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Conserved domains on  [gi|655198358|ref|WP_028622761|]
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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, ...
 133-264 2.77e-43

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 144.06  E-value: 2.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 133 GTRLPEMGLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQDNTEVNFLFVNQGEGERLIADFLDAEGLS 212
Cdd:COG0526    5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAVKAFLKELGLP 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655198358 213 LeNVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGELSHASLARALEQ 264
Cdd:COG0526   85 Y-PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEK 135
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 133-264 2.77e-43

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 144.06  E-value: 2.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 133 GTRLPEMGLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQDNTEVNFLFVNQGEGERLIADFLDAEGLS 212
Cdd:COG0526    5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAVKAFLKELGLP 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655198358 213 LeNVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGELSHASLARALEQ 264
Cdd:COG0526   85 Y-PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEK 135
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 141-251 2.62e-34

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: 120.03  E-value: 2.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 141 LRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQD--NTEVNFLFVNQGEGER-LIADFLDAEGLSLeNVL 217
Cdd:cd02966    4 LPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEykDDGVEVVGVNVDDDDPaAVKAFLKKYGITF-PVL 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 655198358 218 LDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLG 251
Cdd:cd02966   83 LDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
129-266 3.03e-19

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 82.36  E-value: 3.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 129 AFEQGTRLPEMGLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAK--AQQDNTEVNFLFVNQGEGERLIADFL 206
Cdd:PRK03147  34 KVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNElyPKYKEKGVEIIAVNVDETELAVKNFV 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 207 DAEGLSLEnVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGELSHASLARALEQFK 266
Cdd:PRK03147 114 NRYGLTFP-VAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLEEYLEKIK 172
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 133-243 2.98e-15

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: 70.33  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  133 GTRLPEMGLRDIQGKPAALQDYVGKPLVVNLWAT-WCPPCRREMPVLAKAQQDNTE--VNFLFVNQGEGERLIAdFLDAE 209
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKlgVEVLGVSVDSPESHKA-FAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 655198358  210 GLSLeNVLLDTGGRLGQHVG------SAALPTTLFYDAEG 243
Cdd:pfam00578  81 GLPF-PLLSDPDGEVARAYGvlneeeGGALRATFVIDPDG 119
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 137-253 1.96e-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: 58.25  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  137 PEMGLRDIQGKPAALQDYV---GKPLVVNLWATWCPPCRREMPVLAKAQQDNteVNFLFVNQGEGERLIADFLDAEGLSL 213
Cdd:TIGR00385  41 PAFRLASLDEPGQFYTADVltqGKPVLLNVWASWCPPCRAEHPYLNELAKQG--LPIVGVDYKDDRQNAIKFLKELGNPY 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 655198358  214 ENVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGEL 253
Cdd:TIGR00385 119 QLSLFDPDGMLGLDLGVYGAPETFLVDGNGVIRYRHAGPL 158
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 133-264 2.77e-43

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 144.06  E-value: 2.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 133 GTRLPEMGLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQDNTEVNFLFVNQGEGERLIADFLDAEGLS 212
Cdd:COG0526    5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPEAVKAFLKELGLP 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655198358 213 LeNVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGELSHASLARALEQ 264
Cdd:COG0526   85 Y-PVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEK 135
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 141-251 2.62e-34

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: 120.03  E-value: 2.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 141 LRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQD--NTEVNFLFVNQGEGER-LIADFLDAEGLSLeNVL 217
Cdd:cd02966    4 LPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEykDDGVEVVGVNVDDDDPaAVKAFLKKYGITF-PVL 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 655198358 218 LDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLG 251
Cdd:cd02966   83 LDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
137-271 5.07e-23

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 91.47  E-value: 5.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 137 PEMGLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQDNTE--VNFLFVNQGEGERLiADFLDAEGLSLE 214
Cdd:COG1225    2 PDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDkgVEVLGVSSDSDEAH-KKFAEKYGLPFP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 655198358 215 nVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGELSHASLARALEQFKVKNQP 271
Cdd:COG1225   81 -LLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEALLAELK 136
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
129-266 3.03e-19

