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Conserved domains on  [gi|495296179|ref|WP_008020932|]
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MULTISPECIES: TlpA disulfide reductase family protein [Bacteroides]

Protein Classification

TlpA family protein disulfide reductase( domain architecture ID 10001660)

TlpA family protein disulfide reductase such as Bradyrhizobium japonicum thiol:disulfide interchange protein TlpA, an unusual thioredoxin which has been implicated in the biogenesis of cytochrome aa3 and also characterized as a reductant for the copper metallochaperone ScoI, and similar to ResA and DsbE, which are essential proteins in cytochrome c maturation

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 199-339 6.99e-41

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 139.82  E-value: 6.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKadDLEFISVSLDDSEAKWRKMLDEE 278
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDENPEAVKAFLKEL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495296179 279 KLPWVMLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGKLAARNVRG---EQVREAILKI 339
Cdd:COG0526   82 GLPYPVLLDPDG---------ELAKAYGVRGIPTTVLIDKDGKIVARHVGPlspEELEEALEKL 136
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 199-339 6.99e-41

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 139.82  E-value: 6.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKadDLEFISVSLDDSEAKWRKMLDEE 278
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDENPEAVKAFLKEL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495296179 279 KLPWVMLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGKLAARNVRG---EQVREAILKI 339
Cdd:COG0526   82 GLPYPVLLDPDG---------ELAKAYGVRGIPTTVLIDKDGKIVARHVGPlspEELEEALEKL 136
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 205-327 3.47e-33

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 118.88  E-value: 3.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 205 DFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDDS-EAKWRKMLDEEKLPWV 283
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDdPAAVKAFLKKYGITFP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 495296179 284 MLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGKLAARNV 327
Cdd:cd02966   81 VLLDPDG---------ELAKAYGVRGLPTTFLIDRDGRIRARHV 115
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 199-325 3.15e-26

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: 100.76  E-value: 3.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDF-CASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDDSE--AKWRKml 275
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFyPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPEshKAFAE-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495296179  276 dEEKLPWVMLWDKAGfpknsktpsAIQTAYG------FYSIPFLVVIDKEGKLAAR 325
Cdd:pfam00578  79 -KYGLPFPLLSDPDG---------EVARAYGvlneeeGGALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
199-336 8.70e-20

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 85.05  E-value: 8.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDDSEAKWRKMLDEE 278
Cdd:PRK03147  37 VGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRY 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495296179 279 KLPWVMLWDKAGFPKNsktpsaiqtAYGFYSIPFLVVIDKEGKLaARNVRGEQVREAI 336
Cdd:PRK03147 117 GLTFPVAIDKGRQVID---------AYGVGPLPTTFLIDKDGKV-VKVITGEMTEEQL 164
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 198-334 1.39e-08

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: 53.63  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  198 IIGAECPDFTFT--DANGKNVSLKDFR-GKIVVLDFCASWCGPCRKEMRSMltiyNELKADDLEFISVSLDDSEAKWRKM 274
Cdd:TIGR00385  35 LIGKPVPAFRLAslDEPGQFYTADVLTqGKPVLLNVWASWCPPCRAEHPYL----NELAKQGLPIVGVDYKDDRQNAIKF 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  275 LDEEKLPWVMLWDkagfpkNSKTPSAIQtaYGFYSIPFLVVIDKEGKLAARNVrGEQVRE 334
Cdd:TIGR00385 111 LKELGNPYQLSLF------DPDGMLGLD--LGVYGAPETFLVDGNGVIRYRHA-GPLNPE 161
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 199-339 6.99e-41

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 139.82  E-value: 6.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKadDLEFISVSLDDSEAKWRKMLDEE 278
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVDENPEAVKAFLKEL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495296179 279 KLPWVMLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGKLAARNVRG---EQVREAILKI 339
Cdd:COG0526   82 GLPYPVLLDPDG---------ELAKAYGVRGIPTTVLIDKDGKIVARHVGPlspEELEEALEKL 136
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
204-338 8.66e-41

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 139.62  E-value: 8.66e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 204 PDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDDSEaKWRKMLDEEKLPWV 283
Cdd:COG1225    2 PDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDE-AHKKFAEKYGLPFP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495296179 284 MLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGKLAARNVRG-------EQVREAILK 338
Cdd:COG1225   81 LLSDPDG---------EVAKAYGVRGTPTTFLIDPDGKIRYVWVGPvdprphlEEVLEALLA 133
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 205-327 3.47e-33

