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Conserved domains on  [gi|753283820|gb|AJG53097|]
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thiol-disulfide oxidoreductase resA [Bacillus cereus 03BB102]

Protein Classification

thiol-disulfide oxidoreductase ResA( domain architecture ID 10792244)

thiol-disulfide oxidoreductase ResA is required in disulfide reduction during c-type cytochrome synthesis

Gene Symbol:  resA
Gene Ontology:  GO:0016209|GO:0015036|GO:0017004
PubMed:  18422485|16971393

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-173 1.95e-113

thiol-disulfide oxidoreductase ResA;


:

Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 319.26  E-value: 1.95e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   1 MKKNRLLFRVIILLILSGAVGFTLYQGFFADKEKMQIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEM 80
Cdd:PRK03147   1 MKKNRLLFRTIILLILLAAVGYTIYSNFFADKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  81 PYMNELYPKYKEKGVEIIALDADETDIAVKNFVNQYGLKFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGEQT 160
Cdd:PRK03147  81 PYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMT 160

                        170
                 ....*....|...
gi 753283820 161 KEQLEGYLKKITP 173
Cdd:PRK03147 161 EEQLEEYLEKIKP 173
 
Name Accession Description Interval E-value
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-173 1.95e-113

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 319.26  E-value: 1.95e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   1 MKKNRLLFRVIILLILSGAVGFTLYQGFFADKEKMQIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEM 80
Cdd:PRK03147   1 MKKNRLLFRTIILLILLAAVGYTIYSNFFADKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  81 PYMNELYPKYKEKGVEIIALDADETDIAVKNFVNQYGLKFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGEQT 160
Cdd:PRK03147  81 PYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMT 160

                        170
                 ....*....|...
gi 753283820 161 KEQLEGYLKKITP 173
Cdd:PRK03147 161 EEQLEEYLEKIKP 173
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-171 1.77e-50

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 158.70  E-value: 1.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  36 QIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYkeKGVEIIALDADETDIAVKNFVNQ 115
Cdd:COG0526    3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDENPEAVKAFLKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 753283820 116 YGLKFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGEQTKEQLEGYLKKI 171
Cdd:COG0526   81 LGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKL 136
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 43-157 4.79e-47

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: 149.31  E-value: 4.79e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  43 NFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADETDIA-VKNFVNQYGLKFP 121
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAaVKAFLKKYGITFP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 753283820 122 VAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIG 157
Cdd:cd02966   81 VLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 37-154 1.80e-41

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: 135.43  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   37 IGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGT-WCKPCEKEMPYMNELYPKYKEKGVEIIALDADeTDIAVKNFVNQ 115
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVD-SPESHKAFAEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 753283820  116 YGLKFPVAIDKGQKIIGTYGV------GPLPTSFLIDKDGKVVEQ 154
Cdd:pfam00578  80 YGLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDGKVRYI 124
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 6-169 3.42e-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: 79.82  E-value: 3.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820    6 LLFRVIILLILSGAVGFTLYQGFFADK----EKMQIGKEAPNFVVTDLEGK-KIELKDL--KGKGVFLNFWGTWCKPCEK 78
Cdd:TIGR00385   1 LLLPLIIFLGIAAALLWQLARNAEGDDpkalPSALIGKPVPAFRLASLDEPgQFYTADVltQGKPVLLNVWASWCPPCRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   79 EMPYMNELypkyKEKGVEIIALD-ADETDIAVKnFVNQYGLKFPVAIDKGQKIIG-TYGVGPLPTSFLIDKDGKVVEQII 156
Cdd:TIGR00385  81 EHPYLNEL----AKQGLPIVGVDyKDDRQNAIK-FLKELGNPYQLSLFDPDGMLGlDLGVYGAPETFLVDGNGVIRYRHA 155

                         170
                  ....*....|...
gi 753283820  157 GEQTKEQLEGYLK 169
Cdd:TIGR00385 156 GPLNPEVWTEEFL 168
 
Name Accession Description Interval E-value
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-173 1.95e-113

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 319.26  E-value: 1.95e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   1 MKKNRLLFRVIILLILSGAVGFTLYQGFFADKEKMQIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEM 80
Cdd:PRK03147   1 MKKNRLLFRTIILLILLAAVGYTIYSNFFADKEKVQVGKEAPNFVLTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  81 PYMNELYPKYKEKGVEIIALDADETDIAVKNFVNQYGLKFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGEQT 160
Cdd:PRK03147  81 PYMNELYPKYKEKGVEIIAVNVDETELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMT 160

                        170
                 ....*....|...
gi 753283820 161 KEQLEGYLKKITP 173
Cdd:PRK03147 161 EEQLEEYLEKIKP 173
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 36-171 1.77e-50

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 158.70  E-value: 1.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  36 QIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYkeKGVEIIALDADETDIAVKNFVNQ 115
Cdd:COG0526    3 AVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDENPEAVKAFLKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 753283820 116 YGLKFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGEQTKEQLEGYLKKI 171
Cdd:COG0526   81 LGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKL 136
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
41-171 3.60e-47

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 150.02  E-value: 3.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  41 APNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADETDiAVKNFVNQYGLKF 120
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDE-AHKKFAEKYGLPF 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 753283820 121 PVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIG-----EQTKEQLEGYLKKI 171
Cdd:COG1225   80 PLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGpvdprPHLEEVLEALLAEL 135
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 43-157 4.79e-47

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: 149.31  E-value: 4.79e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  43 NFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADETDIA-VKNFVNQYGLKFP 121
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAaVKAFLKKYGITFP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 753283820 122 VAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIG 157
Cdd:cd02966   81 VLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 37-154 1.80e-41

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: 135.43  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   37 IGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGT-WCKPCEKEMPYMNELYPKYKEKGVEIIALDADeTDIAVKNFVNQ 115
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSVD-SPESHKAFAEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 753283820  116 YGLKFPVAIDKGQKIIGTYGV------GPLPTSFLIDKDGKVVEQ 154
Cdd:pfam00578  80 YGLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDGKVRYI 124
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 36-171 6.60e-32

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 111.69  E-value: 6.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   36 QIGKEAPNFVVTD--LEGKKIELKDLKGKGVFLNFW-GTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADETDIAVKNF 112
Cdd:pfam08534   1 KAGDKAPDFTLPDaaTDGNTVSLSDFKGKKVVLNFWpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 753283820  113 VNQYGLKFPVAIDKGQKIIGTYGVG---------PLPTSFLIDKDGKVVEQIIGEQTKEQLEGYLKKI 171
Cdd:pfam08534  81 WGKEGLPFPFLSDGNAAFTKALGLPieedasaglRSPRYAVIDEDGKVVYLFVGPEPGVDVSDAEAVL 148
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 39-165 6.25e-26

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: 95.72  E-value: 6.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  39 KEAPNFVVTDLEGKKIEL--KDLKGKGVFLNFWGTWCKPCEKEMPYMNELypkYKEKGVEIIALDADETDIAVKNFVNQY 116
Cdd:cd03010    1 KPAPAFSLPALPGPDKTLtsADLKGKPYLLNVWASWCAPCREEHPVLMAL---ARQGRVPIYGINYKDNPENALAWLARH 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 753283820 117 GLKF-PVAIDKGQKI---IGTYGVgplPTSFLIDKDGKVVEQIIGEQTKEQLE 165
Cdd:cd03010   78 GNPYaAVGFDPDGRVgidLGVYGV---PETFLIDGDGIIRYKHVGPLTPEVWE 127
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 6-169 3.42e-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: 79.82  E-value: 3.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820    6 LLFRVIILLILSGAVGFTLYQGFFADK----EKMQIGKEAPNFVVTDLEGK-KIELKDL--KGKGVFLNFWGTWCKPCEK 78
Cdd:TIGR00385   1 LLLPLIIFLGIAAALLWQLARNAEGDDpkalPSALIGKPVPAFRLASLDEPgQFYTADVltQGKPVLLNVWASWCPPCRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   79 EMPYMNELypkyKEKGVEIIALD-ADETDIAVKnFVNQYGLKFPVAIDKGQKIIG-TYGVGPLPTSFLIDKDGKVVEQII 156
Cdd:TIGR00385  81 EHPYLNEL----AKQGLPIVGVDyKDDRQNAIK-FLKELGNPYQLSLFDPDGMLGlDLGVYGAPETFLVDGNGVIRYRHA 155

                         170
                  ....*....|...
gi 753283820  157 GEQTKEQLEGYLK 169
Cdd:TIGR00385 156 GPLNPEVWTEEFL 168
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 52-158 4.83e-19

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: 78.12  E-value: 4.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  52 KKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALD----ADETDIA-VKNFVNQYGLKFPVAIDK 126
Cdd:cd03012   14 KPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHspefAFERDLAnVKSAVLRYGITYPVANDN 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 753283820 127 GQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGE 158
Cdd:cd03012   94 DYATWRAYGNQYWPALYLIDPTGNVRHVHFGE 125
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 41-162 2.11e-18

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: 76.82  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  41 APNFVVTDLEGKKIELKDLKGKGVFLNFW-GTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADETDiAVKNFVNQYG-L 118
Cdd:cd02971    2 APDFTLPATDGGEVSLSDFKGKWVVLFFYpKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPF-SHKAWAEKEGgL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 753283820 119 KFPVAIDKGQKIIGTYGV---------GPLPTSFLIDKDGKVVEQIIGEQTKE 162
Cdd:cd02971   81 NFPLLSDPDGEFAKAYGVlieksagggLAARATFIIDPDGKIRYVEVEPLPTG 133
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 61-151 2.29e-18

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: 75.42  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   61 GKGVFLNFWGTWCKPCEKEMPYMNELYPKYKE-KGVEIIALDADETDIAVKNFVNQYGLKF---PVAIDKGQKIIGTYGV 136
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKkKNVEIVFVSLDRDLEEFKDYLKKMPKDWlsvPFDDDERNELKRKYGV 80

                          90
                  ....*....|....*
gi 753283820  137 GPLPTSFLIDKDGKV 151
Cdd:pfam13905  81 NAIPTLVLLDPNGEV 95
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 39-153 4.01e-18

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: 76.05  E-value: 4.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  39 KEAPNFVVTDLEGKKIELKDLKGKGVFLNFW---GTwckP-CEKEMPYMNELYPKYKEKGVEIIALDADETDiAVKNFVN 114
Cdd:cd03017    1 DKAPDFTLPDQDGETVSLSDLRGKPVVLYFYpkdDT---PgCTKEACDFRDLYEEFKALGAVVIGVSPDSVE-SHAKFAE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 753283820 115 QYGLKFPVAIDKGQKIIGTYGV---------GPLPTSFLIDKDGKVVE 153
Cdd:cd03017   77 KYGLPFPLLSDPDGKLAKAYGVwgekkkkymGIERSTFLIDPDGKIVK 124
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 1-171 5.20e-17

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 74.26  E-value: 5.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   1 MKKNRLLFRVIILLILSGAVGFTLYQGFFADK----EKMQIGKEAPNFVVTDLE--GKKIELKDL-KGKGVFLNFWGTWC 73
Cdd:PRK15412   1 MKRNVLLIPLIIFLAIAAALLWQLARNAEGDDptnlESALIGKPVPKFRLESLEnpGQFYQADVLtQGKPVLLNVWATWC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  74 KPCEKEMPYMNELypkyKEKGVEIIALDADETDIAVKNFVNQYGLKFPVAIDKGQKIIG-TYGVGPLPTSFLIDKDGKVV 152
Cdd:PRK15412  81 PTCRAEHQYLNQL----SAQGIRVVGMNYKDDRQKAISWLKELGNPYALSLFDGDGMLGlDLGVYGAPETFLIDGNGIIR 156

                        170
                 ....*....|....*....
gi 753283820 153 EQIIGEQTKEQLEGYLKKI 171
Cdd:PRK15412 157 YRHAGDLNPRVWESEIKPL 175
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 35-161 5.80e-15

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: 68.07  E-value: 5.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  35 MQIGKEAPNFVVTDLEGKKIELKDLKGKG-VFLNFW-GTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADETdIAVKNF 112
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKpVVLVFFpLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSP-FSLRAW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 753283820 113 VNQYGLKFPVAIDKGQK--IIGTYGV-GPLPT-----SFLIDKDGKVVEQIIGEQTK 161
Cdd:cd03018   80 AEENGLTFPLLSDFWPHgeVAKAYGVfDEDLGvaeraVFVIDRDGIIRYAWVSDDGE 136
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 42-151 7.36e-15

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: 66.94  E-value: 7.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  42 PNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVeiiALDADeTDIAVKNFVNQYGLKFP 121
Cdd:cd03011    1 PLFTATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYPVVSV---ALRSG-DDGAVARFMQKKGYGFP 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 753283820 122 VAIDKGQKIIGTYGVGPLPTSFLIDKDGKV 151
Cdd:cd03011   77 VINDPDGVISARWGVSVTPAIVIVDPGGIV 106
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
35-156 1.19e-12

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


Pssm-ID: 440219  Cd Length: 196  Bit Score: 62.79  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  35 MQIGKEAPNFVVT---DLEGKKIELKDLKGKGVFLNFWgtwckP------CEKEMPYMNELYPKYKEKGVEIIALDAD-- 103
Cdd:COG0450    3 PLIGDKAPDFTAEathGGEFKKISLSDYKGKWVVLFFH-----PadftfvCPTELGAFAKRYEEFKKLGVEVIGLSVDsv 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 753283820 104 ETDIA-VKNFVNQYGL---KFPVAIDKGQKIIGTYGVgpLP--------TSFLIDKDGKVVEQII 156
Cdd:COG0450   78 FSHKAwHETIKEKGGIvkiKFPIIADPTGKIARAYGM--LHpedgvavrGVFIIDPDGKIRAIEV 140
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 37-156 2.36e-12

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: 61.75  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  37 IGKEAPNF----VVTDLEGKKIELKDLKGKGVFLNFWgtwckP------CEKEMPYMNELYPKYKEKGVEIIALDAD--- 103
Cdd:cd03015    1 VGKKAPDFkataVVPNGEFKEISLSDYKGKWVVLFFY-----PldftfvCPTEIIAFSDRYEEFKKLNAEVLGVSTDshf 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 753283820 104 ------ETDIAvKNFVNqyGLKFPVAIDKGQKIIGTYGV-----G-PLPTSFLIDKDGKVVEQII 156
Cdd:cd03015   76 shlawrNTPRK-EGGLG--KINFPLLADPKKKISRDYGVldeeeGvALRGTFIIDPEGIIRHITV 137
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 51-167 2.41e-12

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: 60.76  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  51 GKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGV--EIIALDADETDIAVK-NFVNQYGLKFPVAIDKG 127
Cdd:cd03009    8 GGKVPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKESGKnfEIVFISWDRDEESFNdYFSKMPWLAVPFSDRER 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 753283820 128 -QKIIGTYGVGPLPTSFLIDKDGKVVEqiigEQTKEQLEGY 167
Cdd:cd03009   88 rSRLNRTFKIEGIPTLIILDADGEVVT----TDARELVLEY 124
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 38-152 3.01e-12

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: 61.49  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  38 GKEAPNFVVTDLEGKKIELKDL-KGKGVFLNFWGTWCkpcekemPYMNELYP-------KYKEKGVEIIALDADETDI-- 107
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFaDGKALVVMFICNHC-------PYVKAIEDrlnrlakEYGAKGVAVVAINSNDIEAyp 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 753283820 108 -----AVKNFVNQYGLKFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVV 152
Cdd:cd02969   74 edspeNMKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLV 123
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 64-171 1.25e-11

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: 58.29  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  64 VFLNFWGTWCKPCEKEMPYMNELYPKYKEKgVEIIALDADEtdiavknfvnqyglkfpvaidkGQKIIGTYGVGPLPTSF 143
Cdd:COG3118   21 VLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDVDE----------------------NPELAAQFGVRSIPTLL 77

                         90       100
                 ....*....|....*....|....*...
gi 753283820 144 LIdKDGKVVEQIIGEQTKEQLEGYLKKI 171
Cdd:COG3118   78 LF-KDGQPVDRFVGALPKEQLREFLDKV 104
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 40-152 1.27e-11

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: 59.29  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  40 EAPNFVVTDLEGKKIELKDLKGKG----VFLNFWgtWCKPCEKEMPYMNELYPKYKEKGVEIIALdADETDIAVKNFVNQ 115
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGpvvvVFYRGF--GCPFCREYLRALSKLLPELDALGVELVAV-GPESPEKLEAFDKG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 753283820 116 YGLKFPVAIDKGQKIIGTYGV-----------------------------GPLPTSFLIDKDGKVV 152
Cdd:cd02970   78 KFLPFPVYADPDRKLYRALGLvrslpwsntpralwknaaigfrgndegdgLQLPGVFVIGPDGTIL 143
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 57-165 1.48e-11

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 61.79  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   57 KDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEK-----GVEIIALDADETDIAVKNFVNQYGLKFPVAIDKGQKII 131
Cdd:PLN02919  416 RDLKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQpftvvGVHSAKFDNEKDLEAIRNAVLRYNISHPVVNDGDMYLW 495

                          90       100       110
                  ....*....|....*....|....*....|....
gi 753283820  132 GTYGVGPLPTSFLIDKDGKVVEQIIGEQTKEQLE 165
Cdd:PLN02919  496 RELGVSSWPTFAVVSPNGKLIAQLSGEGHRKDLD 529
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 59-169 1.45e-09

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: 52.18  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  59 LKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEkgVEIIALDADETdiavknfvnqyglkfpvaidkgQKIIGTYGVGP 138
Cdd:cd02947    8 KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDVDEN----------------------PELAEEYGVRS 63

                         90       100       110
                 ....*....|....*....|....*....|.
gi 753283820 139 LPTsFLIDKDGKVVEQIIGEQTKEQLEGYLK 169
Cdd:cd02947   64 IPT-FLFFKNGKEVDRVVGADPKEELEEFLE 93
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 64-170 1.92e-09

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: 52.29  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   64 VFLNFWGTWCKPCEKEMPYMNELYPKYKEKgVEIIALDADE-TDIAVKnfvnqyglkfpvaidkgqkiigtYGVGPLPTS 142
Cdd:TIGR01068  17 VLVDFWAPWCGPCKMIAPILEELAKEYEGK-VKFVKLNVDEnPDIAAK-----------------------YGIRSIPTL 72

                          90       100
                  ....*....|....*....|....*...
gi 753283820  143 FLIdKDGKVVEQIIGEQTKEQLEGYLKK 170
Cdd:TIGR01068  73 LLF-KNGKEVDRSVGALPKAALKQLINK 99
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 31-163 4.12e-09

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: 54.50  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  31 DKEKMQIGKEAPNFVVTDLEGKKIELKdlKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALdADETDIAVK 110
Cdd:PRK14018  28 DAGTATVPHTLSTLKTADNRPASVYLK--KDKPTLIKFWASWCPLCLSELGETEKWAQDAKFSSANLITV-ASPGFLHEK 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820 111 N---FVNQY-GL---KFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGEQTKEQ 163
Cdd:PRK14018 105 KdgdFQKWYaGLdypKLPVLTDNGGTLAQSLNISVYPSWAIIGKDGDVQRIVKGSISEAQ 164
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 61-165 2.26e-06

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 45.02  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  61 GKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKgVEIIALDADETdiavknfvnqyglkfpvaidKGQKIIGTYGVGPLP 140
Cdd:cd02950   20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQ-VNFVMLNVDNP--------------------KWLPEIDRYRVDGIP 78

                         90       100
                 ....*....|....*....|....*
gi 753283820 141 TSFLIDKDGKVVEQIIGEQTKEQLE 165
Cdd:cd02950   79 HFVFLDREGNEEGQSIGLQPKQVLA 103
PLN02399 PLN02399
phospholipid hydroperoxide glutathione peroxidase
 39-171 3.59e-06

phospholipid hydroperoxide glutathione peroxidase


Pssm-ID: 178021 [Multi-domain]  Cd Length: 236  Bit Score: 45.28  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  39 KEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADE-------TDIAVKN 111
Cdd:PLN02399  77 KSVHDFTVKDIDGKDVALSKFKGKVLLIVNVASKCGLTSSNYSELSHLYEKYKTQGFEILAFPCNQfggqepgSNPEIKQ 156

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 753283820 112 FV-NQYGLKFPVaIDK----GQKIIGTYG---------VGPLPT----SFLIDKDGKVVEQIIGEQTKEQLEGYLKKI 171
Cdd:PLN02399 157 FAcTRFKAEFPI-FDKvdvnGPSTAPVYQflksnaggfLGDLIKwnfeKFLVDKNGKVVERYPPTTSPFQIEKDIQKL 233
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 53-152 4.64e-06

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: 43.76  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  53 KIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGV--EIIALDADETDIAVKNFVNQYG--LKFPVAIDKGQ 128
Cdd:cd02964    9 VVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEEGKnfEIVFVSRDRSEESFNEYFSEMPpwLAVPFEDEELR 88

                         90       100
                 ....*....|....*....|....*
gi 753283820 129 KIIG-TYGVGPLPTSFLIDKDGKVV 152
Cdd:cd02964   89 ELLEkQFKVEGIPTLVVLKPDGDVV 113
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 12-171 4.93e-06

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 45.57  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  12 ILLILSGAVGFTLYQGFFADKEKMQIGKEAPnfVVTDLEGKKIELKDlKGKGVFLNFWGTWCKPCeKEM--------PYM 83
Cdd:COG4232  274 LALLLGALSGADPLQPLAAGAAAAAAAAGLA--WQADLEAALAEARA-EGKPVFVDFTADWCVTC-KENertvfsdpEVQ 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  84 NELypkykEKGVEIIALDADETDIAVKNFVNQYGLkfpvaidkgqkiigtYGVgplPTSFLIDKDGKVVEQIIGEQTKEQ 163
Cdd:COG4232  350 AAL-----ADDVVLLKADVTDNDPEITALLKRFGR---------------FGV---PTYVFYDPDGEELPRLGFMLTADE 406


                 ....*...
gi 753283820 164 LEGYLKKI 171
Cdd:COG4232  407 FLAALEKA 414
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 47-171 6.48e-06

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 43.74  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  47 TDLEGKKIELKDLKGKGVFLNFWGTWCK-PCEKEMPYMNELYPKYKEKGVE----------------------------- 96
Cdd:COG1999    6 TDQDGKPVTLADLRGKPVLVFFGYTSCPdVCPTTLANLAQVQEALGEDGGDdvqvlfisvdperdtpevlkayaeafgap 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 753283820  97 -IIALDADETDIavKNFVNQYGlkFPVAIDKGqkiiGTYGVGPLPTSFLIDKDGKVVEQIIGEQTKEQLEGYLKKI 171
Cdd:COG1999   86 rWIGLTGDPEEI--AALAKAFG--VYYEKVPD----GDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKAL 153
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 64-170 9.90e-06

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: 42.22  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   64 VFLNFWGTWCKPCEKEMPYMNELYPKYKEKgVEIIALDADE-TDIAVKnfvnqyglkfpvaidkgqkiigtYGVGPLPTs 142
Cdd:pfam00085  21 VLVDFYAPWCGPCKMLAPEYEELAQEYKGN-VVFAKVDVDEnPDLASK-----------------------YGVRGYPT- 75

                          90       100
                  ....*....|....*....|....*...
gi 753283820  143 FLIDKDGKVVEQIIGEQTKEQLEGYLKK 170
Cdd:pfam00085  76 LIFFKNGQPVDDYVGARPKDALAAFLKA 103
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 37-151 1.29e-05

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 43.68  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  37 IGKEAPNFVVTDLEGKkIELKDLKGKGVFLNFwgtwCKP------CEKEMPYMNELYPKYKEKGVEIIALDAD--ETDIA 108
Cdd:cd03016    1 LGDTAPNFEADTTHGP-IKFHDYLGDSWGILF----SHPadftpvCTTELGAFAKLAPEFKKRNVKLIGLSVDsvESHIK 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 753283820 109 VKNFVNQYG---LKFPVAIDKGQKIIGTYGV------GPLP--TSFLIDKDGKV 151
Cdd:cd03016   76 WIEDIEEYTgveIPFPIIADPDREVAKLLGMidpdagSTLTvrAVFIIDPDKKI 129
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 1-172 2.81e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 41.81  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   1 MKKnrLLFRVIILLILSGAVG---FTLYQGFFADKEKMQIgkeapnfvvtdlEGKKIelkdlkgkgvFLNFWGTWCKPCe 77
Cdd:COG2143    1 MKK--LLLLLLLLLLLAAAAAaqeISFLLDLEEDLALAKA------------EGKPI----------LLFFESDWCPYC- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  78 KEMpyMNELYP-----KYKEKGVEIIALDADEtDIAVKNFvnqyglkfpvaidKGQKII-----GTYGVGPLPTSFLIDK 147
Cdd:COG2143   56 KKL--HKEVFSdpevaAYLKENFVVVQLDAEG-DKEVTDF-------------DGETLTekelaRKYGVRGTPTLVFFDA 119

                        170       180
                 ....*....|....*....|....*
gi 753283820 148 DGKVVEQIIGEQTKEQLEGYLKKIT 172
Cdd:COG2143  120 EGKEIARIPGYLKPETFLALLKYVA 144
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
60-168 1.04e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 39.72  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820   60 KGKGVFLNFWGTWCKPC---EKEMPYMNELYPKYKEKGVEIIA--LDADETDIAVKNFVNQYGLkfpvaidkGQKiigtY 134
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCkklKKELLEDPDVTVYLGPNFVFIAVniWCAKEVAKAFTDILENKEL--------GRK----Y 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 753283820  135 GVGPLPTSFLIDKDGKvVEQIIGEQTKEQLEGYL 168
Cdd:pfam13098  71 GVRGTPTIVFFDGKGE-LLRLPGYVPAEEFLALL 103
trxA PRK09381
thioredoxin TrxA;
59-168 1.34e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 39.66  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  59 LKGKGVFL-NFWGTWCKPCEKEMPYMNELYPKYKEKgVEIIALDadetdiavknfvnqyglkfpvaIDKGQKIIGTYGVG 137
Cdd:PRK09381  18 LKADGAILvDFWAEWCGPCKMIAPILDEIADEYQGK-LTVAKLN----------------------IDQNPGTAPKYGIR 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 753283820 138 PLPTsFLIDKDGKVVEQIIGEQTKEQLEGYL 168
Cdd:PRK09381  75 GIPT-LLLFKNGEVAATKVGALSKGQLKEFL 104
PLN02412 PLN02412
probable glutathione peroxidase
 37-154 2.30e-04

probable glutathione peroxidase


Pssm-ID: 166053 [Multi-domain]  Cd Length: 167  Bit Score: 39.59  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  37 IGKEAP----NFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADE-------- 104
Cdd:PLN02412   1 MAEESPksiyDFTVKDIGGNDVSLNQYKGKVLLIVNVASKCGLTDSNYKELNVLYEKYKEQGFEILAFPCNQflgqepgs 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 753283820 105 TDIAVKNFVNQYGLKFPVaIDK----GQKIIGTY-------------GVGPLPTSFLIDKDGKVVEQ 154
Cdd:PLN02412  81 NEEIQQTVCTRFKAEFPI-FDKvdvnGKNTAPLYkylkaekgglfgdAIKWNFTKFLVSKEGKVVQR 146
PTZ00056 PTZ00056
glutathione peroxidase; Provisional
 43-122 3.75e-04

glutathione peroxidase; Provisional


Pssm-ID: 240248 [Multi-domain]  Cd Length: 199  Bit Score: 39.45  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  43 NFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALDA---------DETDIavKNFV 113
Cdd:PTZ00056  21 DYTVKTLEGTTVPMSSLKNKVLMITNSASKCGLTKKHVDQMNRLHSVFNPLGLEILAFPTsqflnqefpNTKDI--RKFN 98


                 ....*....
gi 753283820 114 NQYGLKFPV 122
Cdd:PTZ00056  99 DKNKIKYNF 107
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 35-155 1.19e-03

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 37.61  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  35 MQIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWgtwckpcEKEMP------------YMNELypkyKEKGVEIIALDA 102
Cdd:PRK09437   4 LKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYFY-------PKAMTpgctvqacglrdNMDEL----KKAGVVVLGIST 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 753283820 103 DETDiAVKNFVNQYGLKFPVAIDKGQKIIGTYGV------------GPLPTSFLIDKDGKvVEQI 155
Cdd:PRK09437  73 DKPE-KLSRFAEKELLNFTLLSDEDHQVAEQFGVwgekkfmgktydGIHRISFLIDADGK-IEHV 135
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 41-152 1.60e-03

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


Pssm-ID: 239266  Cd Length: 142  Bit Score: 36.81  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  41 APNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCK-PCEKEMPYMNELYPKYKEKGVEIIAL-----D-ADETDIAVKNFV 113
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPdVCPTTLANLAQALKQLGADGGDDVQVvfisvDpERDTPEVLKAYA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 753283820 114 NQYGLKF------PVAIDKGQK-----------IIGTYGVGPLPTSFLIDKDGKVV 152
Cdd:cd02968   82 KAFGPGWigltgtPEEIEALAKafgvyyekvpeDDGDYLVDHSAAIYLVDPDGKLV 137
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 61-107 1.79e-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: 37.73  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 753283820   61 GKGVFLNFWGTWCKPCEKEMPYMNELYPKYK--EKGVEIIALDADETDI 107
Cdd:TIGR01130 364 TKDVLVEFYAPWCGHCKNLAPIYEELAEKYKdaESDVVIAKMDATANDV 412
mauD cd02967
Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD ...
 42-152 1.80e-03

Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD gene found in methylotrophic bacteria, which are able to use methylamine as a sole carbon source and a nitrogen source. mauD is an essential accessory protein for the biosynthesis of methylamine dehydrogenase (MADH), the enzyme that catalyzes the oxidation of methylamine and other primary amines. MADH possesses an alpha2beta2 subunit structure; the alpha subunit is also referred to as the large subunit. Each beta (small) subunit contains a tryptophan tryptophylquinone (TTQ) prosthetic group. Accessory proteins are essential for the proper transport of MADH to the periplasm, TTQ synthesis and the formation of several structural disulfide bonds. Bacterial mutants containing an insertion on the mauD gene were unable to grow on methylamine as a sole carbon source, were found to lack the MADH small subunit and had decreased amounts of the MADH large subunit.


Pssm-ID: 239265  Cd Length: 114  Bit Score: 36.22  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  42 PNFVVTDLEGKKIELKDLK-GKGVFLNFWGTWCKPCEKEMPYMNELypKYKEKGVEIIALDADETDIAVKNFVNQYGL-K 119
Cdd:cd02967    1 PTFDLTTIDGAPVRIGGISpGRPTLLFFLSPTCPVCKKLLPVIRSI--ARAEADWLDVVLASDGEKAEHQRFLKKHGLeA 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 753283820 120 FPVAIDkgQKIIGTYGVGPLPTSFLIDKDGKVV 152
Cdd:cd02967   79 FPYVLS--AELGMAYQVSKLPYAVLLDEAGVIA 109
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 36-162 1.86e-03

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: 36.79  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  36 QIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNfwgtwCKP------CEKEMPYMNELYPKYkeKGVEIIALDADeTDIAV 109
Cdd:cd03014    1 KVGDKAPDFTLVTSDLSEVSLADFAGKVKVIS-----VFPsidtpvCATQTKRFNKEAAKL--DNTVVLTISAD-LPFAQ 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753283820 110 KNFVNQYGLK-FPVAIDKGQKIIG-TYGV-----GPLPTS-FLIDKDGKVV-EQIIGEQTKE 162
Cdd:cd03014   73 KRWCGAEGVDnVTTLSDFRDHSFGkAYGVlikdlGLLARAvFVIDENGKVIyVELVPEITDE 134
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
33-162 4.46e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 35.84  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  33 EKMQIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFW-----GTwckpCEKEMPYMNELYPKYkeKGVEIIALDADeTDI 107
Cdd:COG2077   16 NLPKVGDKAPDFTLVDTDLSDVTLSDFAGKRKVLNIVpsldtPV----CATSTRKFNEEAAKL--DNVVVLTISAD-LPF 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 753283820 108 AVKNFVNQYGLK------------FpvaidkGQKiigtYGV----GPLP--TS---FLIDKDGKVV-EQIIGEQTKE 162
Cdd:COG2077   89 AQKRFCGAEGIDnvvtlsdfrdrsF------GKD----YGVlikeGPLLglLAravFVLDENGKVVyTELVPEITDE 155
PTZ00051 PTZ00051
thioredoxin; Provisional
 64-157 4.71e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 34.85  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753283820  64 VFLNFWGTWCKPCEKEMPYMNELYPKYKEkgveiialdadetdiavknfvnqygLKF-PVAIDKGQKIIGTYGVGPLPTs 142
Cdd:PTZ00051  21 VIVDFYAEWCGPCKRIAPFYEECSKEYTK-------------------------MVFvKVDVDELSEVAEKENITSMPT- 74

                         90
                 ....*....|....*
gi 753283820 143 FLIDKDGKVVEQIIG 157
Cdd:PTZ00051  75 FKVFKNGSVVDTLLG 89
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 64-116 8.36e-03

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 34.29  E-value: 8.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 753283820  64 VFLNFWGTWCkpcekemPYMNELYP-----------KYKEKGVEIIA-LDAD-ETDIAVKNFVNQY 116
Cdd:cd02996   21 VLVNFYADWC-------RFSQMLHPifeeaaakikeEFPDAGKVVWGkVDCDkESDIADRYRINKY 79
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 60-112 9.41e-03

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 35.88  E-value: 9.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 753283820  60 KGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIA-LDADETDIAVKNF 112
Cdd:PTZ00102 374 SDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNDSIIVAkMNGTANETPLEEF 427
 
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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