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 82.36  E-value: 3.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 129 AFEQGTRLPEMGLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAK--AQQDNTEVNFLFVNQGEGERLIADFL 206
Cdd:PRK03147  34 KVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNElyPKYKEKGVEIIAVNVDETELAVKNFV 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 207 DAEGLSLEnVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGELSHASLARALEQFK 266
Cdd:PRK03147 114 NRYGLTFP-VAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLEEYLEKIK 172
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 133-243 2.98e-15

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: 70.33  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  133 GTRLPEMGLRDIQGKPAALQDYVGKPLVVNLWAT-WCPPCRREMPVLAKAQQDNTE--VNFLFVNQGEGERLIAdFLDAE 209
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKlgVEVLGVSVDSPESHKA-FAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 655198358  210 GLSLeNVLLDTGGRLGQHVG------SAALPTTLFYDAEG 243
Cdd:pfam00578  81 GLPF-PLLSDPDGEVARAYGvlneeeGGALRATFVIDPDG 119
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 133-252 8.85e-13

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 64.31  E-value: 8.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  133 GTRLPEMGLRDI--QGKPAALQDYVGKPLVVNLWAT-WCPPCRREMPVLAKAQQDNTE--VNFLFVNQGEGERLIADFLD 207
Cdd:pfam08534   3 GDKAPDFTLPDAatDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEkgVDVVAVNSDNDAFFVKRFWG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 655198358  208 AEGLSLEnVLLDTGGRLGQHVGSA---------ALPTTLFYDAEGRQVGSHLGE 252
Cdd:pfam08534  83 KEGLPFP-FLSDGNAAFTKALGLPieedasaglRSPRYAVIDEDGKVVYLFVGP 135
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 156-263 9.27e-13

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: 62.58  E-value: 9.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 156 GKPLVVNLWATWCPPCRREMPVLAKAQQDNTEVNFLFVNQGEGERLIADFldaeglsleNVLldtggrlgqhvgsaALPT 235
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEY---------GVR--------------SIPT 66

                         90       100
                 ....*....|....*....|....*...
gi 655198358 236 TLFYDaEGRQVGSHLGELSHASLARALE 263
Cdd:cd02947   67 FLFFK-NGKEVDRVVGADPKEELEEFLE 93
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 136-253 4.09e-12

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: 61.82  E-value: 4.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 136 LPEMGLRDIQGKPAAL--QDYVGKPLVVNLWATWCPPCRREMPVL-AKAQQDNTEVnfLFVNQGEGERLIADFLDAEGLS 212
Cdd:cd03010    3 APAFSLPALPGPDKTLtsADLKGKPYLLNVWASWCAPCREEHPVLmALARQGRVPI--YGINYKDNPENALAWLARHGNP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 655198358 213 LENVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGEL 253
Cdd:cd03010   81 YAAVGFDPDGRVGIDLGVYGVPETFLIDGDGIIRYKHVGPL 121
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 137-253 1.96e-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: 58.25  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  137 PEMGLRDIQGKPAALQDYV---GKPLVVNLWATWCPPCRREMPVLAKAQQDNteVNFLFVNQGEGERLIADFLDAEGLSL 213
Cdd:TIGR00385  41 PAFRLASLDEPGQFYTADVltqGKPVLLNVWASWCPPCRAEHPYLNELAKQG--LPIVGVDYKDDRQNAIKFLKELGNPY 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 655198358  214 ENVLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGEL 253
Cdd:TIGR00385 119 QLSLFDPDGMLGLDLGVYGAPETFLVDGNGVIRYRHAGPL 158
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 137-243 5.75e-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: 55.77  E-value: 5.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 137 PEMGLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQDnteVNFLFVNQGEGE-RLIADFLDAEGLSLEn 215
Cdd:cd03011    1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAAD---YPVVSVALRSGDdGAVARFMQKKGYGFP- 76