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 118.88  E-value: 3.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 205 DFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDDS-EAKWRKMLDEEKLPWV 283
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDdPAAVKAFLKKYGITFP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 495296179 284 MLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGKLAARNV 327
Cdd:cd02966   81 VLLDPDG---------ELAKAYGVRGLPTTFLIDRDGRIRARHV 115
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 199-325 3.15e-26

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: 100.76  E-value: 3.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDF-CASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDDSE--AKWRKml 275
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFyPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPEshKAFAE-- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495296179  276 dEEKLPWVMLWDKAGfpknsktpsAIQTAYG------FYSIPFLVVIDKEGKLAAR 325
Cdd:pfam00578  79 -KYGLPFPLLSDPDG---------EVARAYGvlneeeGGALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
199-336 8.70e-20

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 85.05  E-value: 8.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDDSEAKWRKMLDEE 278
Cdd:PRK03147  37 VGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRY 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495296179 279 KLPWVMLWDKAGFPKNsktpsaiqtAYGFYSIPFLVVIDKEGKLaARNVRGEQVREAI 336
Cdd:PRK03147 117 GLTFPVAIDKGRQVID---------AYGVGPLPTTFLIDKDGKV-VKVITGEMTEEQL 164
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 200-327 3.83e-18

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 80.11  E-value: 3.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  200 GAECPDFTFTDA--NGKNVSLKDFRGKIVVLDFCAS-WCGPCRKEMRSMLTIYNELKADDLEFISVSLDDSEAKWRKMLD 276
Cdd:pfam08534   3 GDKAPDFTLPDAatDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVKRFWG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  277 EEKLPWVMLWDKAGfpknsktpsAIQTAYG---------FYSIPFLVVIDKEGKLAARNV 327
Cdd:pfam08534  83 KEGLPFPFLSDGNA---------AFTKALGlpieedasaGLRSPRYAVIDEDGKVVYLFV 133
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 223-321 8.63e-15

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: 69.26  E-value: 8.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  223 GKIVVLDFCASWCGPCRKEMRSMLTIYNELKA-DDLEFISVSLDDSEAKWRKMLDEEKLPWVMlwdkagFPKNSKTPSAI 301
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKkKNVEIVFVSLDRDLEEFKDYLKKMPKDWLS------VPFDDDERNEL 74

                          90       100
                  ....*....|....*....|
gi 495296179  302 QTAYGFYSIPFLVVIDKEGK 321
Cdd:pfam13905  75 KRKYGVNAIPTLVLLDPNGE 94
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 212-330 9.59e-15

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: 70.01  E-value: 9.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 212 NGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKA--DDLEFISVSLDDSE----AKWRKMldeeklPWVML 285
Cdd:cd03009    7 DGGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEsgKNFEIVFISWDRDEesfnDYFSKM------PWLAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 495296179 286 -WDKagfpknSKTPSAIQTAYGFYSIPFLVVIDKEGKLAARNVRGE 330
Cdd:cd03009   81 pFSD------RERRSRLNRTFKIEGIPTLIILDADGEVVTTDAREL 120
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 204-327 2.84e-14

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: 69.11  E-value: 2.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 204 PDFTFTDANGKNVSLKDFRGKIVVL-----DF---CAswcgpcrKEMRSMLTIYNELKADDLEFISVSLDDSEA--KWRK 273
Cdd:cd02971    3 PDFTLPATDGGEVSLSDFKGKWVVLffypkDFtpvCT-------TELCAFRDLAEEFAKGGAEVLGVSVDSPFShkAWAE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495296179 274 mlDEEKLPWVMLWDKAGfpknsktpsAIQTAYGFY---------SIPFLVVIDKEGKLAARNV 327
Cdd:cd02971   76 --KEGGLNFPLLSDPDG---------EFAKAYGVLieksaggglAARATFIIDPDGKIRYVEV 127
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 212-330 1.50e-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: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 212 NGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADD--LEFISVSLDDSEAKWRKMLdEEKLPWVMLwdka 289
Cdd:cd02964    6 GEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGknFEIVFVSRDRSEESFNEYF-SEMPPWLAV---- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495296179 290 gfP-KNSKTPSAIQTAYGFYSIPFLVVIDKEGKLAARNVRGE 330
Cdd:cd02964   81 --PfEDEELRELLEKQFKVEGIPTLVVLKPDGDVVTTNARDE 120
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 207-341 2.93e-13

