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Conserved domains on  [gi|648475437|ref|WP_026167188|]
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thioredoxin family protein [Balneola vulgaris]

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. ...
 12-182 3.37e-99

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: 284.13  E-value: 3.37e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  12 GSKAPAFELIDTNQELRSLADLAGDEGTLVMFICNHCPYVKHLNSKFVELANEYQKKGINWIAISSNDVENYPQDSPELM 91
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  92 KKLAEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDKSLKLYYRGQFDSSRPGNDIPVTGNDLEKAMQNLLESKPAPEP 171
Cdd:cd02969   81 KAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGKPVPVP 160

                        170
                 ....*....|.
gi 648475437 172 QIPSIGCNIKW 182
Cdd:cd02969  161 QTPSIGCSIKW 171
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-182 3.37e-99

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: 284.13  E-value: 3.37e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  12 GSKAPAFELIDTNQELRSLADLAGDEGTLVMFICNHCPYVKHLNSKFVELANEYQKKGINWIAISSNDVENYPQDSPELM 91
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  92 KKLAEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDKSLKLYYRGQFDSSRPGNDIPVTGNDLEKAMQNLLESKPAPEP 171
Cdd:cd02969   81 KAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGKPVPVP 160

                        170
                 ....*....|.
gi 648475437 172 QIPSIGCNIKW 182
Cdd:cd02969  161 QTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
15-167 1.72e-38

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 128.83  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  15 APAFELIDTNQELRSLADLAGDeGTLVMFICNHCPYVKHLNSKFVELANEYQKKGINWIAISSndvenypqDSPELMKKL 94
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGK-PVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS--------DSDEAHKKF 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648475437  95 AEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDKSLKLYYR--GQFDSSRpgndipvtgnDLEKAMQNLLESKP 167
Cdd:COG1225   72 AEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVwvGPVDPRP----------HLEEVLEALLAELK 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 11-136 4.11e-25

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: 94.21  E-value: 4.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   11 LGSKAPAFELIDTNQELRSLADLAGDeGTLVMFICN-HCPYVKHLNSKFVELANEYQKKGINWIAISSndvenypqDSPE 89
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGK-WVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSV--------DSPE 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 648475437   90 LMKKLAEEEGFPFPYLYDENQEVAKAYKA------ACTPDLFLFDKSLKLYYR 136
Cdd:pfam00578  72 SHKAFAEKYGLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-129 5.72e-10

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 55.78  E-value: 5.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   1 MAATKSIMlELGSKAPAFELIDTNQELRSLADLAGdEGTLVMF---ICNHC----PYVKhlnskfvELANEYQKKGINWI 73
Cdd:PRK03147  28 FFADKEKV-QVGKEAPNFVLTDLEGKKIELKDLKG-KGVFLNFwgtWCKPCekemPYMN-------ELYPKYKEKGVEII 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 648475437  74 AISSndvenypqDSPEL-MKKLAEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDK 129
Cdd:PRK03147  99 AVNV--------DETELaVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDK 147
 
Name Accession Description Interval E-value
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 12-182 3.37e-99

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: 284.13  E-value: 3.37e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  12 GSKAPAFELIDTNQELRSLADLAGDEGTLVMFICNHCPYVKHLNSKFVELANEYQKKGINWIAISSNDVENYPQDSPELM 91
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYPEDSPENM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  92 KKLAEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDKSLKLYYRGQFDSSRPGNDIPVTGNDLEKAMQNLLESKPAPEP 171
Cdd:cd02969   81 KAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLVYRGRIDDSRPGNDPPVTGRDLRAALDALLAGKPVPVP 160

                        170
                 ....*....|.
gi 648475437 172 QIPSIGCNIKW 182
Cdd:cd02969  161 QTPSIGCSIKW 171
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
15-167 1.72e-38

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 128.83  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  15 APAFELIDTNQELRSLADLAGDeGTLVMFICNHCPYVKHLNSKFVELANEYQKKGINWIAISSndvenypqDSPELMKKL 94
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGK-PVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS--------DSDEAHKKF 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648475437  95 AEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDKSLKLYYR--GQFDSSRpgndipvtgnDLEKAMQNLLESKP 167
Cdd:COG1225   72 AEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVwvGPVDPRP----------HLEEVLEALLAELK 136
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 11-136 4.11e-25

