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Conserved domains on  [gi|1084773552|gb|OGQ13166|]
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hypothetical protein A3D30_09680 [Deltaproteobacteria bacterium RIFCSPHIGHO2_02_FULL_43_33]

Protein Classification

TlpA disulfide reductase family protein( domain architecture ID 10121831)

TlpA disulfide reductase family protein 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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 11-126 1.44e-48

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: 152.01  E-value: 1.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  11 DFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDSEEDV-QKVGKFIKKKGYTFL 89
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDpAAVKAFLKKYGITFP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1084773552  90 VLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEG 126
Cdd:cd02966    81 VLLDPDGELAKA-YGVRGLPTTFLIDRDGRIRARHVG 116
 
Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 11-126 1.44e-48

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: 152.01  E-value: 1.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  11 DFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDSEEDV-QKVGKFIKKKGYTFL 89
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDpAAVKAFLKKYGITFP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1084773552  90 VLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEG 126
Cdd:cd02966    81 VLLDPDGELAKA-YGVRGLPTTFLIDRDGRIRARHVG 116
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 8-145 2.00e-48

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 152.54  E-value: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFkdKGLVIAAVDSEEDVQKVGKFIKKKGYT 87
Cdd:COG0526     7 PAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDENPEAVKAFLKELGLP 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1084773552  88 FLVLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEGARawDSEEIFRLIEEILKK 145
Cdd:COG0526    85 YPVLLDPDGELAKA-YGVRGIPTTVLIDKDGKIVARHVGPL--SPEELEEALEKLLAK 139
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
8-127 4.04e-40

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 132.43  E-value: 4.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDSEEDVQKVGKFIKKKGYT 87
Cdd:PRK03147   40 EAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRYGLT 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1084773552  88 FLVLLDSDGAVsSDTYRAIGFPTTYLIDRRGMVIGKAEGA 127
Cdd:PRK03147  120 FPVAIDKGRQV-IDAYGVGPLPTTFLIDKDGKVVKVITGE 158
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-120 8.40e-34

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: 114.63  E-value: 8.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFWAT-WCPPCVVEMPSIEALHKRFKDKGLVIAAV--DSEEDVQkvgKFIKKK 84
Cdd:pfam00578   4 KAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVsvDSPESHK---AFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1084773552  85 GYTFLVLLDSDGAVSSDtYRA------IGFPTTYLIDRRGMV 120
Cdd:pfam00578  81 GLPFPLLSDPDGEVARA-YGVlneeegGALRATFVIDPDGKV 121
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 8-126 4.78e-19

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: 78.28  E-value: 4.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKK--VSLKDF-KGKVVFLNFWATWCPPCVVEMPSIEALHKRfkdkGLVIAAVDSEEDVQKVGKFIKKK 84
Cdd:TIGR00385  39 PVPAFRLASLDEPGqfYTADVLtQGKPVLLNVWASWCPPCRAEHPYLNELAKQ----GLPIVGVDYKDDRQNAIKFLKEL 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1084773552  85 GYTF-LVLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEG 126
Cdd:TIGR00385 115 GNPYqLSLFDPDGMLGLD-LGVYGAPETFLVDGNGVIRYRHAG 156
 
Name Accession Description Interval E-value
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 11-126 1.44e-48

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: 152.01  E-value: 1.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  11 DFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDSEEDV-QKVGKFIKKKGYTFL 89
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDpAAVKAFLKKYGITFP 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1084773552  90 VLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEG 126
Cdd:cd02966    81 VLLDPDGELAKA-YGVRGLPTTFLIDRDGRIRARHVG 116
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 8-145 2.00e-48

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 152.54  E-value: 2.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFkdKGLVIAAVDSEEDVQKVGKFIKKKGYT 87
Cdd:COG0526     7 PAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDENPEAVKAFLKELGLP 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1084773552  88 FLVLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEGARawDSEEIFRLIEEILKK 145
Cdd:COG0526    85 YPVLLDPDGELAKA-YGVRGIPTTVLIDKDGKIVARHVGPL--SPEELEEALEKLLAK 139
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
9-145 3.26e-48

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 151.56  E-value: 3.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   9 APDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVdSEEDVQKVGKFIKKKGYTF 88
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGV-SSDSDEAHKKFAEKYGLPF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1084773552  89 LVLLDSDGAVsSDTYRAIGFPTTYLIDRRGMVIGKAEGARAWDsEEIFRLIEEILKK 145
Cdd:COG1225    80 PLLSDPDGEV-AKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPR-PHLEEVLEALLAE 134
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
8-127 4.04e-40

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 132.43  E-value: 4.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDSEEDVQKVGKFIKKKGYT 87
Cdd:PRK03147   40 EAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRYGLT 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1084773552  88 FLVLLDSDGAVsSDTYRAIGFPTTYLIDRRGMVIGKAEGA 127
Cdd:PRK03147  120 FPVAIDKGRQV-IDAYGVGPLPTTFLIDKDGKVVKVITGE 158
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 8-120 8.40e-34

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: 114.63  E-value: 8.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFWAT-WCPPCVVEMPSIEALHKRFKDKGLVIAAV--DSEEDVQkvgKFIKKK 84
Cdd:pfam00578   4 KAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVsvDSPESHK---AFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1084773552  85 GYTFLVLLDSDGAVSSDtYRA------IGFPTTYLIDRRGMV 120
Cdd:pfam00578  81 GLPFPLLSDPDGEVARA-YGVlneeegGALRATFVIDPDGKV 121
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 8-121 4.67e-29

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 103.60  E-value: 4.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNT--LDGKKVSLKDFKGKVVFLNFWAT-WCPPCVVEMPSIEALHKRFKDKGLVIAAVDSEEDVQKVGKFIKKK 84
Cdd:pfam08534   5 KAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVKRFWGKE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1084773552  85 GYTFLVLLDSDGAVS--------SDTYRAIGFPTTYLIDRRGMVI 121
Cdd:pfam08534  85 GLPFPFLSDGNAAFTkalglpieEDASAGLRSPRYAVIDEDGKVV 129
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 8-134 1.24e-25

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: 94.18  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDG--KKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRfkdKGLVIAAVDSEEDVQKVGKFIKKKG 85
Cdd:cd03010     2 PAPAFSLPALPGpdKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQ---GRVPIYGINYKDNPENALAWLARHG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084773552  86 --YTfLVLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEGARAWDSEE 134
Cdd:cd03010    79 npYA-AVGFDPDGRVGID-LGVYGVPETFLIDGDGIIRYKHVGPLTPEVWE 127
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 10-120 1.75e-20

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: 80.81  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  10 PDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKdkglVIA-AVDSEEDvQKVGKFIKKKGYTF 88
Cdd:cd03011     1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYP----VVSvALRSGDD-GAVARFMQKKGYGF 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1084773552  89 LVLLDSDGAVSSDtYRAIGFPTTYLIDRRGMV 120
Cdd:cd03011    76 PVINDPDGVISAR-WGVSVTPAIVIVDPGGIV 106
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 10-126 4.75e-20

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: 79.66  E-value: 4.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  10 PDFT-----LNTldGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDS-----EEDVQKVGK 79
Cdd:cd03012     1 PEFEgilqwLNT--DKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSpefafERDLANVKS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1084773552  80 FIKKKGYTFLVLLDSDgavsSDTYRAIG---FPTTYLIDRRGMVIGKAEG 126
Cdd:cd03012    79 AVLRYGITYPVANDND----YATWRAYGnqyWPALYLIDPTGNVRHVHFG 124
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 8-126 4.78e-19

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: 78.28  E-value: 4.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKK--VSLKDF-KGKVVFLNFWATWCPPCVVEMPSIEALHKRfkdkGLVIAAVDSEEDVQKVGKFIKKK 84
Cdd:TIGR00385  39 PVPAFRLASLDEPGqfYTADVLtQGKPVLLNVWASWCPPCRAEHPYLNELAKQ----GLPIVGVDYKDDRQNAIKFLKEL 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1084773552  85 GYTF-LVLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEG 126
Cdd:TIGR00385 115 GNPYqLSLFDPDGMLGLD-LGVYGAPETFLVDGNGVIRYRHAG 156
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 8-133 1.81e-16

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 71.95  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLD--GKKVSLKDF-KGKVVFLNFWATWCPPCVVEMPSIEALHKrfkdKGLVIAAVDSEEDVQKVGKFIKKK 84
Cdd:PRK15412   44 PVPKFRLESLEnpGQFYQADVLtQGKPVLLNVWATWCPTCRAEHQYLNQLSA----QGIRVVGMNYKDDRQKAISWLKEL 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1084773552  85 GYTF-LVLLDSDGAVSSDtYRAIGFPTTYLIDRRGMVIGKAEG---ARAWDSE 133
Cdd:PRK15412  120 GNPYaLSLFDGDGMLGLD-LGVYGAPETFLIDGNGIIRYRHAGdlnPRVWESE 171
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 8-118 1.31e-15

