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Conserved domains on  [gi|489180310|ref|WP_003089792|]
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MULTISPECIES: TlpA disulfide reductase family protein [Pseudomonas]

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, ...
 133-262 6.16e-43

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 143.29  E-value: 6.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 133 GTRLPELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAENPDVVFLFANQGESAETVRHFLQGENLR 212
Cdd:COG0526    5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAVKAFLKELGLP 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489180310 213 LdNLLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRGSLARYL 262
Cdd:COG0526   85 Y-PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEAL 133
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 133-262 6.16e-43

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 143.29  E-value: 6.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 133 GTRLPELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAENPDVVFLFANQGESAETVRHFLQGENLR 212
Cdd:COG0526    5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAVKAFLKELGLP 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489180310 213 LdNLLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRGSLARYL 262
Cdd:COG0526   85 Y-PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEAL 133
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 138-251 3.54e-32

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 114.64  E-value: 3.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 138 ELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAE--NPDVVFLFANQGES-AETVRHFLQGENLRLD 214
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEykDDGVEVVGVNVDDDdPAAVKAFLKKYGITFP 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489180310 215 NLLfDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLG 251
Cdd:cd02966   81 VLL-DPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
121-262 1.63e-17

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 77.74  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 121 LLGSLGLGIY----------ERGTRLPELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAENPD--V 188
Cdd:PRK03147  16 LLAAVGYTIYsnffadkekvQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEkgV 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489180310 189 VFLFANQGESAETVRHFLQGENLRLDnLLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRGSLARYL 262
Cdd:PRK03147  96 EIIAVNVDETELAVKNFVNRYGLTFP-VAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLEEYL 168
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 133-245 1.69e-16

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: 73.80  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  133 GTRLPELSLRNAAGESVQLADFRGRPLVINLWAS-WCPPCRREMPVLQQAQAEnpdvvflFANQG--------ESAETVR 203
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEE-------FKKLGvevlgvsvDSPESHK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 489180310  204 HFLQGENLRLDnLLFDNGGQLGQQVG------SVALPTTVFYTAEGRL 245
Cdd:pfam00578  75 AFAEKYGLPFP-LLSDPDGEVARAYGvlneeeGGALRATFVIDPDGKV 121
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 155-258 7.88e-10

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: 56.71  E-value: 7.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  155 RGRPLVINLWASWCPPCRREMPVLQQAQAENPDVVFLfaNQGESAETVRHFLQgenlRLDN----LLFDNGGQLGQQVGS 230
Cdd:TIGR00385  62 QGKPVLLNVWASWCPPCRAEHPYLNELAKQGLPIVGV--DYKDDRQNAIKFLK----ELGNpyqlSLFDPDGMLGLDLGV 135

                          90       100
                  ....*....|....*....|....*...
gi 489180310  231 VALPTTVFYTAEGRLLGSHLGELSRGSL 258
Cdd:TIGR00385 136 YGAPETFLVDGNGVIRYRHAGPLNPEVW 163
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 133-262 6.16e-43

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 143.29  E-value: 6.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 133 GTRLPELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAENPDVVFLFANQGESAETVRHFLQGENLR 212
Cdd:COG0526    5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAVKAFLKELGLP 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489180310 213 LdNLLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRGSLARYL 262
Cdd:COG0526   85 Y-PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEAL 133
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 138-251 3.54e-32

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 114.64  E-value: 3.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 138 ELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAE--NPDVVFLFANQGES-AETVRHFLQGENLRLD 214
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEykDDGVEVVGVNVDDDdPAAVKAFLKKYGITFP 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489180310 215 NLLfDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLG 251
Cdd:cd02966   81 VLL-DPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
137-253 4.25e-26

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 99.55  E-value: 4.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 137 PELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAE--NPDVVFLFANqGESAETVRHFLQGENLRLD 214
Cdd:COG1225    2 PDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEfkDKGVEVLGVS-SDSDEAHKKFAEKYGLPFP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489180310 215 nLLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGEL 253
Cdd:COG1225   81 -LLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPV 118
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
121-262 1.63e-17

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 77.74  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 121 LLGSLGLGIY----------ERGTRLPELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAENPD--V 188
Cdd:PRK03147  16 LLAAVGYTIYsnffadkekvQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEkgV 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489180310 189 VFLFANQGESAETVRHFLQGENLRLDnLLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRGSLARYL 262
Cdd:PRK03147  96 EIIAVNVDETELAVKNFVNRYGLTFP-VAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLEEYL 168
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 133-245 1.69e-16

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: 73.80  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  133 GTRLPELSLRNAAGESVQLADFRGRPLVINLWAS-WCPPCRREMPVLQQAQAEnpdvvflFANQG--------ESAETVR 203
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEE-------FKKLGvevlgvsvDSPESHK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 489180310  204 HFLQGENLRLDnLLFDNGGQLGQQVG------SVALPTTVFYTAEGRL 245
Cdd:pfam00578  75 AFAEKYGLPFP-LLSDPDGEVARAYGvlneeeGGALRATFVIDPDGKV 121
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 136-259 2.44e-14

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 67.99  E-value: 2.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 136 LPELSLRNAAGESVQL--ADFRGRPLVINLWASWCPPCRREMPVLQQaQAENPDVVFLFANQGESAETVRHFLQgenlRL 213
Cdd:cd03010    3 APAFSLPALPGPDKTLtsADLKGKPYLLNVWASWCAPCREEHPVLMA-LARQGRVPIYGINYKDNPENALAWLA----RH 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489180310 214 DN----LLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRGSLA 259
Cdd:cd03010   78 GNpyaaVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPLTPEVWE 127
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 133-261 2.96e-12

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 62.77  E-value: 2.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  133 GTRLPELSLRNAA--GESVQLADFRGRPLVINLWAS-WCPPCRREMPVLQ--QAQAENPDVVFLFANQGESAETVRHFLQ 207
Cdd:pfam08534   3 GDKAPDFTLPDAAtdGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEklNELYKEKGVDVVAVNSDNDAFFVKRFWG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489180310  208 GENlrLDNL-LFDNGGQLGQQVGS---------VALPTTVFYTAEGRLLGSHLGELSRGSLARY 261
Cdd:pfam08534  83 KEG--LPFPfLSDGNAAFTKALGLpieedasagLRSPRYAVIDEDGKVVYLFVGPEPGVDVSDA 144
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 156-232 5.77e-12

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: 60.65  E-value: 5.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 156 GRPLVINLWASWCPPCRREMPVLQQAQAENPDVVFLFANQGESAETVRHFlqgeNLR----LdnLLFDNGGQLGQQVGSV 231
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEY----GVRsiptF--LFFKNGKEVDRVVGAD 83


                 .
gi 489180310 232 A 232
Cdd:cd02947   84 P 84
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 137-243 1.92e-10

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: 57.31  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 137 PELSLRNAAGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQAQAENPdVVFLFANQGESAETVRhFLQGENLRLDNl 216
Cdd:cd03011    1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYP-VVSVALRSGDDGAVAR-FMQKKGYGFPV- 77

                         90       100
                 ....*....|....*....|....*..
gi 489180310 217 LFDNGGQLGQQVGSVALPTTVFYTAEG 243
Cdd:cd03011   78 INDPDGVISARWGVSVTPAIVIVDPGG 104
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 155-258 7.88e-10

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: 56.71  E-value: 7.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  155 RGRPLVINLWASWCPPCRREMPVLQQAQAENPDVVFLfaNQGESAETVRHFLQgenlRLDN----LLFDNGGQLGQQVGS 230
Cdd:TIGR00385  62 QGKPVLLNVWASWCPPCRAEHPYLNELAKQGLPIVGV--DYKDDRQNAIKFLK----ELGNpyqlSLFDPDGMLGLDLGV 135

                          90       100
                  ....*....|....*....|....*...
gi 489180310  231 VALPTTVFYTAEGRLLGSHLGELSRGSL 258
Cdd:TIGR00385 136 YGAPETFLVDGNGVIRYRHAGPLNPEVW 163
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 155-254 8.53e-10

