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Conserved domains on  [gi|1596252168|gb|TDP13471|]
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peroxiredoxin [Kinneretia asaccharophila]

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, ...
 30-168 2.43e-39

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 130.19  E-value: 2.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  30 RDKAPAISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKarGFDTLAVAMSyDPPAYVANFAASR 109
Cdd:COG0526     5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVD-ENPEAVKAFLKEL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1596252168 110 KLPFGVAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKRYVGTPDFAALHGLVEKLLAE 168
Cdd:COG0526    82 GLPYPVLLDPDGELAKAYG-VRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 30-168 2.43e-39

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 130.19  E-value: 2.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  30 RDKAPAISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKarGFDTLAVAMSyDPPAYVANFAASR 109
Cdd:COG0526     5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVD-ENPEAVKAFLKEL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1596252168 110 KLPFGVAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKRYVGTPDFAALHGLVEKLLAE 168
Cdd:COG0526    82 GLPYPVLLDPDGELAKAYG-VRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 35-151 2.76e-39

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: 129.28  E-value: 2.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  35 AISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAVAMSYDPPAYVANFAASRKLPFG 114
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGITFP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1596252168 115 VAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKRYVG 151
Cdd:cd02966    81 VLLDPDGELAKAYG-VRGLPTTFLIDRDGRIRARHVG 116
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 31-165 6.89e-27

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 98.98  E-value: 6.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVL--LDGSKFDSAQWQGKVMLVNFWAT-SCTTCVAEMPEIVATHEKFKARGFDTLAVAMSYDPPaYVANFAA 107
Cdd:pfam08534   4 DKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAF-FVKRFWG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1596252168 108 SRKLPFGVAIDNTGAIAQKFGDI--------QLTPTTLLINKRGEIVKRYVGTPDFAALHGLVEKL 165
Cdd:pfam08534  83 KEGLPFPFLSDGNAAFTKALGLPieedasagLRSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
31-165 5.87e-23

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 89.29  E-value: 5.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAVAMSyDPPAYVANFAASRK 110
Cdd:PRK03147   39 KEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVD-ETELAVKNFVNRYG 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1596252168 111 LPFGVAIDNTGAIAQKFGDIQLtPTTLLINKRGEIVKRYVGTPDFAALHGLVEKL 165
Cdd:PRK03147  118 LTFPVAIDKGRQVIDAYGVGPL-PTTFLIDKDGKVVKVITGEMTEEQLEEYLEKI 171
 
Name Accession Description Interval E-value
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 30-168 2.43e-39

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 130.19  E-value: 2.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  30 RDKAPAISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKarGFDTLAVAMSyDPPAYVANFAASR 109
Cdd:COG0526     5 GKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVDVD-ENPEAVKAFLKEL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1596252168 110 KLPFGVAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKRYVGTPDFAALHGLVEKLLAE 168
Cdd:COG0526    82 GLPYPVLLDPDGELAKAYG-VRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 35-151 2.76e-39

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: 129.28  E-value: 2.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  35 AISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAVAMSYDPPAYVANFAASRKLPFG 114
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAVKAFLKKYGITFP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1596252168 115 VAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKRYVG 151
Cdd:cd02966    81 VLLDPDGELAKAYG-VRGLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
33-169 1.11e-37

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 126.13  E-value: 1.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  33 APAISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAVamSYDPPAYVANFAASRKLP 112
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV--SSDSDEAHKKFAEKYGLP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1596252168 113 FGVAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKRYVGTPDFAA-LHGLVEKLLAEA 169
Cdd:COG1225    79 FPLLSDPDGEVAKAYG-VRGTPTTFLIDPDGKIRYVWVGPVDPRPhLEEVLEALLAEL 135
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 31-165 6.89e-27

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 98.98  E-value: 6.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVL--LDGSKFDSAQWQGKVMLVNFWAT-SCTTCVAEMPEIVATHEKFKARGFDTLAVAMSYDPPaYVANFAA 107
Cdd:pfam08534   4 DKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAF-FVKRFWG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1596252168 108 SRKLPFGVAIDNTGAIAQKFGDI--------QLTPTTLLINKRGEIVKRYVGTPDFAALHGLVEKL 165
Cdd:pfam08534  83 KEGLPFPFLSDGNAAFTKALGLPieedasagLRSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
31-165 5.87e-23

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 89.29  E-value: 5.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAVAMSyDPPAYVANFAASRK 110
Cdd:PRK03147   39 KEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVD-ETELAVKNFVNRYG 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1596252168 111 LPFGVAIDNTGAIAQKFGDIQLtPTTLLINKRGEIVKRYVGTPDFAALHGLVEKL 165
Cdd:PRK03147  118 LTFPVAIDKGRQVIDAYGVGPL-PTTFLIDKDGKVVKVITGEMTEEQLEEYLEKI 171
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 31-148 4.36e-20

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: 80.73  E-value: 4.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVLLDGSKFDSAQWQGKVMLVNFWAT-SCTTCVAEMPEIVATHEKFKARGFDTLAVamSYDPPAYVANFAASR 109
Cdd:pfam00578   3 DKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGV--SVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1596252168 110 KLPFGVAIDNTGAIAQKFG----DIQLT-PTTLLINKRGEIVKR 148
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGvlneEEGGAlRATFVIDPDGKVRYI 124
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 33-155 8.41e-20

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: 79.93  E-value: 8.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  33 APAISYVLLDGSK--FDSAQWQGKVMLVNFWATSCTTCVAEMPEIVAthekFKARGFDTLaVAMSY-DPPAYVANFAASR 109
Cdd:cd03010     3 APAFSLPALPGPDktLTSADLKGKPYLLNVWASWCAPCREEHPVLMA----LARQGRVPI-YGINYkDNPENALAWLARH 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1596252168 110 KLPF-GVAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKRYVG--TPDF 155
Cdd:cd03010    78 GNPYaAVGFDPDGRVGIDLG-VYGVPETFLIDGDGIIRYKHVGplTPEV 125
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 34-152 1.06e-16

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: 71.95  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  34 PAISYVLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVAThekfkARGFDTLAVAMSYDPPAYVANFAASRKLPF 113
Cdd:cd03011     1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQL-----AADYPVVSVALRSGDDGAVARFMQKKGYGF 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1596252168 114 GVAIDNTGAIAQKFGdIQLTPTTLLInKRGEIVKRYVGT 152
Cdd:cd03011    76 PVINDPDGVISARWG-VSVTPAIVIV-DPGGIVFVTTGV 112
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 42-168 2.20e-09

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 53.37  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  42 DGSKFDSAQWQGKVMLVNFWATSCTT-CVAEMPEIVATHEKFKARGFDTLAVAM-SYDP----PAYVANFAASRKLP--F 113
Cdd:COG1999     9 DGKPVTLADLRGKPVLVFFGYTSCPDvCPTTLANLAQVQEALGEDGGDDVQVLFiSVDPerdtPEVLKAYAEAFGAPrwI 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1596252168 114 GVaidnTG------AIAQKFG-----------DIQLTPTTLLINKRGEIVKRYVGTPDFAALHGLVEKLLAE 168
Cdd:COG1999    89 GL----TGdpeeiaALAKAFGvyyekvpdgdyTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 49-151 2.26e-09

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


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 52.69  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  49 AQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKArgfDTLAVAMSYDP-------PAYVANFAASRKLPFGVAIDNTG 121
Cdd:cd03012    19 AQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKD---DGLVVIGVHSPefaferdLANVKSAVLRYGITYPVANDNDY 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 1596252168 122 AIAQKFGdIQLTPTTLLINKRGEIVKRYVG 151
Cdd:cd03012    96 ATWRAYG-NQYWPALYLIDPTGNVRHVHFG 124
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 53-145 2.45e-09