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 66.46  E-value: 2.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 207 TFTDANGKNVSLKDFRGKIVVLDFCASWC-GPCRKEMRSMLTIYNELKA---DDLEFISVSLD---DSEAKWRKMLDEEK 279
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCpDVCPTTLANLAQVQEALGEdggDDVQVLFISVDperDTPEVLKAYAEAFG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495296179 280 LP-WVMLwdkagfpknSKTPSAIQT---AYGFYSIP------------FLVVIDKEGKLAARNVRGEQVREAILKIRQ 341
Cdd:COG1999   84 APrWIGL---------TGDPEEIAAlakAFGVYYEKvpdgdytfdhsaAVYLVDPDGRLRGYYPAGEDPEELAADLKA 152
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 204-324 1.41e-12

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: 64.16  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 204 PDFTFTDANGKNVSLKDFRGKIVVLDF----CASWCGPCRKEMRSMLTIYNELKADDLEFISVSLD---DSEAKWRKMLD 276
Cdd:cd02968    3 PDFTLTDQDGRPVTLSDLKGKPVLVYFgythCPDVCPTTLANLAQALKQLGADGGDDVQVVFISVDperDTPEVLKAYAK 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495296179 277 EEKLPWVMLwdkAGFPKNSKtpsAIQTAYGFYSIP--------------FLVVIDKEGKLAA 324
Cdd:cd02968   83 AFGPGWIGL---TGTPEEIE---ALAKAFGVYYEKvpeddgdylvdhsaAIYLVDPDGKLVR 138
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 200-336 1.52e-09

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: 56.48  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 200 GAECPDFTFTDANGKNVSLKDFR-GKIVVLDF-CASwCgPCRKEMRSML-TIYNELKADDLEFISVS-------LDDSEA 269
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFAdGKALVVMFiCNH-C-PYVKAIEDRLnRLAKEYGAKGVAVVAINsndieayPEDSPE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495296179 270 KWRKMLDEEKLPWVMLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGKL------------AARNVRGEQVREAI 336
Cdd:cd02969   79 NMKAKAKEHGYPFPYLLDETQ---------EVAKAYGAACTPDFFLFDPDGKLvyrgriddsrpgNDPPVTGRDLRAAL 148
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 201-328 1.92e-09

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: 55.25  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 201 AECPDFTFTDANGKNVSLKDFRGKIVVLDFCaswcgP------CRKEMRSMLTIYNELKADDLEFISVSLDDSE--AKWR 272
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFY-----PkddtpgCTKEACDFRDLYEEFKALGAVVIGVSPDSVEshAKFA 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495296179 273 kmlDEEKLPWVMLWDKAGfpknsktpsAIQTAYGFYSIPFLV---------VIDKEGKLAA--RNVR 328
Cdd:cd03017   76 ---EKYGLPFPLLSDPDG---------KLAKAYGVWGEKKKKymgierstfLIDPDGKIVKvwRKVK 130
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 198-334 1.39e-08

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: 53.63  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  198 IIGAECPDFTFT--DANGKNVSLKDFR-GKIVVLDFCASWCGPCRKEMRSMltiyNELKADDLEFISVSLDDSEAKWRKM 274
Cdd:TIGR00385  35 LIGKPVPAFRLAslDEPGQFYTADVLTqGKPVLLNVWASWCPPCRAEHPYL----NELAKQGLPIVGVDYKDDRQNAIKF 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  275 LDEEKLPWVMLWDkagfpkNSKTPSAIQtaYGFYSIPFLVVIDKEGKLAARNVrGEQVRE 334
Cdd:TIGR00385 111 LKELGNPYQLSLF------DPDGMLGLD--LGVYGAPETFLVDGNGVIRYRHA-GPLNPE 161
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 199-327 4.80e-08

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: 51.51  E-value: 4.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRG-KIVVLDFC-ASWCGPCRKEMRSMLTIYNELKADDLEFISVSLDD--SEAKWRkm 274
Cdd:cd03018    3 VGDKAPDFELPDQNGQEVRLSEFRGrKPVVLVFFpLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSpfSLRAWA-- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 275 lDEEKLPWVMLWDkagfpknSKTPSAIQTAYGFYsIPFL-------VVIDKEGKLAARNV 327
Cdd:cd03018   81 -EENGLTFPLLSD-------FWPHGEVAKAYGVF-DEDLgvaeravFVIDRDGIIRYAWV 131
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 204-265 1.56e-07