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: 94.21  E-value: 4.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   11 LGSKAPAFELIDTNQELRSLADLAGDeGTLVMFICN-HCPYVKHLNSKFVELANEYQKKGINWIAISSndvenypqDSPE 89
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGK-WVVLFFYPAdWTPVCTTELPALADLYEEFKKLGVEVLGVSV--------DSPE 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 648475437   90 LMKKLAEEEGFPFPYLYDENQEVAKAYKA------ACTPDLFLFDKSLKLYYR 136
Cdd:pfam00578  72 SHKAFAEKYGLPFPLLSDPDGEVARAYGVlneeegGALRATFVIDPDGKVRYI 124
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 8-165 1.32e-19

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 80.50  E-value: 1.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   8 MLELGSKAPAFELIDTNQELRSLADLAGdEGTLVMFICNHCPYVKHLNSKFVELANEYqkKGINWIAISSNDvenypqdS 87
Cdd:COG0526    1 MKAVGKPAPDFTLTDLDGKPLSLADLKG-KPVLVNFWATWCPPCRAEMPVLKELAEEY--GGVVFVGVDVDE-------N 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  88 PELMKKLAEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDKSLKLYYR--GQFDSSrpgndipvtgnDLEKAMQNLLES 165
Cdd:COG0526   71 PEAVKAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARhvGPLSPE-----------ELEEALEKLLAK 139
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 12-155 1.44e-17

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 75.48  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   12 GSKAPAFELIDTNQELR--SLADLAGdeGTLVMFI--CNHCPYVKHLNSKFVELANEYQKKGINWIAISSndvenypQDS 87
Cdd:pfam08534   3 GDKAPDFTLPDAATDGNtvSLSDFKG--KKVVLNFwpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNS-------DND 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648475437   88 PELMKKLAEEEGFPFPYLYDENQEVAKAYKAA---------CTPDLFLFDKSLKLYYRGQFDSsrPGNDIPVTGNDL 155
Cdd:pfam08534  74 AFFVKRFWGKEGLPFPFLSDGNAAFTKALGLPieedasaglRSPRYAVIDEDGKVVYLFVGPE--PGVDVSDAEAVL 148
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 14-116 3.74e-14

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: 66.61  E-value: 3.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  14 KAPAFELIDTNQELRSLADLAGDEGTLVMFICN-HCPYVK-HLNSkFVELANEYQKKGINWIAISsndvenypQDSPELM 91
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGfGCPFCReYLRA-LSKLLPELDALGVELVAVG--------PESPEKL 71

                         90       100
                 ....*....|....*....|....*
gi 648475437  92 KKLAEEEGFPFPYLYDENQEVAKAY 116
Cdd:cd02970   72 EAFDKGKFLPFPVYADPDRKLYRAL 96
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 17-136 9.11e-14

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: 64.56  E-value: 9.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  17 AFELIDTNQELRSLADLAGDeGTLVMFI---CNHC----PYvkhlnskFVELANEYQKKGINWIAIssndveNYPQDSPE 89
Cdd:cd02966    1 DFSLPDLDGKPVSLSDLKGK-VVLVNFWaswCPPCraemPE-------LEALAKEYKDDGVEVVGV------NVDDDDPA 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 648475437  90 LMKKLAEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDKSLKLYYR 136
Cdd:cd02966   67 AVKAFLKKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRAR 113
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 14-118 1.18e-10

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: 56.79  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  14 KAPAFELIDTNQELRSLADLAGdeGTLVMFI-------------CNhcpyvkhlnskFVELANEYQKKGINWIAISSndv 80
Cdd:cd03017    2 KAPDFTLPDQDGETVSLSDLRG--KPVVLYFypkddtpgctkeaCD-----------FRDLYEEFKALGAVVIGVSP--- 65

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648475437  81 enypqDSPELMKKLAEEEGFPFPYLYDENQEVAKAYKA 118
Cdd:cd03017   66 -----DSVESHAKFAEKYGLPFPLLSDPDGKLAKAYGV 98
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
1-129 5.72e-10

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 55.78  E-value: 5.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   1 MAATKSIMlELGSKAPAFELIDTNQELRSLADLAGdEGTLVMF---ICNHC----PYVKhlnskfvELANEYQKKGINWI 73
Cdd:PRK03147  28 FFADKEKV-QVGKEAPNFVLTDLEGKKIELKDLKG-KGVFLNFwgtWCKPCekemPYMN-------ELYPKYKEKGVEII 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 648475437  74 AISSndvenypqDSPEL-MKKLAEEEGFPFPYLYDENQEVAKAYKAACTPDLFLFDK 129
Cdd:PRK03147  99 AVNV--------DETELaVKNFVNRYGLTFPVAIDKGRQVIDAYGVGPLPTTFLIDK 147
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 9-116 5.09e-09

