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Conserved domains on  [gi|1482770757|ref|WP_119821342|]
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thioredoxin family protein [Halalkaliarchaeum desulfuricum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
1-210 2.49e-75

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


:

Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 225.39  E-value: 2.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   1 MSLLTDENKRQIGELLERMDEPVTIHTFTDDCETCEECLEFNREMAETSELLSVEEHEFDGEaaeeygatkyDHGP-VQV 79
Cdd:COG3634     1 MAMLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEVYDKDDV----------ERAPsFAI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757  80 LEGGDVSGVNYFGLPTGQEINSYITDIVELSTGDPDLSVDLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRFAMVNE 159
Cdd:COG3634    71 LRDGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNP 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1482770757 160 HVTGEMIQSQEFMEVAQEYGVRGVPQINVNGsDGEFTGNLPPQQFLSEVKN 210
Cdd:COG3634   151 NITHEMIDGAEFPDEAEKYGVMSVPTVVLNG-EVFFVGRMPEEEILEKLDT 200
 
Name Accession Description Interval E-value
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
1-210 2.49e-75

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 225.39  E-value: 2.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   1 MSLLTDENKRQIGELLERMDEPVTIHTFTDDCETCEECLEFNREMAETSELLSVEEHEFDGEaaeeygatkyDHGP-VQV 79
Cdd:COG3634     1 MAMLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEVYDKDDV----------ERAPsFAI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757  80 LEGGDVSGVNYFGLPTGQEINSYITDIVELSTGDPDLSVDLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRFAMVNE 159
Cdd:COG3634    71 LRDGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNP 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1482770757 160 HVTGEMIQSQEFMEVAQEYGVRGVPQINVNGsDGEFTGNLPPQQFLSEVKN 210
Cdd:COG3634   151 NITHEMIDGAEFPDEAEKYGVMSVPTVVLNG-EVFFVGRMPEEEILEKLDT 200
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 4-211 2.48e-59

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: 185.34  E-value: 2.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   4 LTDENKRQIGEL-LERMDEPVTIHTFTDD----CETCEECLEFNREMAETSELLSVEEHEFDG----EAAEEYGATKYDh 74
Cdd:TIGR02187   1 LSEEDREILKELfLKELKNPVEIVVFTDNdkegCQYCKETEQLLEELSEVSPKLKLEIYDFDTpedkEEAEKYGVERVP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757  75 gPVQVLEGGDVSGVNYFGLPTGQEINSYITDIVELSTGDPDLSVDLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRF 154
Cdd:TIGR02187  80 -TTIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKF 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1482770757 155 AMVNEHVTGEMIQSQEFMEVAQEYGVRGVPQINVNGSDGEFTGNLPPQQFLSEVKNA 211
Cdd:TIGR02187 159 ALANDKILGEMIEANENPDLAEKYGVMSVPKIVINKGVEEFVGAYPEEQFLEYILSA 215
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 131-197 4.67e-22

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: 85.31  E-value: 4.67e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482770757 131 VEITVFVTPTCPHCPGAVQTAHRFAMVNEHVTGEMIQSQEFMEVAQEYGVRGVPQINVNGSDgEFTG 197
Cdd:cd02973     1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKV-EFVG 66
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 3-190 1.87e-20

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 88.68  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   3 LLTDENKRQIGELLERMDEPVTIHTFTDDCETCEECLEFNREMAETSELLSVEEHEFDGEAAEeygatkydhgpVQVLEG 82
Cdd:PRK15317    1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLDVRKPS-----------FSITRP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757  83 GDVSGVNYFGLPTGQEINSYITDIVELSTGDPDLSVDLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRFAMVNEHVT 162
Cdd:PRK15317   70 GEDTGVRFAGIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNIT 149

                         170       180
                  ....*....|....*....|....*...
gi 1482770757 163 GEMIQSQEFMEVAQEYGVRGVPQINVNG 190
Cdd:PRK15317  150 HTMIDGALFQDEVEARNIMAVPTVFLNG 177
Thioredoxin_3 pfam13192
Thioredoxin domain;
137-208 4.74e-09

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 51.06  E-value: 4.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1482770757 137 VTPTCPHCPgAVQTAHRFAMVNEHVTGEMIQSQEFMEVAqEYGVRGVPQINVNGSDgEFTGNLPPQQFLSEV 208
Cdd:pfam13192   1 LGPGCPKCP-QLEKAVKEAAAELGIDAEVEKVTDFPEIA-KYGVMSTPALVINGKV-VSSGKVPSEEEIRKL 69
 