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: 68.73  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFW---ATwcPPCVVEMPSIEALHKRFKDKGLVIAAVdSEEDVQKVGKFIKKK 84
Cdd:cd03017     2 KAPDFTLPDQDGETVSLSDLRGKPVVLYFYpkdDT--PGCTKEACDFRDLYEEFKALGAVVIGV-SPDSVESHAKFAEKY 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1084773552  85 GYTFLVLLDSDGAVsSDTYRAIGFP---------TTYLIDRRG 118
Cdd:cd03017    79 GLPFPLLSDPDGKL-AKAYGVWGEKkkkymgierSTFLIDPDG 120
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 8-121 3.19e-15

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: 68.42  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGK----VVFLNfwaTWCPpcVVEM--PSIEALHKRFKDKGLVIAAVDS-------EEDV 74
Cdd:cd02969     3 PAPDFSLPDTDGKTYSLADFADGkalvVMFIC---NHCP--YVKAieDRLNRLAKEYGAKGVAVVAINSndieaypEDSP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1084773552  75 QKVGKFIKKKGYTFLVLLDSDGAVsSDTYRAIGFPTTYLIDRRGMVI 121
Cdd:cd02969    78 ENMKAKAKEHGYPFPYLLDETQEV-AKAYGAACTPDFFLFDPDGKLV 123
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 8-121 1.63e-13

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 63.34  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFW-ATWCPPCVVEMPSIEALHKRFKDKGLVIAAVdSEEDVQKVGKFIKK-KG 85
Cdd:cd02971     1 KAPDFTLPATDGGEVSLSDFKGKWVVLFFYpKDFTPVCTTELCAFRDLAEEFAKGGAEVLGV-SVDSPFSHKAWAEKeGG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1084773552  86 YTFLVLLDSDGAVSsdtyRAIGFP------------TTYLIDRRGMVI 121
Cdd:cd02971    80 LNFPLLSDPDGEFA----KAYGVLieksaggglaarATFIIDPDGKIR 123
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 29-118 2.96e-13

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: 61.17  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  29 GKVVFLNFWATWCPPCVVEMPSIEALHKRFKD-KGLVIAAVDSEEDVQKVGKFIKKKGYTFLVLLDSDGAVS--SDTYRA 105
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKkKNVEIVFVSLDRDLEEFKDYLKKMPKDWLSVPFDDDERNelKRKYGV 80

                          90
                  ....*....|...
gi 1084773552 106 IGFPTTYLIDRRG 118
Cdd:pfam13905  81 NAIPTLVLLDPNG 93
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 8-120 1.78e-10

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: 55.36  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKG--KVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAA--VDSeedVQKVGKFIKK 83
Cdd:cd03018     6 KAPDFELPDQNGQEVRLSEFRGrkPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGisVDS---PFSLRAWAEE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1084773552  84 KGYTFLVLLDS--DGAVsSDTY-----------RAigfptTYLIDRRGMV 120
Cdd:cd03018    83 NGLTFPLLSDFwpHGEV-AKAYgvfdedlgvaeRA-----VFVIDRDGII 126
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 8-108 9.03e-10

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: 53.52  E-value: 9.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGK----VVFLNFWatWCPPCVVEMPSIEALHKRFKDKGL-VIAAVDSEEDVQKvgKFIK 82
Cdd:cd02970     1 TAPDFELPDAGGETVTLSALLGEgpvvVVFYRGF--GCPFCREYLRALSKLLPELDALGVeLVAVGPESPEKLE--AFDK 76

                          90       100
                  ....*....|....*....|....*.
gi 1084773552  83 KKGYTFLVLLDSDGAVssdtYRAIGF 108
Cdd:cd02970    77 GKFLPFPVYADPDRKL----YRALGL 98
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 8-99 1.36e-09

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 53.02  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFW---ATwcPPCVVEMPSIEALHKRFKDKGLVIAAVdSEEDVQKVGKFIKKK 84
Cdd:PRK09437    9 IAPKFSLPDQDGEQVSLTDFQGQRVLVYFYpkaMT--PGCTVQACGLRDNMDELKKAGVVVLGI-STDKPEKLSRFAEKE 85

                          90
                  ....*....|....*
gi 1084773552  85 GYTFLVLLDSDGAVS 99
Cdd:PRK09437   86 LLNFTLLSDEDHQVA 100
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 11-91 1.93e-09