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: 52.66  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   9 LELGSKAPAFELIDTNQELRSLADLAGDEGTLVMF-------ICNH--CPYVKHLnSKFVELaneyqkkGINWIAISSnd 79
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFfplaftpVCTKelCALRDSL-ELFEAA-------GAEVLGISV-- 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 648475437  80 venypqDSPELMKKLAEEEGFPFPYLYDENQ--EVAKAY 116
Cdd:cd03018   71 ------DSPFSLRAWAEENGLTFPLLSDFWPhgEVAKAY 103
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 14-116 5.40e-09

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: 52.55  E-value: 5.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  14 KAPAFELIDTNQELRSLADLAGdeGTLVMF-------------ICNhcpyvkhlnskFVELANEYQKKGINWIAISSndv 80
Cdd:cd02971    1 KAPDFTLPATDGGEVSLSDFKG--KWVVLFfypkdftpvctteLCA-----------FRDLAEEFAKGGAEVLGVSV--- 64

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 648475437  81 enypqDSPELMKKLAE-EEGFPFPYLYDENQEVAKAY 116
Cdd:cd02971   65 -----DSPFSHKAWAEkEGGLNFPLLSDPDGEFAKAY 96
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 9-116 1.62e-07

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 48.78  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   9 LELGSKAPAFELIDTNQELRSLADLAGDEgTLVMFicnhcpYVKHL------------NSKfvelaNEYQKKGINWIAIS 76
Cdd:PRK09437   4 LKAGDIAPKFSLPDQDGEQVSLTDFQGQR-VLVYF------YPKAMtpgctvqacglrDNM-----DELKKAGVVVLGIS 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 648475437  77 SndvenypqDSPELMKKLAEEEGFPFPYLYDENQEVAKAY 116
Cdd:PRK09437  72 T--------DKPEKLSRFAEKELLNFTLLSDEDHQVAEQF 103
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 15-117 5.63e-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: 38.35  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437  15 APAFELIDTNQELRSLADLAGdEGTLVMFICNHCPYV-----KHLnSKFVELANEYQKKGINWIAISSnDVENypqDSPE 89
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKG-KPVLVYFGYTHCPDVcpttlANL-AQALKQLGADGGDDVQVVFISV-DPER---DTPE 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 648475437  90 LMKKLAEE--EGFPFpyL---YDENQEVAKAYK 117
Cdd:cd02968   76 VLKAYAKAfgPGWIG--LtgtPEEIEALAKAFG 106
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 8-118 1.42e-03

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 37.91  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   8 MLELGSKAPAFELIDTnqelRSLADLAGDEGTLVMFICNHCPYVKHLNSKFVELA---NEYQKKGINWIAISSNDVENYP 84
Cdd:PRK13190   1 PVKLGQKAPDFTVNTT----KGPIDLSKYKGKWVLLFSHPADFTPVCTTEFIAFSrryEDFKKLGVELVGLSVDSIYSHI 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648475437  85 QdspeLMKKLAEEEGF--PFPYLYDENQEVAKAYKA 118
Cdd:PRK13190  77 A----WLRDIEERFGIkiPFPVIADIDKELAREYNL 108
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 39-130 2.67e-03

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: 35.75  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475437   39 TLVMFICNHCPYVKHLNSKFVELANEYQK-KGINWIAISS----NDVENYPQDSPelMKKLAeeegfpFPYLYDENQEVA 113
Cdd:pfam13905   4 VLLYFGASWCKPCRRFTPLLKELYEKLKKkKNVEIVFVSLdrdlEEFKDYLKKMP--KDWLS------VPFDDDERNELK 75

                          90
                  ....*....|....*..
gi 648475437  114 KAYKAACTPDLFLFDKS 130
Cdd:pfam13905  76 RKYGVNAIPTLVLLDPN 92
AhpC-TSA_2 pfam13911
AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide ...
 60-118 5.83e-03

AhpC/TSA antioxidant enzyme; This family contains proteins related to alkyl hydro-peroxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 433575  Cd Length: 114  Bit Score: 35.36  E-value: 5.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 648475437   60 ELANEYQKKGINWIAISsndvenypQDSPELMKKLAEEEGFPFPYLYDENqevAKAYKA 118
Cdd:pfam13911   4 SLKPELDAAGIRLVAIG--------CGTPGRIEEFIKLTGFPFPVYVDPS---RKLYRA 51
 
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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