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: 51.92  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  53 GKVMLVNFWATSCTTCVAEMPEIVATHEKFKAR-GFDTLAVAMSYDPPAYVANFAASRK----LPFGVaiDNTGAIAQKF 127
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKkNVEIVFVSLDRDLEEFKDYLKKMPKdwlsVPFDD--DERNELKRKY 78

                          90
                  ....*....|....*...
gi 1596252168 128 gDIQLTPTTLLINKRGEI 145
Cdd:pfam13905  79 -GVNAIPTLVLLDPNGEV 95
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 31-148 5.02e-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: 52.63  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVLLDGSKFDSAQWQ-GKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAV------AMSYDPPAYVA 103
Cdd:cd02969     2 SPAPDFSLPDTDGKTYSLADFAdGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAInsndieAYPEDSPENMK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1596252168 104 NFAASRKLPFGVAIDNTGAIAQKFGdIQLTPTTLLINKRGEIVKR 148
Cdd:cd02969    82 AKAKEHGYPFPYLLDETQEVAKAYG-AACTPDFFLFDPDGKLVYR 125
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 31-151 8.69e-08

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: 48.70  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVLLDGSKFDSAQWQGKVMLVNFW---ATS-CTTcvaEMPEIVATHEKFKARGFDTLAVamSYDPPAYVANFA 106
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYpkdDTPgCTK---EACDFRDLYEEFKALGAVVIGV--SPDSVESHAKFA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1596252168 107 ASRKLPFGVAIDNTGAIAQKFGDIQLTP--------TTLLINKRGEIVKRYVG 151
Cdd:cd03017    76 EKYGLPFPLLSDPDGKLAKAYGVWGEKKkkymgierSTFLIDPDGKIVKVWRK 128
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 46-163 1.91e-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: 46.78  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  46 FDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKargfdtlavamsydppayvanfaasrKLPFG-VAIDNTGAIA 124
Cdd:cd02947     3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYP--------------------------KVKFVkVDVDENPELA 56

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1596252168 125 QKFGdIQLTPTTLLInKRGEIVKRYVGTPDFAALHGLVE 163
Cdd:cd02947    57 EEYG-VRSIPTFLFF-KNGKEVDRVVGADPKEELEEFLE 93
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 42-149 3.60e-05

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


Pssm-ID: 239266  Cd Length: 142  Bit Score: 41.43  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  42 DGSKFDSAQWQGKVMLVNFWATSCTT-CVAEMPEIVATHEKFKARGFDTL-AVAMSYDP----P----AYVANF------ 105
Cdd:cd02968    11 DGRPVTLSDLKGKPVLVYFGYTHCPDvCPTTLANLAQALKQLGADGGDDVqVVFISVDPerdtPevlkAYAKAFgpgwig 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1596252168 106 -----AASRKL--PFGVAIDNTGAIAQKfGDIQLTPTTLLINKRGEIVKRY 149
Cdd:cd02968    91 ltgtpEEIEALakAFGVYYEKVPEDDGD-YLVDHSAAIYLVDPDGKLVRYY 140
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 31-128 6.61e-05

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: 40.72  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  31 DKAPAISYVLLDGSKF--DSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAVamSYDPPAYVANFAAS 108
Cdd:cd03018     5 DKAPDFELPDQNGQEVrlSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGI--SVDSPFSLRAWAEE 82

                          90       100
                  ....*....|....*....|..
gi 1596252168 109 RKLPFGVAID--NTGAIAQKFG 128
Cdd:cd03018    83 NGLTFPLLSDfwPHGEVAKAYG 104
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 39-158 1.39e-04

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 39.13  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  39 VLLDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEivathekfkargFDTLAVAMSYDPPAYVAnfaasrklpfgvAID 118
Cdd:cd02961     1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPE------------YEKLAKELKGDGKVVVA------------KVD 56

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1596252168 119 NT--GAIAQKFGdIQLTPTTLLINKRGEIVKRYVGTPDFAAL 158
Cdd:cd02961    57 CTanNDLCSEYG-VRGYPTIKLFPNGSKEPVKYEGPRTLESL 97
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 52-151 1.61e-04

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 40.36  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  52 QGKVMLVNFWATSCTTCVAEMPEIvathEKFKARGFDTlaVAMSY-DPPAYVANFAASRKLPFGVAI-DNTGAIAQKFGd 129
Cdd:PRK15412   67 QGKPVLLNVWATWCPTCRAEHQYL----NQLSAQGIRV--VGMNYkDDRQKAISWLKELGNPYALSLfDGDGMLGLDLG- 139

                          90       100
                  ....*....|....*....|..
gi 1596252168 130 IQLTPTTLLINKRGEIVKRYVG 151
Cdd:PRK15412  140 VYGAPETFLIDGNGIIRYRHAG 161
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 32-128 1.68e-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: 39.65  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  32 KAPAISYVLLDGSKFD-SAQW-QGKVMLV---NFWatsCTTCVAEMPEIVATHEKFKARGFDTLAVamSYDPPAYVANFA 106
Cdd:cd02970     1 TAPDFELPDAGGETVTlSALLgEGPVVVVfyrGFG---CPFCREYLRALSKLLPELDALGVELVAV--GPESPEKLEAFD 75

                          90       100
                  ....*....|....*....|..
gi 1596252168 107 ASRKLPFGVAIDNTGAIAQKFG 128
Cdd:cd02970    76 KGKFLPFPVYADPDRKLYRALG 97
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 42-125 2.17e-04

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: 39.09  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  42 DGSKFDSAQWQGKVMLVNFWATSCTT-CVAEMPEIVATHEKFKARGFDTLAVAMSYDP----PAYVANFAASrklpFGVA 116
Cdd:pfam02630  10 DGKAVTEADFEGRPSLVFFGFTHCPDvCPTTLPNMAQVLDALGEEGIDVQPVFITVDPerdtPEVLAEYLEA----FGPR 85

                          90
                  ....*....|
gi 1596252168 117 IDN-TGAIAQ 125
Cdd:pfam02630  86 IIGlTGSPEQ 95
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 42-148 2.91e-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: 38.81  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  42 DGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARG--FDTLAVAMSYDPPAYVANFAasrKLPFgVAI-- 117
Cdd:cd03009     7 DGGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGknFEIVFISWDRDEESFNDYFS---KMPW-LAVpf 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1596252168 118 -DNTG--AIAQKFGdIQLTPTTLLINKRGEIVKR 148
Cdd:cd03009    83 sDRERrsRLNRTFK-IEGIPTLIILDADGEVVTT 115
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 41-115 1.88e-03

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 37.14  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  41 LDGSKFDSAQWQGKVMLVNFWATSCTTCVAEMPEIVATHEKFKARGFDTLAVAMS------YDPPAYVANFAASRKLPFG 114
Cdd:PTZ00056   27 LEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSqflnqeFPNTKDIRKFNDKNKIKYN 106


                  .
gi 1596252168 115 V 115
Cdd:PTZ00056  107 F 107
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
52-151 2.32e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 35.86  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252168  52 QGKVMLVNFWATSCTTCV---AEMPEIVATHEKFKaRGFDTLAVAMSYDPPAYVANFAASRKLPFGvaidntgaiaQKFG 128
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKklkKELLEDPDVTVYLG-PNFVFIAVNIWCAKEVAKAFTDILENKELG----------RKYG 71

                          90       100
                  ....*....|....*....|...
gi 1596252168 129 dIQLTPTTLLINKRGEIVkRYVG 151
Cdd:pfam13098  72 -VRGTPTIVFFDGKGELL-RLPG 92
 
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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