NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1722220843|ref|WP_146533543|]
View 

redoxin family protein [Rubripirellula reticaptiva]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 41-190 6.73e-23

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


:

Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 89.35  E-value: 6.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  41 KVGQEAPDFEL--LNTEGKMISLKELTKKTpvvmLVLRGWPGKQCPLCSRQVgEFVSKQSEF---DEVQVVMIYPGPAEL 115
Cdd:pfam08534   1 KAGDKAPDFTLpdAATDGNTVSLSDFKGKK----VVLNFWPGAFCPTCSAEH-PYLEKLNELykeKGVDVVAVNSDNDAF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1722220843 116 LtehAKEFQGSqtFPANYHFVLDPDYKFTNDWGLRWDAPYET--AYPSTFVVNEDQKILFGKTVVSHG-DRADVATVV 190
Cdd:pfam08534  76 F---VKRFWGK--EGLPFPFLSDGNAAFTKALGLPIEEDASAglRSPRYAVIDEDGKVVYLFVGPEPGvDVSDAEAVL 148
 
Name Accession Description Interval E-value
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 41-190 6.73e-23

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 89.35  E-value: 6.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  41 KVGQEAPDFEL--LNTEGKMISLKELTKKTpvvmLVLRGWPGKQCPLCSRQVgEFVSKQSEF---DEVQVVMIYPGPAEL 115
Cdd:pfam08534   1 KAGDKAPDFTLpdAATDGNTVSLSDFKGKK----VVLNFWPGAFCPTCSAEH-PYLEKLNELykeKGVDVVAVNSDNDAF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1722220843 116 LtehAKEFQGSqtFPANYHFVLDPDYKFTNDWGLRWDAPYET--AYPSTFVVNEDQKILFGKTVVSHG-DRADVATVV 190
Cdd:pfam08534  76 F---VKRFWGK--EGLPFPFLSDGNAAFTKALGLPIEEDASAglRSPRYAVIDEDGKVVYLFVGPEPGvDVSDAEAVL 148
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 45-173 7.34e-23

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: 89.34  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  45 EAPDFELLNTEGKMISLKELTKKTPVVMLVLRGWpgkQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELLTEHAke 122
Cdd:cd02970     1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGF---GCPFCREYLRALSKLLPELDAlgVELVAVGPESPEKLEAFD-- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1722220843 123 fqgsQTFPANYHFVLDPDYKFTNDWGLRW----------------------DAPYETAYPSTFVVNEDQKILF 173
Cdd:cd02970    76 ----KGKFLPFPVYADPDRKLYRALGLVRslpwsntpralwknaaigfrgnDEGDGLQLPGVFVIGPDGTILF 144
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
46-193 2.26e-19

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 79.91  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  46 APDFELLNTEGKMISLKELTKKtPVVMLVLRGWpgkqCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELLTEHAKEF 123
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGK-PVVLYFYATW----CPGCTAELPELRDLYEEFKDkgVEVLGVSSDSDEAHKKFAEKY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843 124 QgsqtfpANYHFVLDPDYKFTNDWGLRWdapyetaYPSTFVVNEDQKILFgKTVVSHGDRADVATVVAEL 193
Cdd:COG1225    76 G------LPFPLLSDPDGEVAKAYGVRG-------TPTTFLIDPDGKIRY-VWVGPVDPRPHLEEVLEAL 131
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
41-171 4.87e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 44.99  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  41 KVGQEAPDFELLNTEGKMISLKELTKKTpvVMLVLrgWpGKQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELLTE 118
Cdd:PRK03147   36 QVGKEAPNFVLTDLEGKKIELKDLKGKG--VFLNF--W-GTWCKPCEKEMPYMNELYPKYKEkgVEIIAVNVDETELAVK 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1722220843 119 H-AKEFQgsQTFPAnyhfVLDPDYKFTNDWGLrwdapyeTAYPSTFVVNEDQKI 171
Cdd:PRK03147  111 NfVNRYG--LTFPV----AIDKGRQVIDAYGV-------GPLPTTFLIDKDGKV 151
 
Name Accession Description Interval E-value
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 41-190 6.73e-23

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 89.35  E-value: 6.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  41 KVGQEAPDFEL--LNTEGKMISLKELTKKTpvvmLVLRGWPGKQCPLCSRQVgEFVSKQSEF---DEVQVVMIYPGPAEL 115
Cdd:pfam08534   1 KAGDKAPDFTLpdAATDGNTVSLSDFKGKK----VVLNFWPGAFCPTCSAEH-PYLEKLNELykeKGVDVVAVNSDNDAF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1722220843 116 LtehAKEFQGSqtFPANYHFVLDPDYKFTNDWGLRWDAPYET--AYPSTFVVNEDQKILFGKTVVSHG-DRADVATVV 190
Cdd:pfam08534  76 F---VKRFWGK--EGLPFPFLSDGNAAFTKALGLPIEEDASAglRSPRYAVIDEDGKVVYLFVGPEPGvDVSDAEAVL 148
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 45-173 7.34e-23