                         90       100
                 ....*....|....*....|....*...
gi 655198358 216 VLLDTGGRLGQHVGSAALPTTLFYDAEG 243
Cdd:cd03011   77 VINDPDGVISARWGVSVTPAIVIVDPGG 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 156-265 4.84e-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: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 156 GKPLVVNLWATWCPPCRREMPVLAK-AQQDNTEVNFLFVNqgegerliadfldaeglslenvlLDTGGRLGQHVGSAALP 234
Cdd:COG3118   18 DKPVLVDFWAPWCGPCKMLAPVLEElAAEYGGKVKFVKVD-----------------------VDENPELAAQFGVRSIP 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 655198358 235 TTLFYdAEGRQVGSHLGELSHASLARALEQF 265
Cdd:COG3118   75 TLLLF-KDGQPVDRFVGALPKEQLREFLDKV 104
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 156-244 4.12e-08

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


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 50.00  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  156 GKPLVVNLWATWCPPCRREMPVLAKAQQDNTE---VNFLFVNQGEGERLIADFLDAEGLSLENVLLDTGGR--LGQHVGS 230
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKkknVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERneLKRKYGV 80

                          90
                  ....*....|....
gi 655198358  231 AALPTTLFYDAEGR 244
Cdd:pfam13905  81 NAIPTLVLLDPNGE 94
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 156-254 4.31e-08

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 51.92  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 156 GKPLVVNLWATWCPPCRREMPVLAKAQQDNTEVnfLFVNQGEGERLIADFLDAEGLSLENVLLDTGGRLGQHVGSAALPT 235
Cdd:PRK15412  68 GKPVLLNVWATWCPTCRAEHQYLNQLSAQGIRV--VGMNYKDDRQKAISWLKELGNPYALSLFDGDGMLGLDLGVYGAPE 145

                         90
                 ....*....|....*....
gi 655198358 236 TLFYDAEGRQVGSHLGELS 254
Cdd:PRK15412 146 TFLIDGNGIIRYRHAGDLN 164
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 127-256 3.94e-07

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: 50.64  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 127 LHAFEQgtrlpemgLRDIQGKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQDNTEVNFLFVNQGE----GERLI 202
Cdd:PRK14018  35 PHTLST--------LKTADNRPASVYLKKDKPTLIKFWASWCPLCLSELGETEKWAQDAKFSSANLITVASpgflHEKKD 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 655198358 203 ADFLD-AEGLSLEN--VLLDTGGRLGQHVGSAALPTTLFYDAEGRQVGSHLGELSHA 256
Cdd:PRK14018 107 GDFQKwYAGLDYPKlpVLTDNGGTLAQSLNISVYPSWAIIGKDGDVQRIVKGSISEA 163
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 157-266 1.23e-06

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 45.74  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  157 KPLVVNLWATWCPPCRREMPVLAK-AQQDNTEVNFLFVNQGEGERLIADFldaeglslenvlldtggrlgqhvGSAALPT 235
Cdd:TIGR01068  15 KPVLVDFWAPWCGPCKMIAPILEElAKEYEGKVKFVKLNVDENPDIAAKY-----------------------GIRSIPT 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 655198358  236 TLFYDaEGRQVGSHLGELSHASLARALEQFK 266
Cdd:TIGR01068  72 LLLFK-NGKEVDRSVGALPKAALKQLINKNL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 151-203 1.03e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 44.29  E-value: 1.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 655198358 151 LQDyvGKPLVVNLWATWCPPCRREMPVLAK-AQQDNTEVNFLFVNQgEGERLIA 203
Cdd:PRK10996  49 LQD--DLPVVIDFWAPWCGPCRNFAPIFEDvAAERSGKVRFVKVNT-EAERELS 99
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 156-266 1.76e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 43.74  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 156 GKPLVVNLWATWCPPCRR---EmpVLAKAQ-QDNTEVNFLFVNqgegerliadfLDAEGlSLENVLLDtGGRLGQHVGSA 231
Cdd:COG2143   40 GKPILLFFESDWCPYCKKlhkE--VFSDPEvAAYLKENFVVVQ-----------LDAEG-DKEVTDFD-GETLTEKELAR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 655198358 232 AL-----PTTLFYDAEGRQVGSHLGELSHASLARALEQFK 266
Cdd:COG2143  105 KYgvrgtPTLVFFDAEGKEIARIPGYLKPETFLALLKYVA 144
Thioredoxin_9 pfam14595
Thioredoxin;
165-252 2.27e-05

Thioredoxin;