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 49.87  E-value: 1.56e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495296179  204 PDFTFTDANGKNVSLKDFRGKIVVLDFCASWCgP--CRKEMRSMLTIYNELK--ADDLEFISVSLD 265
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFFGFTHC-PdvCPTTLPNMAQVLDALGeeGIDVQPVFITVD 66
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 222-336 1.65e-07

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 49.05  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 222 RGKIVVLDFCASWCGPCrkemRSMLTIYNELKA---DDLEFISVSLDDSEakwrkmldeeklpwvmlwdkagfpknsktp 298
Cdd:COG3118   17 SDKPVLVDFWAPWCGPC----KMLAPVLEELAAeygGKVKFVKVDVDENP------------------------------ 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 495296179 299 sAIQTAYGFYSIPFLVVIdKEGKLAARNVRG---EQVREAI 336
Cdd:COG3118   63 -ELAAQFGVRSIPTLLLF-KDGQPVDRFVGAlpkEQLREFL 101
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 204-321 2.15e-07

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: 49.22  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 204 PDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIynelkADDLEFISVSL-DDSEAKWRKMLDEEKLPW 282
Cdd:cd03011    1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQL-----AADYPVVSVALrSGDDGAVARFMQKKGYGF 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495296179 283 VMLWDKAGfpknsktpsAIQTAYGFYSIPFLVVIDKEGK 321
Cdd:cd03011   76 PVINDPDG---------VISARWGVSVTPAIVIVDPGGI 105
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 204-327 2.66e-07

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: 48.73  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 204 PDFTFTDAngknvslkDFRGKIVVLDFCASWCGPCRKEMRSMLtiynELKAD-DLEFISVSLDDSEAKWRKMLDEEKLPW 282
Cdd:cd03010   14 PDKTLTSA--------DLKGKPYLLNVWASWCAPCREEHPVLM----ALARQgRVPIYGINYKDNPENALAWLARHGNPY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495296179 283 VMLwdkaGFPKNSKTpsAIqtAYGFYSIPFLVVIDKEGKLAARNV 327
Cdd:cd03010   82 AAV----GFDPDGRV--GI--DLGVYGVPETFLIDGDGIIRYKHV 118
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 199-322 2.66e-07

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: 49.81  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFT--DANG--KNVSLKDFRGKIVVL-----DF---CASwcgpcrkEMRSMLTIYNELKADDLEFISVSLDD 266
Cdd:cd03015    1 VGKKAPDFKATavVPNGefKEISLSDYKGKWVVLffyplDFtfvCPT-------EIIAFSDRYEEFKKLNAEVLGVSTDS 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495296179 267 --SEAKWRKMLDEE----KLPWVMLWDKAGfpknsktpsAIQTAYGFY----SIPF--LVVIDKEGKL 322
Cdd:cd03015   74 hfSHLAWRNTPRKEgglgKINFPLLADPKK---------KISRDYGVLdeeeGVALrgTFIIDPEGII 132
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 223-336 3.53e-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: 47.55  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 223 GKIVVLDFCASWCGPCRKemrsMLTIYNEL--KADDLEFISVSLDDSEAKWRKmldeeklpwvmlwdkagfpknsktpsa 300
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKA----IAPVLEELaeEYPKVKFVKVDVDENPELAEE--------------------------- 58

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495296179 301 iqtaYGFYSIPFLVVIdKEGKLAARNVR---GEQVREAI 336
Cdd:cd02947   59 ----YGVRSIPTFLFF-KNGKEVDRVVGadpKEELEEFL 92
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 208-339 1.37e-05

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 43.43  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  208 FTDANGKNVSLKDfrGKIVVLDFCASWCGPCRkemrsMLT-IYNEL---KADDLEFISVSLDDseakwrkmldeeklpwv 283
Cdd:TIGR01068   1 LTDANFDETIASS--DKPVLVDFWAPWCGPCK-----MIApILEELakeYEGKVKFVKLNVDE----------------- 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495296179  284 mlwdkagfpkNSKTPSaiqtAYGFYSIPFLVVIdKEGKLAARNVrGEQVREAILKI 339
Cdd:TIGR01068  57 ----------NPDIAA----KYGIRSIPTLLLF-KNGKEVDRSV-GALPKAALKQL 96
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
199-322 1.19e-04

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 42.37  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDF---TFTDANGKNVSLKDFRGKIVVL-----DF---CASwcgpcrkEMRSMLTIYNELKADDLEFISVSLD-- 265
Cdd:COG0450    5 IGDKAPDFtaeATHGGEFKKISLSDYKGKWVVLffhpaDFtfvCPT-------ELGAFAKRYEEFKKLGVEVIGLSVDsv 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 266 DSEAKW----RKMLDEEKLPWVMLWDKAGfpknsktpsAIQTAYGFYsIP---------FLvvIDKEGKL 322
Cdd:COG0450   78 FSHKAWhetiKEKGGIVKIKFPIIADPTG---------KIARAYGML-HPedgvavrgvFI--IDPDGKI 135
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 204-327 1.83e-04

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: 41.19  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 204 PDFTFTDANGKNVSLKDFR--GKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFISVS---LDDSEAKWRK----- 273
Cdd:cd02970    3 PDFELPDAGGETVTLSALLgeGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGpesPEKLEAFDKGkflpf 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495296179 274 --MLDEEK-----------LPWVMLWdkAGFPKNSKTPSAIQTAYGFYSIPFLVVIDKEGKLAARNV 327
Cdd:cd02970   83 pvYADPDRklyralglvrsLPWSNTP--RALWKNAAIGFRGNDEGDGLQLPGVFVIGPDGTILFAHV 147
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 205-236 3.97e-04

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: 40.19  E-value: 3.97e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 495296179 205 DFTFTDANGKNVSLKDFRGKIVVLDFCASWCG 236
Cdd:cd00340    4 DFSVKDIDGEPVSLSKYKGKVLLIVNVASKCG 35
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 222-265 4.61e-04

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


Pssm-ID: 239246 [Multi-domain]  Cd Length: 102  Bit Score: 38.86  E-value: 4.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495296179 222 RGKIVVLDFCASWCGPCrKEMRSMLT-IYNELKADDLEFISVSLD 265
Cdd:cd02948   16 NKGLTVVDVYQEWCGPC-KAVVSLFKkIKNELGDDLLHFATAEAD 59
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 199-334 5.83e-04

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 39.49  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDFCASWCGP-CRKEMRSMLTIYNELkaDDLEFISVSLDDSEAKWRkmlde 277
Cdd:cd03014    2 VGDKAPDFTLVTSDLSEVSLADFAGKVKVISVFPSIDTPvCATQTKRFNKEAAKL--DNTVVLTISADLPFAQKR----- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495296179 278 eklpwvmlWDKAGFPKNSKTPSAIQT-----AYGFYsIPFL-------VVIDKEGKLAARnvrgEQVRE 334
Cdd:cd03014   75 --------WCGAEGVDNVTTLSDFRDhsfgkAYGVL-IKDLgllaravFVIDENGKVIYV----ELVPE 130
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 223-325 7.11e-04

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 40.94  E-value: 7.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 223 GKIVVLDFCASWCGPCrKEM-RSMLT---IYNELKaDDLEFISVSLDDSEAKWRKMLDEeklpwvmlwdkagfpknsktp 298
Cdd:COG4232  320 GKPVFVDFTADWCVTC-KENeRTVFSdpeVQAALA-DDVVLLKADVTDNDPEITALLKR--------------------- 376

                         90       100
                 ....*....|....*....|....*..
gi 495296179 299 saiqtaYGFYSIPFLVVIDKEGKLAAR 325
Cdd:COG4232  377 ------FGRFGVPTYVFYDPDGEELPR 397
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 227-285 8.71e-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: 8.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 227 VLDFCASWCGPCRKeMRSMLTIYNELKAD-DLEFISVSLDDSEAKWRKMLDEEKLPWVML 285
Cdd:cd01659    1 LVLFYAPWCPFCQA-LRPVLAELALLNKGvKFEAVDVDEDPALEKELKRYGVGGVPTLVV 59
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 223-339 1.07e-03

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 38.86  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 223 GKIVVLDFCASWCGPCRKEMRSMLTIYNELKaDDLEFISVSLDDSeaKWRKMLDEeklpwvmlwdkagfpknsktpsaiq 302
Cdd:cd02950   20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYG-DQVNFVMLNVDNP--KWLPEIDR------------------------- 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495296179 303 taYGFYSIPFLVVIDKEGKLAARNVrGEQVREAILKI 339
Cdd:cd02950   72 --YRVDGIPHFVFLDREGNEEGQSI-GLQPKQVLAQN 105
PLN02412 PLN02412
probable glutathione peroxidase
 205-261 1.23e-03

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 39.20  E-value: 1.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495296179 205 DFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFIS 261
Cdd:PLN02412  11 DFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILA 67
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
223-339 1.76e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.40  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179  223 GKIVVLDFCASWCGPCRK---EMRSMLTIYNELKAdDLEFISVSLDDSEakwrkmldeeklpwvmlwDKAGFPKNSKTPS 299
Cdd:pfam13098   4 GKPVLVVFTDPDCPYCKKlkkELLEDPDVTVYLGP-NFVFIAVNIWCAK------------------EVAKAFTDILENK 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 495296179  300 AIQTAYGFYSIPFLVVIDKEGKLAarNVRGEQVREAILKI 339
Cdd:pfam13098  65 ELGRKYGVRGTPTIVFFDGKGELL--RLPGYVPAEEFLAL 102
tpx PRK00522
thiol peroxidase;
199-265 2.08e-03

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 38.34  E-value: 2.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 199 IGAECPDFTFTDANGKNVSLKDFRGKIVVLDFCASW-CGPCRKEMRSmltiYNELKA--DDLEFISVSLD 265
Cdd:PRK00522  20 VGDKAPDFTLVANDLSDVSLADFAGKRKVLNIFPSIdTGVCATSVRK----FNQEAAelDNTVVLCISAD 85
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 207-240 2.22e-03

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: 37.21  E-value: 2.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 495296179  207 TFTDANGKNVSLKDfrGKIVVLDFCASWCGPCRK 240
Cdd:pfam00085   4 VLTDANFDEVVQKS--SKPVLVDFYAPWCGPCKM 35
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 209-298 2.66e-03

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 36.84  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 209 TDANGKNVSLKDfrGKIVVLDFCASWCGPCRKemrsMLTIYNEL-----KADDLEFISVSLDDSEAKWRKMLDEEKLPWV 283
Cdd:cd02998    6 TDSNFDKVVGDD--KKDVLVEFYAPWCGHCKN----LAPEYEKLaavfaNEDDVVIAKVDADEANKDLAKKYGVSGFPTL 79

                         90
                 ....*....|....*
gi 495296179 284 MLwdkagFPKNSKTP 298
Cdd:cd02998   80 KF-----FPKGSTEP 89
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 205-261 2.72e-03

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 38.73  E-value: 2.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495296179 205 DFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFIS 261
Cdd:PLN02399  81 DFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILA 137
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 223-325 3.97e-03

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 37.19  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 223 GKIVVLDFCASWCGPCRKEMRSMLTiyNELKADDLE--FISVSLDdseakwrkMLDEEKLPWvmlwdkagFPKNSKTPSA 300
Cdd:COG2143   40 GKPILLFFESDWCPYCKKLHKEVFS--DPEVAAYLKenFVVVQLD--------AEGDKEVTD--------FDGETLTEKE 101

                         90       100
                 ....*....|....*....|....*
gi 495296179 301 IQTAYGFYSIPFLVVIDKEGKLAAR 325
Cdd:COG2143  102 LARKYGVRGTPTLVFFDAEGKEIAR 126
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 205-262 4.07e-03

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 37.91  E-value: 4.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495296179 205 DFTFTDANGKNVSLKDFRGKIVVLDFCASWCGPCRKEMRSMLTIYNELKADDLEFISV 262
Cdd:PTZ00056  21 DYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAF 78
PTZ00051 PTZ00051
thioredoxin; Provisional
 225-266 7.71e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 35.62  E-value: 7.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 495296179 225 IVVLDFCASWCGPCRKemrsMLTIYNELKAD--DLEFISVSLDD 266
Cdd:PTZ00051  20 LVIVDFYAEWCGPCKR----IAPFYEECSKEytKMVFVKVDVDE 59
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 200-288 9.42e-03

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 36.45  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495296179 200 GAECPDFTFTDANGKNVSLKDFRGKIVVLDF--------C-ASWCGpCRKEMrsmltiyNELKADDLEFISVSLDDSEaK 270
Cdd:PRK09437   7 GDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFypkamtpgCtVQACG-LRDNM-------DELKKAGVVVLGISTDKPE-K 77

                         90
                 ....*....|....*...
gi 495296179 271 WRKMLDEEKLPWVMLWDK 288
Cdd:PRK09437  78 LSRFAEKELLNFTLLSDE 95
 
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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