Name Accession Description Interval E-value
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
1-210 2.49e-75

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 225.39  E-value: 2.49e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   1 MSLLTDENKRQIGELLERMDEPVTIHTFTDDCETCEECLEFNREMAETSELLSVEEHEFDGEaaeeygatkyDHGP-VQV 79
Cdd:COG3634     1 MAMLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEVYDKDDV----------ERAPsFAI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757  80 LEGGDVSGVNYFGLPTGQEINSYITDIVELSTGDPDLSVDLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRFAMVNE 159
Cdd:COG3634    71 LRDGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNP 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1482770757 160 HVTGEMIQSQEFMEVAQEYGVRGVPQINVNGsDGEFTGNLPPQQFLSEVKN 210
Cdd:COG3634   151 NITHEMIDGAEFPDEAEKYGVMSVPTVVLNG-EVFFVGRMPEEEILEKLDT 200
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 4-211 2.48e-59

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: 185.34  E-value: 2.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   4 LTDENKRQIGEL-LERMDEPVTIHTFTDD----CETCEECLEFNREMAETSELLSVEEHEFDG----EAAEEYGATKYDh 74
Cdd:TIGR02187   1 LSEEDREILKELfLKELKNPVEIVVFTDNdkegCQYCKETEQLLEELSEVSPKLKLEIYDFDTpedkEEAEKYGVERVP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757  75 gPVQVLEGGDVSGVNYFGLPTGQEINSYITDIVELSTGDPDLSVDLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRF 154
Cdd:TIGR02187  80 -TTIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKF 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1482770757 155 AMVNEHVTGEMIQSQEFMEVAQEYGVRGVPQINVNGSDGEFTGNLPPQQFLSEVKNA 211
Cdd:TIGR02187 159 ALANDKILGEMIEANENPDLAEKYGVMSVPKIVINKGVEEFVGAYPEEQFLEYILSA 215
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 131-197 4.67e-22

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: 85.31  E-value: 4.67e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482770757 131 VEITVFVTPTCPHCPGAVQTAHRFAMVNEHVTGEMIQSQEFMEVAQEYGVRGVPQINVNGSDgEFTG 197
Cdd:cd02973     1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKV-EFVG 66
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 3-190 1.87e-20

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 88.68  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   3 LLTDENKRQIGELLERMDEPVTIHTFTDDCETCEECLEFNREMAETSELLSVEEHEFDGEAAEeygatkydhgpVQVLEG 82
Cdd:PRK15317    1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLDVRKPS-----------FSITRP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757  83 GDVSGVNYFGLPTGQEINSYITDIVELSTGDPDLSVDLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRFAMVNEHVT 162
Cdd:PRK15317   70 GEDTGVRFAGIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNIT 149

                         170       180
                  ....*....|....*....|....*...
gi 1482770757 163 GEMIQSQEFMEVAQEYGVRGVPQINVNG 190
Cdd:PRK15317  150 HTMIDGALFQDEVEARNIMAVPTVFLNG 177
PfPDO_like_N cd02975
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ...
 2-110 3.56e-18

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: 76.66  E-value: 3.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757   2 SLLTDENKRQIGEL-LERMDEPVTIHTFT--DDCETCEECLEFNREMAETSELLSVEEHEF--DGEAAEEYGATKYdhgP 76
Cdd:cd02975     1 GLLSDEDRKALKEEfFKEMKNPVDLVVFSskEGCQYCEVTKQLLEELSELSDKLKLEIYDFdeDKEKAEKYGVERV---P 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1482770757  77 VQVLEGGDVS--GVNYFGLPTGQEINSYITDIVELS 110
Cdd:cd02975    78 TTIFLQDGGKdgGIRYYGLPAGYEFASLIEDIVRVS 113
AhpF_NTD_C cd03026
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ...
 119-195 1.33e-13

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: 63.85  E-value: 1.33e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482770757 119 DLIEAVQEIDEPVEITVFVTPTCPHCPGAVQTAHRFAMVNEHVTGEMIQSQEFMEVAQEYGVRGVPQINVNGSDGEF 195
Cdd:cd03026     2 DLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGF 78
Thioredoxin_3 pfam13192
Thioredoxin domain;
137-208 4.74e-09