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 56.92  E-value: 8.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 155 RGRPLVINLWASWCPPCRREMPVLQQAQAENPDVVFLfaNQGESAETVRHFLQGENLRLDNLLFDNGGQLGQQVGSVALP 234
Cdd:PRK15412  67 QGKPVLLNVWATWCPTCRAEHQYLNQLSAQGIRVVGM--NYKDDRQKAISWLKELGNPYALSLFDGDGMLGLDLGVYGAP 144

                         90       100
                 ....*....|....*....|
gi 489180310 235 TTVFYTAEGRLLGSHLGELS 254
Cdd:PRK15412 145 ETFLIDGNGIIRYRHAGDLN 164
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 155-262 5.21e-09

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: 52.90  E-value: 5.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 155 RGRPLVINLWASWCPPCRREMPVLQQAQAE-NPDVVFLFANQGESAETVRHFlqgenlrldnllfdnggqlgqQVGSVal 233
Cdd:COG3118   17 SDKPVLVDFWAPWCGPCKMLAPVLEELAAEyGGKVKFVKVDVDENPELAAQF---------------------GVRSI-- 73

                         90       100
                 ....*....|....*....|....*....
gi 489180310 234 PTTVFYtAEGRLLGSHLGELSRGSLARYL 262
Cdd:COG3118   74 PTLLLF-KDGQPVDRFVGALPKEQLREFL 101
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 156-244 1.57e-08

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 51.15  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  156 GRPLVINLWASWCPPCRREMPVLQQAQ---AENPDVVFLFANQGESAETVRHFLQGENLRLDNLLFDNG--GQLGQQVGS 230
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYeklKKKKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDerNELKRKYGV 80

                          90
                  ....*....|....
gi 489180310  231 VALPTTVFYTAEGR 244
Cdd:pfam13905  81 NAIPTLVLLDPNGE 94
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 160-222 1.88e-06

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: 44.61  E-value: 1.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489180310 160 VINLWASWCPPCRREMPVLQQAQAENPDVVFLFANQGESAETVRHFLQGENLRLDNLLFDNGG 222
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLVVFGPG 63
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 157-234 4.58e-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: 44.20  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  157 RPLVINLWASWCPPCRREMPVLQQ-AQAENPDVVFLFANQGESAETVRHFlqgeNLR----LdnLLFDNGGQLGQQVGsv 231
Cdd:TIGR01068  15 KPVLVDFWAPWCGPCKMIAPILEElAKEYEGKVKFVKLNVDENPDIAAKY----GIRsiptL--LLFKNGKEVDRSVG-- 86


                  ...
gi 489180310  232 ALP 234
Cdd:TIGR01068  87 ALP 89
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
156-262 2.93e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 42.03  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  156 GRPLVINLWASWCPPCRREMPVLqqaqAENPDVVFLFanQGESAETVRHFLQGENLRLDNLLFDNGGQLGQQVGSVALPT 235
Cdd:pfam13098   4 GKPVLVVFTDPDCPYCKKLKKEL----LEDPDVTVYL--GPNFVFIAVNIWCAKEVAKAFTDILENKELGRKYGVRGTPT 77

                          90       100
                  ....*....|....*....|....*..
gi 489180310  236 TVFYTAEGRLLGsHLGELSRGSLARYL 262
Cdd:pfam13098  78 IVFFDGKGELLR-LPGYVPAEEFLALL 103
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 147-262 3.52e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 42.97  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 147 ESVQLADFRGRPLVINLWASWCPPCRReM-------PVLQQAQAENPDVVFLFAnqgESAETVRHFlQGENLrldnllfd 219
Cdd:COG2143   31 EDLALAKAEGKPILLFFESDWCPYCKK-LhkevfsdPEVAAYLKENFVVVQLDA---EGDKEVTDF-DGETL-------- 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489180310 220 NGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRGSLARYL 262
Cdd:COG2143   98 TEKELARKYGVRGTPTLVFFDAEGKEIARIPGYLKPETFLALL 140
Thioredoxin_9 pfam14595
Thioredoxin;
147-252 6.03e-05

