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Conserved domains on  [gi|503031152|ref|WP_013266128|]
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thioredoxin family protein [Acidilobus saccharovorans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlrX_arch super family cl27120
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 10-228 1.62e-77

Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.


The actual alignment was detected with superfamily member TIGR02187:

Pssm-ID: 274021 [Multi-domain]  Cd Length: 215  Bit Score: 233.11  E-value: 1.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152   10 LDEELIKELKDT-LAYMVSPVTVDLFID-DASRCETCEDAYKLVKTIADASPvrdgkkMLQLRVFSKSKPEDLEEFKRQN 87
Cdd:TIGR02187   1 LSEEDREILKELfLKELKNPVEIVVFTDnDKEGCQYCKETEQLLEELSEVSP------KLKLEIYDFDTPEDKEEAEKYG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152   88 VERVPTVTLLG----GVIRYTGTPAGEEIRGFIETIMRISEGESGLDPETKKQLASLKGSVHIETVVTPSCPYCPYAALL 163
Cdd:TIGR02187  75 VERVPTTIILEegkdGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLM 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503031152  164 ANMFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALN-GVMSFIGVPYEEDFINYVVAA 228
Cdd:TIGR02187 155 AHKFALA-----NDKILGEMIEANENPDLAEKYGVMSVPKIVINkGVEEFVGAYPEEQFLEYILSA 215
 
Name Accession Description Interval E-value
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 10-228 1.62e-77

Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.


Pssm-ID: 274021 [Multi-domain]  Cd Length: 215  Bit Score: 233.11  E-value: 1.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152   10 LDEELIKELKDT-LAYMVSPVTVDLFID-DASRCETCEDAYKLVKTIADASPvrdgkkMLQLRVFSKSKPEDLEEFKRQN 87
Cdd:TIGR02187   1 LSEEDREILKELfLKELKNPVEIVVFTDnDKEGCQYCKETEQLLEELSEVSP------KLKLEIYDFDTPEDKEEAEKYG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152   88 VERVPTVTLLG----GVIRYTGTPAGEEIRGFIETIMRISEGESGLDPETKKQLASLKGSVHIETVVTPSCPYCPYAALL 163
Cdd:TIGR02187  75 VERVPTTIILEegkdGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLM 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503031152  164 ANMFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALN-GVMSFIGVPYEEDFINYVVAA 228
Cdd:TIGR02187 155 AHKFALA-----NDKILGEMIEANENPDLAEKYGVMSVPKIVINkGVEEFVGAYPEEQFLEYILSA 215
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
10-225 1.63e-70

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 214.61  E-value: 1.63e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  10 LDEELIKELKDTLAYMVSPVTVDLFIDDasrCETCEDAYKLVKTIADASPvrdgkkMLQLRVFSKSkpedleefkrqNVE 89
Cdd:COG3634    4 LDDELKAQLKEYLEKLKNPVELVLFLDD---CEKSEELRELLEEIASLSD------KISLEVYDKD-----------DVE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  90 RVPTVTLL----GGVIRYTGTPAGEEIRGFIETIMRISEGESGLDPETKKQLASLKGSVHIETVVTPSCPYCPYAALLAN 165
Cdd:COG3634   64 RAPSFAILrdgeDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALN 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152 166 MFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALNGVMSFIGVPYEEDFINYV 225
Cdd:COG3634  144 LMAVL-----NPNITHEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKL 198
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 144-215 5.10e-25

Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.


Pssm-ID: 239271 [Multi-domain]  Cd Length: 67  Bit Score: 93.79  E-value: 5.10e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503031152 144 VHIETVVTPSCPYCPYAALLANMFAyeswkQNNPKVISDTVEAYENMDIAEKYGVMSVPAIALNGVMSFIGV 215
Cdd:cd02973    1 VNIEVFVSPTCPYCPDAVQAANRIA-----ALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 10-208 1.45e-10

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 60.56  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  10 LDEELIKELKDTLAYMVSPVTVDLFIDDAsrcETCEDAYKLVKTIADASPvrdgkkMLQLRvfskskpedleefKRQNVE 89
Cdd:PRK15317   2 LDANLKTQLKQYLELLERPIELVASLDDS---EKSAELKELLEEIASLSD------KITVE-------------EDSLDV 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  90 RVPTVTLL----GGVIRYTGTPAGEEIRGFIETIMRISEGESGLDPETKKQLASLKGSVHIETVVTPSCPYCP--YAALl 163
Cdd:PRK15317  60 RKPSFSITrpgeDTGVRFAGIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPdvVQAL- 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 503031152 164 aNMFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALNG 208
Cdd:PRK15317 139 -NLMAVL-----NPNITHTMIDGALFQDEVEARNIMAVPTVFLNG 177
Thioredoxin_3 pfam13192
Thioredoxin domain;
150-225 1.86e-08

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 49.91  E-value: 1.86e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503031152  150 VTPSCPYCPyaaLLANMFAYESWKQNnpkvISDTVEAYENMDIAEKYGVMSVPAIALNGVMSFIG-VPYEEDFINYV 225
Cdd:pfam13192   1 LGPGCPKCP---QLEKAVKEAAAELG----IDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGkVPSEEEIRKLL 70
 
Name Accession Description Interval E-value
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 10-228 1.62e-77

Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.


Pssm-ID: 274021 [Multi-domain]  Cd Length: 215  Bit Score: 233.11  E-value: 1.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152   10 LDEELIKELKDT-LAYMVSPVTVDLFID-DASRCETCEDAYKLVKTIADASPvrdgkkMLQLRVFSKSKPEDLEEFKRQN 87
Cdd:TIGR02187   1 LSEEDREILKELfLKELKNPVEIVVFTDnDKEGCQYCKETEQLLEELSEVSP------KLKLEIYDFDTPEDKEEAEKYG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152   88 VERVPTVTLLG----GVIRYTGTPAGEEIRGFIETIMRISEGESGLDPETKKQLASLKGSVHIETVVTPSCPYCPYAALL 163
Cdd:TIGR02187  75 VERVPTTIILEegkdGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLM 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503031152  164 ANMFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALN-GVMSFIGVPYEEDFINYVVAA 228
Cdd:TIGR02187 155 AHKFALA-----NDKILGEMIEANENPDLAEKYGVMSVPKIVINkGVEEFVGAYPEEQFLEYILSA 215
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
10-225 1.63e-70

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 214.61  E-value: 1.63e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  10 LDEELIKELKDTLAYMVSPVTVDLFIDDasrCETCEDAYKLVKTIADASPvrdgkkMLQLRVFSKSkpedleefkrqNVE 89
Cdd:COG3634    4 LDDELKAQLKEYLEKLKNPVELVLFLDD---CEKSEELRELLEEIASLSD------KISLEVYDKD-----------DVE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  90 RVPTVTLL----GGVIRYTGTPAGEEIRGFIETIMRISEGESGLDPETKKQLASLKGSVHIETVVTPSCPYCPYAALLAN 165
Cdd:COG3634   64 RAPSFAILrdgeDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALN 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152 166 MFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALNGVMSFIGVPYEEDFINYV 225
Cdd:COG3634  144 LMAVL-----NPNITHEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKL 198
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 144-215 5.10e-25

Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.


Pssm-ID: 239271 [Multi-domain]  Cd Length: 67  Bit Score: 93.79  E-value: 5.10e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503031152 144 VHIETVVTPSCPYCPYAALLANMFAyeswkQNNPKVISDTVEAYENMDIAEKYGVMSVPAIALNGVMSFIGV 215
Cdd:cd02973    1 VNIEVFVSPTCPYCPDAVQAANRIA-----ALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
PfPDO_like_N cd02975
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ...
 10-123 6.83e-21

Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions.


Pssm-ID: 239273 [Multi-domain]  Cd Length: 113  Bit Score: 84.36  E-value: 6.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  10 LDEELIKELKD-TLAYMVSPVTVDLFIDdASRCETCEDAYKLVKTIADASPvrdgkkMLQLRVFSKSkpEDLEEFKRQNV 88
Cdd:cd02975    3 LSDEDRKALKEeFFKEMKNPVDLVVFSS-KEGCQYCEVTKQLLEELSELSD------KLKLEIYDFD--EDKEKAEKYGV 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503031152  89 ERVPTVTLL-----GGVIRYTGTPAGEEIRGFIETIMRIS 123
Cdd:cd02975   74 ERVPTTIFLqdggkDGGIRYYGLPAGYEFASLIEDIVRVS 113
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 10-208 1.45e-10

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 60.56  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  10 LDEELIKELKDTLAYMVSPVTVDLFIDDAsrcETCEDAYKLVKTIADASPvrdgkkMLQLRvfskskpedleefKRQNVE 89
Cdd:PRK15317   2 LDANLKTQLKQYLELLERPIELVASLDDS---EKSAELKELLEEIASLSD------KITVE-------------EDSLDV 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152  90 RVPTVTLL----GGVIRYTGTPAGEEIRGFIETIMRISEGESGLDPETKKQLASLKGSVHIETVVTPSCPYCP--YAALl 163
Cdd:PRK15317  60 RKPSFSITrpgeDTGVRFAGIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPdvVQAL- 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 503031152 164 aNMFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALNG 208
Cdd:PRK15317 139 -NLMAVL-----NPNITHTMIDGALFQDEVEARNIMAVPTVFLNG 177
Thioredoxin_3 pfam13192
Thioredoxin domain;
150-225 1.86e-08

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 49.91  E-value: 1.86e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503031152  150 VTPSCPYCPyaaLLANMFAYESWKQNnpkvISDTVEAYENMDIAEKYGVMSVPAIALNGVMSFIG-VPYEEDFINYV 225
Cdd:pfam13192   1 LGPGCPKCP---QLEKAVKEAAAELG----IDAEVEKVTDFPEIAKYGVMSTPALVINGKVVSSGkVPSEEEIRKLL 70
AhpF_NTD_C cd03026
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ...
 132-208 8.47e-08

TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.


Pssm-ID: 239324 [Multi-domain]  Cd Length: 89  Bit Score: 48.83  E-value: 8.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503031152 132 ETKKQLASLKGSVHIETVVTPSCPYCPYAALLANMFAYEswkqnNPKVISDTVEAYENMDIAEKYGVMSVPAIALNG 208
Cdd:cd03026    2 DLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVL-----NPNIEHEMIDGALFQDEVEERGIMSVPAIFLNG 73
Thioredoxin_3 pfam13192
Thioredoxin domain;
39-117 2.74e-03

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 35.65  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152   39 SRCETCEDAYKLVKTIADASPVRdgkkmlqlrvFSKSKPEDLEEFKRQNVERVPTVtLLGGVIRYTGT-PAGEEIRGFIE 117
Cdd:pfam13192   3 PGCPKCPQLEKAVKEAAAELGID----------AEVEKVTDFPEIAKYGVMSTPAL-VINGKVVSSGKvPSEEEIRKLLE 71
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 151-225 2.96e-03

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: 36.00  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503031152 151 TPSCPYCpyaallaNMFA--YESWKQNNPKVISDTVEAYENMDIAEKYGVMSVPAIAL--NG--VMSFIGVPYEEDFINY 224
Cdd:cd02947   19 APWCGPC-------KAIApvLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFfkNGkeVDRVVGADPKEELEEF 91


                 .
gi 503031152 225 V 225
Cdd:cd02947   92 L 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 173-221 5.53e-03

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: 35.57  E-value: 5.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503031152 173 KQNNPKVISDTVEAYENMDIAEKYGVMSVPAIAL--NG--VMSFIGVPYEEDF 221
Cdd:COG3118   45 AEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLfkDGqpVDRFVGALPKEQL 97
 
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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