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Conserved domains on  [gi|727722783|ref|WP_033844920|]
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MULTISPECIES: thioredoxin family protein [Geobacillus]

Protein Classification

thioredoxin family protein( domain architecture ID 10121933)

thioredoxin family protein with similarity to peroxiredoxins, may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein thiol or disulfide bonds using an active site disulfide or dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035
PubMed:  15518547|12517450|15558583|10049365|9099998|11441809|12074972|30367780
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-183 3.28e-103

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: 294.15  E-value: 3.28e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  12 GKQAPPFALTNVvDGRLVRLDDVKSDVATVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSNDVEQYPDDSPEN 91
Cdd:cd02969    1 GSPAPDFSLPDT-DGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  92 MKKVAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCVYRGQLDDSRPSNGIPVTGESIRAALDALLAGRPVPE 171
Cdd:cd02969   80 MKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGKPVPV 159

                        170
                 ....*....|..
gi 727722783 172 HQKPSIGCSIKW 183
Cdd:cd02969  160 PQTPSIGCSIKW 171
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-183 3.28e-103

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: 294.15  E-value: 3.28e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  12 GKQAPPFALTNVvDGRLVRLDDVKSDVATVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSNDVEQYPDDSPEN 91
Cdd:cd02969    1 GSPAPDFSLPDT-DGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  92 MKKVAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCVYRGQLDDSRPSNGIPVTGESIRAALDALLAGRPVPE 171
Cdd:cd02969   80 MKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGKPVPV 159

                        170
                 ....*....|..
gi 727722783 172 HQKPSIGCSIKW 183
Cdd:cd02969  160 PQTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
15-168 2.88e-38

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 128.06  E-value: 2.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  15 APPFALTNVvDGRLVRLDDVKSDVaTVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSndveqypdDSPENMKK 94
Cdd:COG1225    1 APDFTLPDL-DGKTVSLSDLRGKP-VVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS--------DSDEAHKK 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727722783  95 VAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCVYR--GQLDDSrpsngipvtgESIRAALDALLAGRP 168
Cdd:COG1225   71 FAEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVwvGPVDPR----------PHLEEVLEALLAELK 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 11-137 1.14e-21

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: 85.35  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783   11 LGKQAPPFALTNVvDGRLVRLDDVKsDVATVIMFICN-HCPFVKHVQHELVRLANDYMPKGVSFVAINSndveqypdDSP 89
Cdd:pfam00578   1 VGDKAPDFELPDG-DGGTVSLSDYR-GKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSV--------DSP 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 727722783   90 ENMKKVAEELGYPFPYLYDETQEVARAYDA------ACTPDFYIFDRELKCVYR 137
Cdd:pfam00578  71 ESHKAFAEKYGLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
6-135 4.40e-07

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 47.69  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783   6 SNMFP------LGKQAPPFALTNVvDGRLVRLDDVKSDvATVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSn 79
Cdd:PRK03147  26 SNFFAdkekvqVGKEAPNFVLTDL-EGKKIELKDLKGK-GVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNV- 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727722783  80 dveqypDDSPENMKKVAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCV 135
Cdd:PRK03147 103 ------DETELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVV 152
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-183 3.28e-103

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: 294.15  E-value: 3.28e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  12 GKQAPPFALTNVvDGRLVRLDDVKSDVATVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSNDVEQYPDDSPEN 91
Cdd:cd02969    1 GSPAPDFSLPDT-DGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  92 MKKVAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCVYRGQLDDSRPSNGIPVTGESIRAALDALLAGRPVPE 171
Cdd:cd02969   80 MKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGKPVPV 159

                        170
                 ....*....|..
gi 727722783 172 HQKPSIGCSIKW 183
Cdd:cd02969  160 PQTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
15-168 2.88e-38

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 128.06  E-value: 2.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  15 APPFALTNVvDGRLVRLDDVKSDVaTVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSndveqypdDSPENMKK 94
Cdd:COG1225    1 APDFTLPDL-DGKTVSLSDLRGKP-VVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS--------DSDEAHKK 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727722783  95 VAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCVYR--GQLDDSrpsngipvtgESIRAALDALLAGRP 168
Cdd:COG1225   71 FAEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVwvGPVDPR----------PHLEEVLEALLAELK 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 8-166 1.98e-23

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 90.13  E-value: 1.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783   8 MFPLGKQAPPFALTNVvDGRLVRLDDVKSDVaTVIMFICNHCPFVKHVQHELVRLANDYmpKGVSFVAINSndveqypDD 87
Cdd:COG0526    1 MKAVGKPAPDFTLTDL-DGKPLSLADLKGKP-VLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDV-------DE 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727722783  88 SPENMKKVAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCVYRgqlddsrpSNGiPVTGESIRAALDALLAG 166
Cdd:COG0526   70 NPEAVKAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVAR--------HVG-PLSPEELEEALEKLLAK 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 11-137 1.14e-21