Pssm-ID: 434059 [Multi-domain]  Cd Length: 129  Bit Score: 43.02  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  165 ATWCPPCRREMPVLAKAQQDNTEVNFLFVNQGEGERLIADFLdaeglslenvlldTGGRlgqhvgsAALPTTLFYDAEGR 244
Cdd:pfam14595  50 EDWCGDAAQNVPVLAKIAELNPNIELRILLRDENLELMDQYL-------------TGGG-------RAIPTFIFLDEDGE 109


                  ....*...
gi 655198358  245 QVGsHLGE 252
Cdd:pfam14595 110 ELG-VWGP 116
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 157-194 9.39e-05

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: 40.68  E-value: 9.39e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 655198358  157 KPLVVNLWATWCPPCRREMPVLAKAQQDnTEVNFLFVN 194
Cdd:pfam00085  19 KPVLVDFYAPWCGPCKMLAPEYEELAQE-YKGNVVFAK 55
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 146-246 1.06e-04

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: 41.12  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 146 GKPAALQDYVGKPLVVNLWATWCPPCRREMPVLAKAQQD--NTEVNF--LFVNQGEGERLIADFL-----------DAEG 210
Cdd:cd03009    8 GGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKlkESGKNFeiVFISWDRDEESFNDYFskmpwlavpfsDRER 87

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 655198358 211 LSlenvlldtggRLGQHVGSAALPTTLFYDAEGRQV 246
Cdd:cd03009   88 RS----------RLNRTFKIEGIPTLIILDADGEVV 113
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 156-263 1.26e-04

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: 41.17  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 156 GKPLVVNLWATWCPPCRREMPVLAKAQQDNTE-VNFLFVN--QGEGERLIADFlDAEGlslenvlldtggrlgqhvgsaa 232
Cdd:cd02950   20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDqVNFVMLNvdNPKWLPEIDRY-RVDG---------------------- 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 655198358 233 LPTTLFYDAEGRQVGSHLGELSHASLARALE 263
Cdd:cd02950   77 IPHFVFLDREGNEEGQSIGLQPKQVLAQNLD 107
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
156-245 1.28e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 40.49  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358  156 GKPLVVNLWATWCPPCRREMPVLAKaqqdNTEVNFLFvnQGEGERLIADFLDAEGLSLENVLLDTGGRLGQHVGSAALPT 235
Cdd:pfam13098   4 GKPVLVVFTDPDCPYCKKLKKELLE----DPDVTVYL--GPNFVFIAVNIWCAKEVAKAFTDILENKELGRKYGVRGTPT 77

                          90
                  ....*....|
gi 655198358  236 TLFYDAEGRQ 245
Cdd:pfam13098  78 IVFFDGKGEL 87
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 151-194 4.57e-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: 38.41  E-value: 4.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 655198358 151 LQDYVGKPLVVNLWATWCPPCRREMPVLAK-AQQDNTEVNFLFVN 194
Cdd:cd02984    9 LKSDASKLLVLHFWAPWAEPCKQMNQVFEElAKEAFPSVLFLSIE 53
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 141-193 9.26e-04

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 38.73  E-value: 9.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 655198358 141 LRDIQGKPAALQDYVGKPLVVNLWATWCP-PCRREMPVLAKAQQ-----DNTEVNFLFV 193
Cdd:COG1999    5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPdVCPTTLANLAQVQEalgedGGDDVQVLFI 63
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 160-229 3.06e-03

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: 35.37  E-value: 3.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655198358 160 VVNLWATWCPPCRREMPVLAKAQQDNTEVNFLFVNQGEGERLiADFLDAEGLSLENVLLDTGGRLGQHVG 229
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPAL-EKELKRYGVGGVPTLVVFGPGIGVKYG 69
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 141-193 5.14e-03

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: 36.43  E-value: 5.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 655198358 141 LRDIQGKPAALQDYVGKPLVVNLWATWCP-PCRREMPVLAKAQQ-----DNTEVNFLFV 193
Cdd:cd02968    7 LTDQDGRPVTLSDLKGKPVLVYFGYTHCPdVCPTTLANLAQALKqlgadGGDDVQVVFI 65
 
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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