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 51.06  E-value: 4.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1482770757 137 VTPTCPHCPgAVQTAHRFAMVNEHVTGEMIQSQEFMEVAqEYGVRGVPQINVNGSDgEFTGNLPPQQFLSEV 208
Cdd:pfam13192   1 LGPGCPKCP-QLEKAVKEAAAELGIDAEVEKVTDFPEIA-KYGVMSTPALVINGKV-VSSGKVPSEEEIRKL 69
redox_disulf_1 TIGR00411
small redox-active disulfide protein 1; This protein is homologous to a family of proteins ...
 131-197 1.12e-07

small redox-active disulfide protein 1; This protein is homologous to a family of proteins that includes thioredoxins, glutaredoxins, protein-disulfide isomerases, and others, some of which have several such domains. The sequence of this protein at the redox-active disufide site, CPYC, matches glutaredoxins rather than thioredoxins, although its overall sequence seems closer to thioredoxins. It is suggested to be a ribonucleotide-reducing system component distinct from thioredoxin or glutaredoxin. [Unknown function, General]


Pssm-ID: 129505 [Multi-domain]  Cd Length: 82  Bit Score: 47.95  E-value: 1.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1482770757 131 VEITVFVTPTCPHCPGAVQTAHRFAM-VNEHVTGEMIQSQEFMEVAQEYGVRGVPQINVNGsDGEFTG 197
Cdd:TIGR00411   1 VKIELFTSPTCPYCPAAKRVVEEVAKeMGDAVEVEYINVMENPQKAMEYGIMAVPAIVING-DVEFIG 67
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
132-190 5.41e-06

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 42.88  E-value: 5.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482770757 132 EITVFVTPTCPHCPGAVQTAHR----FAMVNehVTGEMIQSQEFMEVaqeYGVRGVPQINVNG 190
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEkgipYEEID--VDEDPEAREELRER---SGRRTVPVIFIGG 58
Glutaredoxin pfam00462
Glutaredoxin;
133-190 1.02e-05

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 41.72  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1482770757 133 ITVFVTPTCPHCPGAVQTAHR----FAMVNehVTGEMIQSQEFMEVAqeyGVRGVPQINVNG 190
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSlgvdFEEID--VDEDPEIREELKELS---GWPTVPQVFIDG 57
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 133-191 3.47e-05

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 40.83  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482770757 133 ITVFVTPTCPHCPGAVQ--TAHRFAMVNEHVTGEMIQSQEFMEVaqeYGVRGVPQINVNGS 191
Cdd:TIGR02196   2 VKVYTTPWCPPCVKAKEylTSKGVAFEEIDVEKDAAAREELLKV---YGQRGVPVIVIGHK 59
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 119-212 2.03e-04

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: 39.42  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757 119 DLIEAVQEIDEPVeITVFVTPTCPHC----P--GAVQTAH----RFAMVNehvtgemiqSQEFMEVAQEYGVRGVPQINV 188
Cdd:COG3118     9 NFEEEVLESDKPV-LVDFWAPWCGPCkmlaPvlEELAAEYggkvKFVKVD---------VDENPELAAQFGVRSIPTLLL 78

                          90       100
                  ....*....|....*....|....*..
gi 1482770757 189 --NGSD-GEFTGNLPPQQFLSEVKNAL 212
Cdd:COG3118    79 fkDGQPvDRFVGALPKEQLREFLDKVL 105
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
133-205 8.13e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.40  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482770757 133 ITVFVTPTCPHC----------PG---AVQTAHRFAMVN----EHVTGEMIQSQEFMEVAQEYGVRGVPQI---NVNGSD 192
Cdd:pfam13098   8 LVVFTDPDCPYCkklkkelledPDvtvYLGPNFVFIAVNiwcaKEVAKAFTDILENKELGRKYGVRGTPTIvffDGKGEL 87

                          90
                  ....*....|...
gi 1482770757 193 GEFTGNLPPQQFL 205
Cdd:pfam13098  88 LRLPGYVPAEEFL 100
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 132-190 2.95e-03

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 35.28  E-value: 2.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482770757 132 EITVFVTPTCPHCPGAVQ--TAHRFAMVNEHVTGemiQSQEFMEVAQEYGVRGVPQINVNG 190
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRflDERGIPFEEVDVDE---DPEALEELKKLNGYRSVPVVVIGD 58
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 172-212 7.86e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 35.74  E-value: 7.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1482770757 172 MEVAQEYGVRGVPQINVNGSdgEFTGNLPPQQFLSEVKNAL 212
Cdd:COG1651   114 TALAQALGVTGTPTFVVNGK--LVSGAVPYEELEAALDAAL 152
 
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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