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: 85.35  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783   11 LGKQAPPFALTNVvDGRLVRLDDVKsDVATVIMFICN-HCPFVKHVQHELVRLANDYMPKGVSFVAINSndveqypdDSP 89
Cdd:pfam00578   1 VGDKAPDFELPDG-DGGTVSLSDYR-GKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSV--------DSP 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 727722783   90 ENMKKVAEELGYPFPYLYDETQEVARAYDA------ACTPDFYIFDRELKCVYR 137
Cdd:pfam00578  71 ESHKAFAEKYGLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDGKVRYI 124
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 17-137 1.56e-17

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: 74.19  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  17 PFALTNVvDGRLVRLDDVKSDVaTVIMFI---CNHCpfvkhvQHE---LVRLANDYMPKGVSFVAINsndveqYPDDSPE 90
Cdd:cd02966    1 DFSLPDL-DGKPVSLSDLKGKV-VLVNFWaswCPPC------RAEmpeLEALAKEYKDDGVEVVGVN------VDDDDPA 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 727722783  91 NMKKVAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCVYR 137
Cdd:cd02966   67 AVKAFLKKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRAR 113
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 10-145 7.34e-16

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 70.86  E-value: 7.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783   10 PLGKQAPPFALTNV-VDGRLVRLDDVKSDVATVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSndveqypDDS 88
Cdd:pfam08534   1 KAGDKAPDFTLPDAaTDGNTVSLSDFKGKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNS-------DND 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727722783   89 PENMKKVAEELGYPFPYLYDETQEVARAYDAA---------CTPDFYIFDRELKCVYRGQLDDSRP 145
Cdd:pfam08534  74 AFFVKRFWGKEGLPFPFLSDGNAAFTKALGLPieedasaglRSPRYAVIDEDGKVVYLFVGPEPGV 139
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 14-117 3.23e-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: 55.83  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  14 QAPPFALTNVvDGRLVRLDDVKSDVATVIMFICN-HCPFVK-HVqHELVRLANDYMPKGVSFVAINSndveqypdDSPEN 91
Cdd:cd02970    1 TAPDFELPDA-GGETVTLSALLGEGPVVVVFYRGfGCPFCReYL-RALSKLLPELDALGVELVAVGP--------ESPEK 70

                         90       100
                 ....*....|....*....|....*.
gi 727722783  92 MKKVAEELGYPFPYLYDETQEVARAY 117
Cdd:cd02970   71 LEAFDKGKFLPFPVYADPDRKLYRAL 96
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
6-135 4.40e-07

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 47.69  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783   6 SNMFP------LGKQAPPFALTNVvDGRLVRLDDVKSDvATVIMFICNHCPFVKHVQHELVRLANDYMPKGVSFVAINSn 79
Cdd:PRK03147  26 SNFFAdkekvqVGKEAPNFVLTDL-EGKKIELKDLKGK-GVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNV- 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727722783  80 dveqypDDSPENMKKVAEELGYPFPYLYDETQEVARAYDAACTPDFYIFDRELKCV 135
Cdd:PRK03147 103 ------DETELAVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDKDGKVV 152
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 12-162 1.38e-06

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: 45.73  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  12 GKQAPPFALTNVvDGRLVRLDDVKSDVATVIMFIcnhcP--FVKHVQHELVRLaNDYMPK----GVSFVAINSndveqyp 85
Cdd:cd03018    4 GDKAPDFELPDQ-NGQEVRLSEFRGRKPVVLVFF----PlaFTPVCTKELCAL-RDSLELfeaaGAEVLGISV------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  86 dDSPENMKKVAEELGYPFPYLYD--ETQEVARAYDaACTPDF-------YIFDRELKCVYRGQLDDSRPSNgIPVtgesI 156
Cdd:cd03018   71 -DSPFSLRAWAEENGLTFPLLSDfwPHGEVAKAYG-VFDEDLgvaeravFVIDRDGIIRYAWVSDDGEPRD-LPD----Y 143


                 ....*.
gi 727722783 157 RAALDA 162
Cdd:cd03018  144 DEALDA 149
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 15-117 8.04e-04

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


Pssm-ID: 239266  Cd Length: 142  Bit Score: 37.97  E-value: 8.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  15 APPFALTNVvDGRLVRLDDVKSDVaTVIMFI---CNH-CPFVKHVQHELVRLANDYMPKGVSFVAInSNDveqyPD-DSP 89
Cdd:cd02968    2 GPDFTLTDQ-DGRPVTLSDLKGKP-VLVYFGythCPDvCPTTLANLAQALKQLGADGGDDVQVVFI-SVD----PErDTP 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 727722783  90 ENMKKVAEELGYPFPYL---YDETQEVARAY 117
Cdd:cd02968   75 EVLKAYAKAFGPGWIGLtgtPEEIEALAKAF 105
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 39-129 8.62e-03

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: 34.97  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727722783  39 ATVIMFICNHCPFVKHVQHELVRLANDYmpkgvSFVAInsndveQYPDDSPENMKKVAEELGYPFPYLYDETQEVARAYD 118
Cdd:cd03011   22 PVLVYFWATWCPVCRFTSPTVNQLAADY-----PVVSV------ALRSGDDGAVARFMQKKGYGFPVINDPDGVISARWG 90

                         90
                 ....*....|.
gi 727722783 119 AACTPDFYIFD 129
Cdd:cd03011   91 VSVTPAIVIVD 101
 
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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