIPKLYIIDKEGKI 361
Cdd:cd03015    82 NTprkeggLGKINFPL--LADPKK----KISRDYGVLdeeegvALRGTFIIDPEGII 132
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 244-382 4.93e-10

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: 58.02  E-value: 4.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 244 GAKAPDFTLPTVTGEEFSLASLQGHIVILDFWAswCAPCiaemPTVKEIY-------AKYKDKGLKVVGI---------- 306
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFI--CNHC----PYVKAIEdrlnrlaKEYGAKGVAVVAInsndieaype 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 307 -SMDNSKaAWMKSiDKIQIPWLHVSSLKgmkrcpVAELYQVYAIPKLYIIDKEGKIV------------DKDLRGEDLKK 373
Cdd:cd02969    75 dSPENMK-AKAKE-HGYPFPYLLDETQE------VAKAYGAACTPDFFLFDPDGKLVyrgriddsrpgnDPPVTGRDLRA 146


                  ....*....
gi 2469828359 374 KVDGLFARQ 382
Cdd:cd02969   147 ALDALLAGK 155
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 267-362 1.27e-08

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: 53.11  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 267 GHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKgLKVVGISMDNSKaaWMKSIDKiqipwlhvsslkgmkrcpvaelYQV 346
Cdd:cd02950    20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQ-VNFVMLNVDNPK--WLPEIDR----------------------YRV 74

                          90
                  ....*....|....*.
gi 2469828359 347 YAIPKLYIIDKEGKIV 362
Cdd:cd02950    75 DGIPHFVFLDREGNEE 90
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 238-312 6.15e-08

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 51.48  E-value: 6.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2469828359 238 MKALAPGAKAPDFTLPTVTGEEFSLASLQGHIVILDFWASWCAP-CIAEMPTVKEIYAKYKDKGLKVVGISMDNSK 312
Cdd:PRK09437    1 MNPLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFYPKAMTPgCTVQACGLRDNMDELKKAGVVVLGISTDKPE 76
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 244-361 1.90e-07

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 50.76  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 244 GAKAPDFTLPTVT--GEEFSLASL-QGHIVILDFWASWCAPCIAEMPTVKEIYAkykdKGLKVVGISM--DNSKA-AWMK 317
Cdd:PRK15412   42 GKPVPKFRLESLEnpGQFYQADVLtQGKPVLLNVWATWCPTCRAEHQYLNQLSA----QGIRVVGMNYkdDRQKAiSWLK 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2469828359 318 SIDKiqiPW-LHVSSLKGMKRCPVAelyqVYAIPKLYIIDKEGKI 361
Cdd:PRK15412  118 ELGN---PYaLSLFDGDGMLGLDLG----VYGAPETFLIDGNGII 155
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 258-380 2.11e-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: 48.32  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 258 EEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDkgLKVVGISMDNSKAawmksidkiqipwlhvsslkgmkr 337
Cdd:cd02947     1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDVDENPE------------------------ 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2469828359 338 cpVAELYQVYAIPKLYIIdKEGKIVDKdLRGEDLKKKVDGLFA 380
Cdd:cd02947    55 --LAEEYGVRSIPTFLFF-KNGKEVDR-VVGADPKEELEEFLE 93
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
244-362 5.61e-07

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 49.69  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 244 GAKAPDFTLPTVTGEEF---SLASLQGHIVILDFWaswcaP------CIAEMPTVKEIYAKYKDKGLKVVGISMDN--SK 312
Cdd:COG0450     6 GDKAPDFTAEATHGGEFkkiSLSDYKGKWVVLFFH-----PadftfvCPTELGAFAKRYEEFKKLGVEVIGLSVDSvfSH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2469828359 313 AAWMKSID------KIQIPWLHVSSLKgmkrcpVAELYQVYaIPK-------LYIIDKEGKIV 362
Cdd:COG0450    81 KAWHETIKekggivKIKFPIIADPTGK------IARAYGML-HPEdgvavrgVFIIDPDGKIR 136
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 255-364 1.98e-06

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: 45.74  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 255 VTGEEFSLASLQGHI-VILDFWASWCAPCIAEMPTVKEIYAKYKDKgLKVVGISMDNSKAawmksidkiqipwlhvsslk 333
Cdd:TIGR01068   1 LTDANFDETIASSDKpVLVDFWAPWCGPCKMIAPILEELAKEYEGK-VKFVKLNVDENPD-------------------- 59

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2469828359 334 gmkrcpVAELYQVYAIPKLyIIDKEGKIVDK 364
Cdd:TIGR01068  60 ------IAAKYGIRSIPTL-LLFKNGKEVDR 83
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 246-310 5.63e-06