Thioredoxin;


Pssm-ID: 434059 [Multi-domain]  Cd Length: 129  Bit Score: 41.87  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  147 ESVQLADFRGRPL-VINLWASWCPPCRREMPVLQQAQAENPDVvflfanqgesaeTVRHFLQGENL-RLDNLLFDnggql 224
Cdd:pfam14595  31 ELIEKIKSIEKPLrILVITEDWCGDAAQNVPVLAKIAELNPNI------------ELRILLRDENLeLMDQYLTG----- 93

                          90       100
                  ....*....|....*....|....*...
gi 489180310  225 gqqvGSVALPTTVFYTAEGRLLGsHLGE 252
Cdd:pfam14595  94 ----GGRAIPTFIFLDEDGEELG-VWGP 116
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 140-192 1.39e-04

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 41.42  E-value: 1.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489180310 140 SLRNAAGESVQLADFRGRPLVINLWASWCP-PCRREMPVLQQAQAE-----NPDVVFLF 192
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPdVCPTTLANLAQVQEAlgedgGDDVQVLF 62
PRK10996 PRK10996
thioredoxin 2; Provisional
 158-238 1.65e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 40.82  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 158 PLVINLWASWCPPCRREMPVLQQ-AQAENPDVVFLFAN-----------QGESAETVRHFLQGEnlRLDNLlfdNGgqlg 225
Cdd:PRK10996  54 PVVIDFWAPWCGPCRNFAPIFEDvAAERSGKVRFVKVNteaerelsarfRIRSIPTIMIFKNGQ--VVDML---NG---- 124

                         90
                 ....*....|...
gi 489180310 226 qqvgsvALPTTVF 238
Cdd:PRK10996 125 ------AVPKAPF 131
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 137-192 3.09e-04

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: 39.89  E-value: 3.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489180310 137 PELSLRNAAGESVQLADFRGRPLVINLWASWCP-PCRREMPVLQQAQAE-----NPDVVFLF 192
Cdd:cd02968    3 PDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPdVCPTTLANLAQALKQlgadgGDDVQVVF 64
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 136-256 4.24e-04

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: 41.40  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 136 LPELSLRNAAGESVQLAdfRGRPLVINLWASWCPPCRREMPVL----QQAQAENPDVVFL----FANQGESAEtVRHFLQ 207
Cdd:PRK14018  38 LSTLKTADNRPASVYLK--KDKPTLIKFWASWCPLCLSELGETekwaQDAKFSSANLITVaspgFLHEKKDGD-FQKWYA 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489180310 208 GENLRLDNLLFDNGGQLGQQVGSVALPTTVFYTAEGRLLGSHLGELSRG 256
Cdd:PRK14018 115 GLDYPKLPVLTDNGGTLAQSLNISVYPSWAIIGKDGDVQRIVKGSISEA 163
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 83-246 6.25e-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: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  83 LAWPGLLAAVLGALFWAWRRP--ALRRSLGVGASLGLAFWLLG-SLGLGIYERGTRLPELSLRNAAGESVQLADFR---- 155
Cdd:COG4232  231 LLWALLLLALALWLLGALRLPhdSSGRRLSVRKGLGLLLLLAGlALLLGALSGADPLQPLAAGAAAAAAAAGLAWQadle 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 156 ---------GRPLVINLWASWCPPCRrempvlqqaqaENPDVVFlfanqgeSAETVRHFLQGE--NLRLDnllFDNG--- 221
Cdd:COG4232  311 aalaearaeGKPVFVDFTADWCVTCK-----------ENERTVF-------SDPEVQAALADDvvLLKAD---VTDNdpe 369

                        170       180
                 ....*....|....*....|....*.
gi 489180310 222 -GQLGQQVGSVALPTTVFYTAEGRLL 246
Cdd:COG4232  370 iTALLKRFGRFGVPTYVFYDPDGEEL 395
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 147-200 6.70e-04

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 37.73  E-value: 6.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310  147 ESVQLADFRGRPLVINLWASWCPPCRR------EMPVLQQAQAENpdVVFLFANQGESAE 200
Cdd:pfam13899   8 EALAAAAERGKPVLVDFGADWCFTCQVlerdflSHEEVKAALAKN--FVLLRLDWTSRDA 65
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 157-194 9.25e-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: 37.64  E-value: 9.25e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489180310 157 RPLVINLWASWCPPCRREMPVLQQ-AQAENPDVVFLFAN 194
Cdd:cd02984   15 KLLVLHFWAPWAEPCKQMNQVFEElAKEAFPSVLFLSIE 53
PTZ00051 PTZ00051
thioredoxin; Provisional
 159-200 9.42e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 37.93  E-value: 9.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489180310 159 LVINLWASWCPPCRREMPVLQQAQAENPDVVFLFANQGESAE 200
Cdd:PTZ00051  21 VIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSE 62
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 141-199 1.14e-03

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


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 38.04  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489180310 141 LRNAaGESVQLADFRGRPLVINLWASWCPPCRREMPVLQQA------QAENPDVVFLFANQGESA 199
Cdd:cd03009    4 LRND-GGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFyeklkeSGKNFEIVFISWDRDEES 67
trxA PRK09381
thioredoxin TrxA;
160-262 2.11e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 36.97  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 160 VINLWASWCPPCRREMPVLQQAQAEnpdvvflfanqgesaetvrhfLQGEnLRLDNLLFDNGGQLGQQVGSVALPTTVFY 239
Cdd:PRK09381  25 LVDFWAEWCGPCKMIAPILDEIADE---------------------YQGK-LTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82

                         90       100
                 ....*....|....*....|...
gi 489180310 240 TaEGRLLGSHLGELSRGSLARYL 262
Cdd:PRK09381  83 K-NGEVAATKVGALSKGQLKEFL 104
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 155-262 2.49e-03

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 36.81  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 155 RGRPLVINLWASWCPPCrREM-------PVLQQAQAENpdVVFLFANQGESAETVRHFLqgenlrldnllfdnggqlgQQ 227
Cdd:cd02953   10 QGKPVFVDFTADWCVTC-KVNekvvfsdPEVQAALKKD--VVLLRADWTKNDPEITALL-------------------KR 67

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489180310 228 VGSVALPTTVFYTAEGRLLGSHL-GELSRGSLARYL 262
Cdd:cd02953   68 FGVFGPPTYLFYGPGGEPEPLRLpGFLTADEFLEAL 103
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 137-192 2.51e-03

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: 37.16  E-value: 2.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489180310  137 PELSLRNAAGESVQLADFRGRPLVINLWASWCPP-CRREMPVLQQAQ----AENPDVVFLF 192
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDvCPTTLPNMAQVLdalgEEGIDVQPVF 62
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 134-161 3.58e-03

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: 36.76  E-value: 3.58e-03
                         10        20
                 ....*....|....*....|....*...
gi 489180310 134 TRLPELSLRNAAGESVQLADFRGRPLVI 161
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVL 28
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 157-189 4.42e-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: 36.06  E-value: 4.42e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 489180310  157 RPLVINLWASWCPPCRREMPVLQQAQAENPDVV 189
Cdd:pfam00085  19 KPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNV 51
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 158-246 7.91e-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: 34.94  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489180310 158 PLVINLWASWCPPCRREMPVLQQAQAENPDvVFLFAnqgesaetvrhflqgenlRLDnllFDNGGQLGQQVGSVALPTTV 237
Cdd:cd02956   14 PVVVDFWAPRSPPSKELLPLLERLAEEYQG-QFVLA------------------KVN---CDAQPQIAQQFGVQALPTVY 71


                 ....*....
gi 489180310 238 FYtAEGRLL 246
Cdd:cd02956   72 LF-AAGQPV 79
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 155-181 8.13e-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: 8.13e-03
                         10        20
                 ....*....|....*....|....*..
gi 489180310 155 RGRPLVINLWASWCPPCRREMPVLQQA 181
Cdd:cd03004   18 RKEPWLVDFYAPWCGPCQALLPELRKA 44
 
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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