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: 89.34  E-value: 7.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  45 EAPDFELLNTEGKMISLKELTKKTPVVMLVLRGWpgkQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELLTEHAke 122
Cdd:cd02970     1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGF---GCPFCREYLRALSKLLPELDAlgVELVAVGPESPEKLEAFD-- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1722220843 123 fqgsQTFPANYHFVLDPDYKFTNDWGLRW----------------------DAPYETAYPSTFVVNEDQKILF 173
Cdd:cd02970    76 ----KGKFLPFPVYADPDRKLYRALGLVRslpwsntpralwknaaigfrgnDEGDGLQLPGVFVIGPDGTILF 144
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 42-171 7.54e-22

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: 85.74  E-value: 7.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  42 VGQEAPDFELLNTEGKMISLKELTKKTpvvmLVLRGWPGKQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELLTEH 119
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDYRGKW----VVLFFYPADWTPVCTTELPALADLYEEFKKlgVEVLGVSVDSPESHKAF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1722220843 120 AKEFQgsqtfpANYHFVLDPDYKFTNDWGLrWDAPYETAYPSTFVVNEDQKI 171
Cdd:pfam00578  77 AEKYG------LPFPLLSDPDGEVARAYGV-LNEEEGGALRATFVIDPDGKV 121
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
46-193 2.26e-19

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 79.91  E-value: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  46 APDFELLNTEGKMISLKELTKKtPVVMLVLRGWpgkqCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELLTEHAKEF 123
Cdd:COG1225     1 APDFTLPDLDGKTVSLSDLRGK-PVVLYFYATW----CPGCTAELPELRDLYEEFKDkgVEVLGVSSDSDEAHKKFAEKY 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843 124 QgsqtfpANYHFVLDPDYKFTNDWGLRWdapyetaYPSTFVVNEDQKILFgKTVVSHGDRADVATVVAEL 193
Cdd:COG1225    76 G------LPFPLLSDPDGEVAKAYGVRG-------TPTTFLIDPDGKIRY-VWVGPVDPRPHLEEVLEAL 131
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 42-193 8.39e-12

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 60.09  E-value: 8.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  42 VGQEAPDFELLNTEGKMISLKELTKKtPVVMLVLRGWpgkqCPLCSRQVGEFVSKQSEFDEVQVVMI-YPGPAELLTEHA 120
Cdd:COG0526     4 VGKPAPDFTLTDLDGKPLSLADLKGK-PVLVNFWATW----CPPCRAEMPVLKELAEEYGGVVFVGVdVDENPEAVKAFL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1722220843 121 KEFQgsqtfpANYHFVLDPDYKFTNDWGLRwdapyetAYPSTFVVNEDQKILFgkTVVSHGDRADVATVVAEL 193
Cdd:COG0526    79 KELG------LPYPVLLDPDGELAKAYGVR-------GIPTTVLIDKDGKIVA--RHVGPLSPEELEEALEKL 136
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 46-173 3.56e-10

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: 55.63  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  46 APDFELLNTEGKMISLKELTKKTpvvmLVLRGWPGKQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAElltEHAK-- 121
Cdd:cd02971     2 APDFTLPATDGGEVSLSDFKGKW----VVLFFYPKDFTPVCTTELCAFRDLAEEFAKggAEVLGVSVDSPF---SHKAwa 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1722220843 122 EFQGSQTFPanyhFVLDPDYKFTNDWGLRWD--APYETAYPSTFVVNEDQKILF 173
Cdd:cd02971    75 EKEGGLNFP----LLSDPDGEFAKAYGVLIEksAGGGLAARATFIIDPDGKIRY 124
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 40-108 1.13e-08

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: 51.89  E-value: 1.13e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722220843  40 PKVGQEAPDFELLNTEGKMISLKELTKKTPVVmLVLrgWPGKQCPLCSRQVGEFVSKQSEFDEVQVVMI 108
Cdd:cd03018     1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKPVV-LVF--FPLAFTPVCTKELCALRDSLELFEAAGAEVL 66
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 44-173 4.25e-08

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 49.85  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  44 QEAPDFELLNTEGKMISLKELTKKTpvvmLVLRGWPGKQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAElltEHAK 121
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRGKP----VVLYFYPKDDTPGCTKEACDFRDLYEEFKAlgAVVIGVSPDSVE---SHAK 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1722220843 122 eFQGSQTFPanyhFVL--DPDYKFTNDWGLRWDAPYETAYP--STFVVNEDQKILF 173
Cdd:cd03017    74 -FAEKYGLP----FPLlsDPDGKLAKAYGVWGEKKKKYMGIerSTFLIDPDGKIVK 124
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 48-173 1.63e-07