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: 45.81  E-value: 5.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2469828359 246 KAPDFTLPTVTGEEFSLASLQGH--IVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDN 310
Cdd:cd02970     1 TAPDFELPDAGGETVTLSALLGEgpVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPES 67
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 254-364 9.67e-06

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 44.15  E-value: 9.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 254 TVTGEEFSLASLQGH-IVILDFWASWCAPCIAEMPTVKEIYAKYKDkglKVVGISMDNSKAAwmksidkiqipwlhvssl 332
Cdd:pfam00085   4 VLTDANFDEVVQKSSkPVLVDFYAPWCGPCKMLAPEYEELAQEYKG---NVVFAKVDVDENP------------------ 62

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2469828359 333 kgmkrcPVAELYQVYAIPKLYIIdKEGKIVDK 364
Cdd:pfam00085  63 ------DLASKYGVRGYPTLIFF-KNGQPVDD 87
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 265-312 1.05e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 47.54  E-value: 1.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2469828359  265 LQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGI---SMDNSK 312
Cdd:PLN02919   418 LKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQPFTVVGVhsaKFDNEK 468
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 247-363 1.10e-05

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 44.90  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 247 APDFTLPTVTGEEFSLASLQGHIVILDFWASWCaP--CIAEMPTVKEIYAKYKDKG---LKVVGISMD------NSKAAW 315
Cdd:cd02968     2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHC-PdvCPTTLANLAQALKQLGADGgddVQVVFISVDperdtpEVLKAY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2469828359 316 MKSIDKIqipWLHVS-SLKGMKRcpVAELYQVYAIPK--------------LYIIDKEGKIVD 363
Cdd:cd02968    81 AKAFGPG---WIGLTgTPEEIEA--LAKAFGVYYEKVpeddgdylvdhsaaIYLVDPDGKLVR 138
PTZ00051 PTZ00051
thioredoxin; Provisional
 256-366 3.77e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 42.17  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 256 TGEEFSLASLQGHIVILDFWASWCAPCIAEMPTVKEIYAKYKdkglKVVGISMDnskaawmksIDKIQipwlhvsslkgm 335
Cdd:PTZ00051    7 SQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYT----KMVFVKVD---------VDELS------------ 61

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2469828359 336 krcPVAELYQVYAIP--KLYiidKEGKIVDKDL 366
Cdd:PTZ00051   62 ---EVAEKENITSMPtfKVF---KNGSVVDTLL 88
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 249-305 3.87e-05

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 43.27  E-value: 3.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2469828359 249 DFTLPTVTGEEFSLASLQGHIVILDFWASWC--APCIAEMptvKEIYAKYKDKGLKVVG 305
Cdd:cd00340     4 DFSVKDIDGEPVSLSKYKGKVLLIVNVASKCgfTPQYEGL---EALYEKYKDRGLVVLG 59
DUF4369 pfam14289
Domain of unknown function (DUF4369); This domain family is found in bacteria, and is ...
 25-109 1.22e-04

Domain of unknown function (DUF4369); This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00578. LPAM signal peptide sequence is found in some family members.


Pssm-ID: 433842  Cd Length: 92  Bit Score: 40.41  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359  25 YQIEGKWaTGI--GKKVYLSNfpaDTPEAVTIDSTIVApDGSYKLSGKLDKMQLLSLTHEGSKGFRPLMGDGKPANILIR 102
Cdd:pfam14289   1 YTIEGTI-KGLkdGTKVYLSY---DGGGLVKLDSAVVK-NGKFTFKGKVDEPPMAYLLIDDKSGALPFFLENGTITIKLD 75


                  ....*..
gi 2469828359 103 DMEYSYK 109
Cdd:pfam14289  76 PGDFIAK 82
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 256-376 1.52e-04

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 40.33  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 256 TGEEFS--LASLQGHIVILDFWASWCAPCiAEMPTVKEIYAKYKDKGLKVVgismdnskaawmkSIDKIQIPwlhvsslk 333
Cdd:cd02984     1 SEEEFEelLKSDASKLLVLHFWAPWAEPC-KQMNQVFEELAKEAFPSVLFL-------------SIEAEELP-------- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2469828359 334 gmkrcPVAELYQVYAIPKLYIIdKEGKIVDKdLRGED---LKKKVD 376
Cdd:cd02984    59 -----EISEKFEITAVPTFVFF-RNGTIVDR-VSGADpkeLAKKVE 97
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 271-327 9.27e-04

Thioredoxin (TRX) superfamily; 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 TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 37.29  E-value: 9.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2469828359 271 ILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDNSKAAWMKSIDKIQIPWL 327
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTL 57
trxA PRK09381
thioredoxin TrxA;
269-311 9.62e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 38.51  E-value: 9.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2469828359 269 IVILDFWASWCAPCIAEMPTVKEIYAKYKDKgLKVVGISMDNS 311
Cdd:PRK09381   23 AILVDFWAEWCGPCKMIAPILDEIADEYQGK-LTVAKLNIDQN 64
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 270-362 1.02e-03

bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB;


Pssm-ID: 184456 [Multi-domain]  Cd Length: 521  Bit Score: 41.01  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 270 VILDFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGIS---MDNSKAA-----WMKSIDKIQIPWLHVSSLKGMKRCPVa 341
Cdd:PRK14018   59 TLIKFWASWCPLCLSELGETEKWAQDAKFSSANLITVAspgFLHEKKDgdfqkWYAGLDYPKLPVLTDNGGTLAQSLNI- 137

                          90       100
                  ....*....|....*....|.
gi 2469828359 342 elyQVYaiPKLYIIDKEGKIV 362
Cdd:PRK14018  138 ---SVY--PSWAIIGKDGDVQ 153
PRK10996 PRK10996
thioredoxin 2; Provisional
 270-299 1.47e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 38.51  E-value: 1.47e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2469828359 270 VILDFWASWCAPCIAEMPTVKEIYAKYKDK 299
Cdd:PRK10996   55 VVIDFWAPWCGPCRNFAPIFEDVAAERSGK 84
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 244-326 2.58e-03

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 38.68  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 244 GAKAPDFTLPTVTGeEFSLASLQGHIVIL-DFWASWCAPCIAEMPTVKEIYAKYKDKGLKVVGISMDN--SKAAWMKSID 320
Cdd:PRK13190    5 GQKAPDFTVNTTKG-PIDLSKYKGKWVLLfSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSiySHIAWLRDIE 83


                  ....*....
gi 2469828359 321 K---IQIPW 326
Cdd:PRK13190   84 ErfgIKIPF 92
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 258-301 5.44e-03

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 36.10  E-value: 5.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2469828359 258 EEFSLASLQgHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKGL 301
Cdd:cd02956     4 QQVLQESTQ-VPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFV 46
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
241-272 6.09e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 37.38  E-value: 6.09e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2469828359 241 LAPGAKAPDFTLPTVTGEEFSLASLQGHIVIL 272
Cdd:COG2077    18 PKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVL 49
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 271-292 9.36e-03

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 35.35  E-value: 9.36e-03
                          10        20
                  ....*....|....*....|..
gi 2469828359 271 ILDFWASWCAPCIAEMPTVKEI 292
Cdd:cd03004    23 LVDFYAPWCGPCQALLPELRKA 44
mauD cd02967
Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD ...
 248-366 9.74e-03

Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD gene found in methylotrophic bacteria, which are able to use methylamine as a sole carbon source and a nitrogen source. mauD is an essential accessory protein for the biosynthesis of methylamine dehydrogenase (MADH), the enzyme that catalyzes the oxidation of methylamine and other primary amines. MADH possesses an alpha2beta2 subunit structure; the alpha subunit is also referred to as the large subunit. Each beta (small) subunit contains a tryptophan tryptophylquinone (TTQ) prosthetic group. Accessory proteins are essential for the proper transport of MADH to the periplasm, TTQ synthesis and the formation of several structural disulfide bonds. Bacterial mutants containing an insertion on the mauD gene were unable to grow on methylamine as a sole carbon source, were found to lack the MADH small subunit and had decreased amounts of the MADH large subunit.


Pssm-ID: 239265  Cd Length: 114  Bit Score: 35.84  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469828359 248 PDFTLPTVTGEEFSLASLQ-GHIVILDFWASWCAPCIAEMPTVKEIYAKYKDKgLKVVGISmDNSKAAWMKSIDKIQ--- 323
Cdd:cd02967     1 PTFDLTTIDGAPVRIGGISpGRPTLLFFLSPTCPVCKKLLPVIRSIARAEADW-LDVVLAS-DGEKAEHQRFLKKHGlea 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2469828359 324 IPWLhVSSLKGMKrcpvaelYQVYAIPKLYIIDKEGKIVDKDL 366
Cdd:cd02967    79 FPYV-LSAELGMA-------YQVSKLPYAVLLDEAGVIAAKGL 113
 
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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