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


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 52.52  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  11 DFTLNTLDGKKVSLKDFKGKVVFL-NFwATWCPpcvvEMPSI---EALHKRFKDKGLVIAAV----------DSEEDVQk 76
Cdd:cd00340     4 DFSVKDIDGEPVSLSKYKGKVLLIvNV-ASKCG----FTPQYeglEALYEKYKDRGLVVLGFpcnqfggqepGSNEEIK- 77

                          90
                  ....*....|....*.
gi 1084773552  77 vgKFIKKK-GYTFLVL 91
Cdd:cd00340    78 --EFCETNyGVTFPMF 91
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 29-143 5.50e-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: 50.59  E-value: 5.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  29 GKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKgLVIAAVDSEEDVQkvgkfikkkgytflvlldsdgavSSDTYRAIGF 108
Cdd:COG3118    18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDVDENPE-----------------------LAAQFGVRSI 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1084773552 109 PTTYLIdRRGMVIGKAEGARawDSEEIFRLIEEIL 143
Cdd:COG3118    74 PTLLLF-KDGQPVDRFVGAL--PKEQLREFLDKVL 105
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 25-128 1.07e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 52.55  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   25 KDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAV-----DSEEDVQKVGKFIKKKGYTFLVLLDSDGAVs 99
Cdd:PLN02919   416 RDLKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQPFTVVGVhsakfDNEKDLEAIRNAVLRYNISHPVVNDGDMYL- 494

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1084773552  100 sdtYRAIG---FPTTYLIDRRGMVIGK--AEGAR 128
Cdd:PLN02919   495 ---WRELGvssWPTFAVVSPNGKLIAQlsGEGHR 525
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 8-122 1.49e-08

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: 50.29  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCP-PCVVEMPSIEALHKRFKDKG-----LVIAAVDSEED-VQKVGKF 80
Cdd:cd02968     1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPdVCPTTLANLAQALKQLGADGgddvqVVFISVDPERDtPEVLKAY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084773552  81 IKKKGYTFLVLLDSDGAVSSDTyRAIGFP-----------------TTYLIDRRGMVIG 122
Cdd:cd02968    81 AKAFGPGWIGLTGTPEEIEALA-KAFGVYyekvpeddgdylvdhsaAIYLVDPDGKLVR 138
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 13-144 1.47e-07

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 47.59  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  13 TLNTLDGKKVSLKDFKGKVVFLNFWATWCP-PCVVEMPSIEALHKRFKDKG---LVIAAV------DSEEDVQKVGKFIK 82
Cdd:COG1999     4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPdVCPTTLANLAQVQEALGEDGgddVQVLFIsvdperDTPEVLKAYAEAFG 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084773552  83 KKGYTFLV--------LLDSDGA----VSSDTYRAIGFPTTYLIDRRGMVIGKAEGARawDSEEIFRLIEEILK 144
Cdd:COG1999    84 APRWIGLTgdpeeiaaLAKAFGVyyekVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGE--DPEELAADLKALLE 155
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 28-72 1.87e-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: 46.01  E-value: 1.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1084773552  28 KGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDkgLVIAAVDSEE 72
Cdd:cd02947     9 SAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDVDE 51
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 18-98 4.84e-07

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: 45.74  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  18 DGKKVSLKDFKGKVVFLNFWATWCPPC------VVEmpSIEALHKRFKDKGLVIAAVDSEED------------------ 73
Cdd:cd03009     7 DGGKVPVSSLEGKTVGLYFSASWCPPCraftpkLVE--FYEKLKESGKNFEIVFISWDRDEEsfndyfskmpwlavpfsd 84

                          90       100
                  ....*....|....*....|....*...
gi 1084773552  74 ---VQKVGKFIKKKGYTFLVLLDSDGAV 98
Cdd:cd03009    85 rerRSRLNRTFKIEGIPTLIILDADGEV 112
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 3-121 3.98e-06

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: 44.87  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   3 EKKPIPAPDFTLNTLDGKKVSLKdfKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDS-----EEDVQKV 77
Cdd:PRK14018   32 ATVPHTLSTLKTADNRPASVYLK--KDKPTLIKFWASWCPLCLSELGETEKWAQDAKFSSANLITVASpgflhEKKDGDF 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1084773552  78 GKFIKKKGYTFL-VLLDSDGAVSSdTYRAIGFPTTYLIDRRGMVI 121
Cdd:PRK14018  110 QKWYAGLDYPKLpVLTDNGGTLAQ-SLNISVYPSWAIIGKDGDVQ 153
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
8-35 4.71e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 43.92  E-value: 4.71e-06
                          10        20
                  ....*....|....*....|....*...
gi 1084773552   8 PAPDFTLNTLDGKKVSLKDFKGKVVFLN 35
Cdd:COG2077    23 KAPDFTLVDTDLSDVTLSDFAGKRKVLN 50
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 27-69 1.10e-05

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: 41.83  E-value: 1.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1084773552  27 FKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKG-LVIAAVD 69
Cdd:cd02961    13 KDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVD 56
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 10-83 1.38e-05

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: 42.17  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  10 PDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPP-CVVEMPSIEALHKRFKDKGLVIAA----VDSEED-VQKVGKFIKK 83
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDvCPTTLPNMAQVLDALGEEGIDVQPvfitVDPERDtPEVLAEYLEA 81
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 11-118 3.78e-05

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 41.76  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  11 DFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAVDSEE-------DVQKVGKFIKK 83
Cdd:PTZ00056   21 DYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTSQflnqefpNTKDIRKFNDK 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1084773552  84 KG--YTFLVLLDSDGAVSSDTYRAIGFPTTYLIDRRG 118
Cdd:PTZ00056  101 NKikYNFFEPIEVNGENTHELFKFLKANCDSMHDENG 137
PLN02412 PLN02412
probable glutathione peroxidase
 1-124 6.42e-05

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 40.74  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   1 MGEKKPIPAPDFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAAV----------DS 70
Cdd:PLN02412    1 MAEESPKSIYDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFpcnqflgqepGS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1084773552  71 EEDVQKVGKFIKKKGYTFLVLLDSDGAVSSDTYRaigfpttYLIDRRGMVIGKA 124
Cdd:PLN02412   81 NEEIQQTVCTRFKAEFPIFDKVDVNGKNTAPLYK-------YLKAEKGGLFGDA 127
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
28-139 8.45e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 39.33  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  28 KGKVVFLNFWATWCPPCVV---EMPSIEALHKRFKDKGLVIA-AVDSEEDVQKVGKFIKKKgytflvlldsdgAVSSDTY 103
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKKlkkELLEDPDVTVYLGPNFVFIAvNIWCAKEVAKAFTDILEN------------KELGRKY 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1084773552 104 RAIGFPTTYLIDRRGmVIGKAEGarAWDSEEIFRLI 139
Cdd:pfam13098  71 GVRGTPTIVFFDGKG-ELLRLPG--YVPAEEFLALL 103
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
8-140 1.01e-04

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 40.44  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552   8 PAPDFTLNTLDG---KKVSLKDFKGKVVFLNFW-ATWCPPCVVEmpsIEALHKR---FKDKGL-VIAA-VDS-------- 70
Cdd:COG0450     8 KAPDFTAEATHGgefKKISLSDYKGKWVVLFFHpADFTFVCPTE---LGAFAKRyeeFKKLGVeVIGLsVDSvfshkawh 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  71 --EEDVQKVGKFikkkgyTFLVLLDSDGAVSSD----------TYRAigfptTYLIDRRGMV---------IGKaegara 129
Cdd:COG0450    85 etIKEKGGIVKI------KFPIIADPTGKIARAygmlhpedgvAVRG-----VFIIDPDGKIraievyplsVGR------ 147

                         170
                  ....*....|.
gi 1084773552 130 wDSEEIFRLIE 140
Cdd:COG0450   148 -NVDEILRVVD 157
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 8-71 2.10e-04

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 39.41  E-value: 2.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084773552   8 PAPDFTLNTLDG----KKVSLKDFKGKVVFLNFWatwcpP------CVVEMPSIEALHKRFKDKGLVIAAV--DSE 71
Cdd:cd03015     4 KAPDFKATAVVPngefKEISLSDYKGKWVVLFFY-----PldftfvCPTEIIAFSDRYEEFKKLNAEVLGVstDSH 74
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 14-86 2.11e-04

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


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 38.39  E-value: 2.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084773552  14 LNTLDGKKVSLKDfkGKVVFLNFWATWCPPCVVEMPSIEALHKRFK-DKGLVIAAVDSEEDVQKVGKFIKKKGY 86
Cdd:cd02998     5 LTDSNFDKVVGDD--KKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAnEDDVVIAKVDADEANKDLAKKYGVSGF 76
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 30-73 2.35e-04

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: 38.04  E-value: 2.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1084773552  30 KVVFLNFWATWCPPCVVEMPSIEALHKRFKDKgLVIAAVDSEED 73
Cdd:TIGR01068  15 KPVLVDFWAPWCGPCKMIAPILEELAKEYEGK-VKFVKLNVDEN 57
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 14-62 2.68e-04

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 38.36  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1084773552  14 LNTLDG-KKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKG 62
Cdd:cd02964     1 LFLLDGeGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEG 50
tpx PRK00522
thiol peroxidase;
9-35 2.87e-04

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 38.73  E-value: 2.87e-04
                          10        20
                  ....*....|....*....|....*..
gi 1084773552   9 APDFTLNTLDGKKVSLKDFKGKVVFLN 35
Cdd:PRK00522   24 APDFTLVANDLSDVSLADFAGKRKVLN 50
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 9-35 3.45e-04

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


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 38.33  E-value: 3.45e-04
                          10        20
                  ....*....|....*....|....*..
gi 1084773552   9 APDFTLNTLDGKKVSLKDFKGKVVFLN 35
Cdd:cd03014     6 APDFTLVTSDLSEVSLADFAGKVKVIS 32
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 25-69 1.09e-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: 36.50  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1084773552  25 KDFKGKVV------FLNFWATWCPPCVVEMPSIEALHKRFkdKGLV-IAAVD 69
Cdd:cd03004     9 EDFPELVLnrkepwLVDFYAPWCGPCQALLPELRKAARAL--KGKVkVGSVD 58
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 33-93 1.93e-03

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 36.91  E-value: 1.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084773552  33 FLNFWATWCPPCVVEMPSIEALHKRFkdKGLV-IAAVDSEEDVQkVGKFIKKKGYTFLVLLD 93
Cdd:PTZ00443   56 FVKFYAPWCSHCRKMAPAWERLAKAL--KGQVnVADLDATRALN-LAKRFAIKGYPTLLLFD 114
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 11-67 2.26e-03

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 36.80  E-value: 2.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1084773552  11 DFTLNTLDGKKVSLKDFKGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKGLVIAA 67
Cdd:PLN02399   81 DFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILA 137
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 30-69 4.06e-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: 34.90  E-value: 4.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1084773552  30 KVVFLNFWATWCPPCVVEMPSIEALHKRFKDKgLVIAAVD 69
Cdd:pfam00085  19 KPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN-VVFAKVD 57
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 28-44 4.25e-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: 34.89  E-value: 4.25e-03
                          10
                  ....*....|....*..
gi 1084773552  28 KGKVVFLNFWATWCPPC 44
Cdd:cd02953    10 QGKPVFVDFTADWCVTC 26
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 28-128 5.07e-03

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 35.27  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084773552  28 KGKVVFLNFWATWCPPCvvempsiEALHKRFKDKGLVIAAVDSEEDVQKVGKFIKKKgytflvLLDSDGAVSS-----DT 102
Cdd:COG2143    39 EGKPILLFFESDWCPYC-------KKLHKEVFSDPEVAAYLKENFVVVQLDAEGDKE------VTDFDGETLTekelaRK 105

                          90       100
                  ....*....|....*....|....*.
gi 1084773552 103 YRAIGFPTTYLIDRRGMVIGKAEGAR 128
Cdd:COG2143   106 YGVRGTPTLVFFDAEGKEIARIPGYL 131
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 32-72 5.24e-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: 34.17  E-value: 5.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1084773552  32 VFLNFWATWCPPCVVEMPSIEALHKRFKDKgLVIAAVDSEE 72
Cdd:cd02956    15 VVVDFWAPRSPPSKELLPLLERLAEEYQGQ-FVLAKVNCDA 54
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 29-72 7.68e-03

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 35.42  E-value: 7.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1084773552  29 GKVVFLNFWATWCPPCVVEMPSIEALHKRFKD--KGLVIAAVDSEE 72
Cdd:TIGR01130 364 TKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDaeSDVVIAKMDATA 409
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 28-89 7.97e-03

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 33.83  E-value: 7.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084773552  28 KGKVVFLNFWATWCPPCVVEMPSIEALHKRFKDKG-LVIAAVDSEEDVQK-VGKFIKKKGY-TFL 89
Cdd:cd02997    16 KEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGkGVLAAVDCTKPEHDaLKEEYNVKGFpTFK 80
 
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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