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: 48.00  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  48 DFELLNTEGKMISLKELTKKtpVVMLVLRG-WpgkqCPLCSRQVGEF--VSKQSEFDEVQVVMI---YPGPAElltehAK 121
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGK--VVLVNFWAsW----CPPCRAEMPELeaLAKEYKDDGVEVVGVnvdDDDPAA-----VK 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1722220843 122 EFqgSQTFPANYHFVLDPDYKFTNDWGLRwdapyetAYPSTFVVNEDQKILF 173
Cdd:cd02966    70 AF--LKKYGITFPVLLDPDGELAKAYGVR-------GLPTTFLIDRDGRIRA 112
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
 41-108 4.45e-07

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: 47.19  E-value: 4.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1722220843  41 KVGQEAPDFELLNTEGKMISLKELTKKTpVVMLVLrgwPGKQCPLCSRQVGEFVSKQSEFDEVQVVMI 108
Cdd:cd03014     1 KVGDKAPDFTLVTSDLSEVSLADFAGKV-KVISVF---PSIDTPVCATQTKRFNKEAAKLDNTVVLTI 64
Tpx COG2077
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
38-108 9.76e-07

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441680  Cd Length: 168  Bit Score: 46.62  E-value: 9.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722220843  38 HPPKVGQEAPDFELLNTEGKMISLKELTKKtPVVMLVLrgwPGKQCPLCSRQVGEFVSKQSEFDEVQVVMI 108
Cdd:COG2077    16 NLPKVGDKAPDFTLVDTDLSDVTLSDFAGK-RKVLNIV---PSLDTPVCATSTRKFNEEAAKLDNVVVLTI 82
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
41-171 4.87e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 44.99  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  41 KVGQEAPDFELLNTEGKMISLKELTKKTpvVMLVLrgWpGKQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELLTE 118
Cdd:PRK03147   36 QVGKEAPNFVLTDLEGKKIELKDLKGKG--VFLNF--W-GTWCKPCEKEMPYMNELYPKYKEkgVEIIAVNVDETELAVK 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1722220843 119 H-AKEFQgsQTFPAnyhfVLDPDYKFTNDWGLrwdapyeTAYPSTFVVNEDQKI 171
Cdd:PRK03147  111 NfVNRYG--LTFPV----AIDKGRQVIDAYGV-------GPLPTTFLIDKDGKV 151
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 43-193 5.58e-06

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: 44.54  E-value: 5.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  43 GQEAPDFELLNTEGKMISLKELTKKTPVVMLVLrgwpGKQCPLCSRQVGEFV--SKQSEFDEVQVVMI-------YP--G 111
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFI----CNHCPYVKAIEDRLNrlAKEYGAKGVAVVAInsndieaYPedS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843 112 PAELLtEHAKEFQgsqtfpANYHFVLDPdykfTNDWGLRWDApyeTAYPSTFVVNEDQKILF-------GKTVVSHGDRA 184
Cdd:cd02969    77 PENMK-AKAKEHG------YPFPYLLDE----TQEVAKAYGA---ACTPDFFLFDPDGKLVYrgriddsRPGNDPPVTGR 142


                  ....*....
gi 1722220843 185 DVATVVAEL 193
Cdd:cd02969   143 DLRAALDAL 151
tpx PRK00522
thiol peroxidase;
40-108 6.28e-05

thiol peroxidase;


Pssm-ID: 179055  Cd Length: 167  Bit Score: 41.43  E-value: 6.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722220843  40 PKVGQEAPDFELLNTEGKMISLKELTKKTPVVMLVlrgwPGKQCPLCSRQVGEFVSKQSEFDEVQVVMI 108
Cdd:PRK00522   18 PQVGDKAPDFTLVANDLSDVSLADFAGKRKVLNIF----PSIDTGVCATSVRKFNQEAAELDNTVVLCI 82
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 39-171 3.86e-03

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 36.45  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  39 PPKVGQEAPDFELLNTEGKMISLKELTKKTPVVMLvlrgWPGKQCPLCSRQVGEFVSKQSEFDE--VQVVMIYPGPAELL 116
Cdd:PRK09437    3 PLKAGDIAPKFSLPDQDGEQVSLTDFQGQRVLVYF----YPKAMTPGCTVQACGLRDNMDELKKagVVVLGISTDKPEKL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722220843 117 TEHA-KEFqgsqtfpANYHFVLDPDYKFTNDWGLrWDAP------YETAYPSTFVVNEDQKI 171
Cdd:PRK09437   79 SRFAeKEL-------LNFTLLSDEDHQVAEQFGV-WGEKkfmgktYDGIHRISFLIDADGKI 132
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 39-108 3.93e-03

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 36.75  E-value: 3.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722220843  39 PPKVGQEAPDFELLNTEGKmISLKELTKKtpvvMLVLRGWPGKQCPLCSRQVGEFVSKQSEFDEVQVVMI 108
Cdd:PRK13190    1 PVKLGQKAPDFTVNTTKGP-IDLSKYKGK----WVLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELV 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH