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Conserved domains on  [gi|2124041428|ref|WP_226990982|]
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thioredoxin family protein [Melioribacter roseus]

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];
31-241 1.18e-85

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


:

Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 253.13  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  31 MYIDDQLKEELQKVLSVLTKDVKIVFFTQEleCQYCRETKGILTELADINDRLHLEVKNFVNdkadaekygVDKIPATVL 110
Cdd:COG3634     2 AMLDDELKAQLKEYLEKLKNPVELVLFLDD--CEKSEELRELLEEIASLSDKISLEVYDKDD---------VERAPSFAI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 111 LDeNGKDYGIRYYGIPSGYEFASLLEDIKMLGTGVTGLPQEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYLN 190
Cdd:COG3634    71 LR-DGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLN 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2124041428 191 DNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEGAAPEQTVLEKVKE 241
Cdd:COG3634   150 PNITHEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
 
Name Accession Description Interval E-value
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
31-241 1.18e-85

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 253.13  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  31 MYIDDQLKEELQKVLSVLTKDVKIVFFTQEleCQYCRETKGILTELADINDRLHLEVKNFVNdkadaekygVDKIPATVL 110
Cdd:COG3634     2 AMLDDELKAQLKEYLEKLKNPVELVLFLDD--CEKSEELRELLEEIASLSDKISLEVYDKDD---------VERAPSFAI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 111 LDeNGKDYGIRYYGIPSGYEFASLLEDIKMLGTGVTGLPQEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYLN 190
Cdd:COG3634    71 LR-DGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLN 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2124041428 191 DNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEGAAPEQTVLEKVKE 241
Cdd:COG3634   150 PNITHEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 36-242 1.91e-84

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: 250.82  E-value: 1.91e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  36 QLKEELQKVLsvlTKDVKIVFFTQELE--CQYCRETKGILTELADINDRLHLEVKNF--VNDKADAEKYGVDKIPATVLL 111
Cdd:TIGR02187   8 ILKELFLKEL---KNPVEIVVFTDNDKegCQYCKETEQLLEELSEVSPKLKLEIYDFdtPEDKEEAEKYGVERVPTTIIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 112 DEnGKDYGIRYYGIPSGYEFASLLEDIKMLGTGVTGLPQEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYLND 191
Cdd:TIGR02187  85 EE-GKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALAND 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2124041428 192 NIKSDMVEATEFPHLSQKYNVRGVPRTVINES-AFLEGAAPEQTVLEKVKEA 242
Cdd:TIGR02187 164 KILGEMIEANENPDLAEKYGVMSVPKIVINKGvEEFVGAYPEEQFLEYILSA 215
PfPDO_like_N cd02975
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ...
 36-142 9.41e-38

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: 128.28  E-value: 9.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  36 QLKEELQKVLsvlTKDVKIVFFTQELECQYCRETKGILTELADINDRLHLEVKNFVNDKADAEKYGVDKIPATVLLDENG 115
Cdd:cd02975    10 ALKEEFFKEM---KNPVDLVVFSSKEGCQYCEVTKQLLEELSELSDKLKLEIYDFDEDKEKAEKYGVERVPTTIFLQDGG 86

                          90       100
                  ....*....|....*....|....*..
gi 2124041428 116 KDYGIRYYGIPSGYEFASLLEDIKMLG 142
Cdd:cd02975    87 KDGGIRYYGLPAGYEFASLIEDIVRVS 113
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 34-239 2.61e-18

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 83.28  E-value: 2.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  34 DDQLKEELQKVLSVLTKDVKIVFFTQELECQycRETKGILTELADINDRLHLEvknfvNDKADAEKygvdkipATVLLDE 113
Cdd:PRK15317    3 DANLKTQLKQYLELLERPIELVASLDDSEKS--AELKELLEEIASLSDKITVE-----EDSLDVRK-------PSFSITR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 114 NGKDYGIRYYGIPSGYEFASLLedIKMLGTGvtGLP----QEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYL 189
Cdd:PRK15317   69 PGEDTGVRFAGIPMGHEFTSLV--LALLQVG--GHPpkldQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVL 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2124041428 190 NDNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEGAAPEQTVLEKV 239
Cdd:PRK15317  145 NPNITHTMIDGALFQDEVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKL 194
Thioredoxin_3 pfam13192
Thioredoxin domain;
169-232 1.56e-11

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 58.38  E-value: 1.56e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124041428 169 VTPTCPYCPQaVITAHKFAYLNDNIKSDMVEATEFPHLSqKYNVRGVPRTVINESAFLEGAAPE 232
Cdd:pfam13192   1 LGPGCPKCPQ-LEKAVKEAAAELGIDAEVEKVTDFPEIA-KYGVMSTPALVINGKVVSSGKVPS 62
 
Name Accession Description Interval E-value
AhpF COG3634
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
31-241 1.18e-85

Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];


Pssm-ID: 442851 [Multi-domain]  Cd Length: 200  Bit Score: 253.13  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  31 MYIDDQLKEELQKVLSVLTKDVKIVFFTQEleCQYCRETKGILTELADINDRLHLEVKNFVNdkadaekygVDKIPATVL 110
Cdd:COG3634     2 AMLDDELKAQLKEYLEKLKNPVELVLFLDD--CEKSEELRELLEEIASLSDKISLEVYDKDD---------VERAPSFAI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 111 LDeNGKDYGIRYYGIPSGYEFASLLEDIKMLGTGVTGLPQEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYLN 190
Cdd:COG3634    71 LR-DGEDTGIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLN 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2124041428 191 DNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEGAAPEQTVLEKVKE 241
Cdd:COG3634   150 PNITHEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 36-242 1.91e-84

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: 250.82  E-value: 1.91e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  36 QLKEELQKVLsvlTKDVKIVFFTQELE--CQYCRETKGILTELADINDRLHLEVKNF--VNDKADAEKYGVDKIPATVLL 111
Cdd:TIGR02187   8 ILKELFLKEL---KNPVEIVVFTDNDKegCQYCKETEQLLEELSEVSPKLKLEIYDFdtPEDKEEAEKYGVERVPTTIIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 112 DEnGKDYGIRYYGIPSGYEFASLLEDIKMLGTGVTGLPQEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYLND 191
Cdd:TIGR02187  85 EE-GKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALAND 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2124041428 192 NIKSDMVEATEFPHLSQKYNVRGVPRTVINES-AFLEGAAPEQTVLEKVKEA 242
Cdd:TIGR02187 164 KILGEMIEANENPDLAEKYGVMSVPKIVINKGvEEFVGAYPEEQFLEYILSA 215
PfPDO_like_N cd02975
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ...
 36-142 9.41e-38

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: 128.28  E-value: 9.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  36 QLKEELQKVLsvlTKDVKIVFFTQELECQYCRETKGILTELADINDRLHLEVKNFVNDKADAEKYGVDKIPATVLLDENG 115
Cdd:cd02975    10 ALKEEFFKEM---KNPVDLVVFSSKEGCQYCEVTKQLLEELSELSDKLKLEIYDFDEDKEKAEKYGVERVPTTIFLQDGG 86

                          90       100
                  ....*....|....*....|....*..
gi 2124041428 116 KDYGIRYYGIPSGYEFASLLEDIKMLG 142
Cdd:cd02975    87 KDGGIRYYGLPAGYEFASLIEDIVRVS 113
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 163-229 2.45e-26

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: 97.26  E-value: 2.45e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124041428 163 VHMQVFVTPTCPYCPQAVITAHKFAYLNDNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEGA 229
Cdd:cd02973     1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 34-239 2.61e-18

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 83.28  E-value: 2.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  34 DDQLKEELQKVLSVLTKDVKIVFFTQELECQycRETKGILTELADINDRLHLEvknfvNDKADAEKygvdkipATVLLDE 113
Cdd:PRK15317    3 DANLKTQLKQYLELLERPIELVASLDDSEKS--AELKELLEEIASLSDKITVE-----EDSLDVRK-------PSFSITR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 114 NGKDYGIRYYGIPSGYEFASLLedIKMLGTGvtGLP----QEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYL 189
Cdd:PRK15317   69 PGEDTGVRFAGIPMGHEFTSLV--LALLQVG--GHPpkldQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVL 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2124041428 190 NDNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEGAAPEQTVLEKV 239
Cdd:PRK15317  145 NPNITHTMIDGALFQDEVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKL 194
AhpF_NTD_C cd03026
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ...
 150-228 7.40e-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: 62.31  E-value: 7.40e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124041428 150 QEIEEEVKKIDKPVHMQVFVTPTCPYCPQAVITAHKFAYLNDNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEG 228
Cdd:cd03026     1 EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFG 79
Thioredoxin_3 pfam13192
Thioredoxin domain;
169-232 1.56e-11

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 58.38  E-value: 1.56e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124041428 169 VTPTCPYCPQaVITAHKFAYLNDNIKSDMVEATEFPHLSqKYNVRGVPRTVINESAFLEGAAPE 232
Cdd:pfam13192   1 LGPGCPKCPQ-LEKAVKEAAAELGIDAEVEKVTDFPEIA-KYGVMSTPALVINGKVVSSGKVPS 62
AhpF_NTD_N cd02974
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ...
 34-135 1.78e-10

Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD forming two contiguous TRX-fold subdomain 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 N-terminal TRX-fold subdomain of AhpF NTD is redox inactive, but is proposed to contain an important residue that aids in the catalytic function of the redox-active CXXC motif contained in the C-terminal TRX-fold subdomain.


Pssm-ID: 239272 [Multi-domain]  Cd Length: 94  Bit Score: 56.05  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  34 DDQLKEELQKVLSVLTKDVKIVFFTQELECQycRETKGILTELADINDRLHLEVKNfvndkadaekyGVDKIPATVLLDE 113
Cdd:cd02974     3 DANLKQQLKAYLERLENPVELVASLDDSEKS--AELLELLEEIASLSDKITLEEDN-----------DDERKPSFSINRP 69

                          90       100
                  ....*....|....*....|..
gi 2124041428 114 nGKDYGIRYYGIPSGYEFASLL 135
Cdd:cd02974    70 -GEDTGIRFAGIPMGHEFTSLV 90
redox_disulf_1 TIGR00411
small redox-active disulfide protein 1; This protein is homologous to a family of proteins ...
 163-243 8.49e-08

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: 48.34  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 163 VHMQVFVTPTCPYCPQAVITAHKFAY-LNDNIKSDMVEATEFPHLSQKYNVRGVPRTVINESAFLEGAAPEQTVLEKVKE 241
Cdd:TIGR00411   1 VKIELFTSPTCPYCPAAKRVVEEVAKeMGDAVEVEYINVMENPQKAMEYGIMAVPAIVINGDVEFIGAPTKEELVEAIKK 80


                  ..
gi 2124041428 242 AL 243
Cdd:TIGR00411  81 RL 82
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 25-137 1.74e-06

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 47.30  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  25 NSIGEKMYiDDQLKEELQKVLSVLTKDVKIVFFtQELECQYCRETKGILTELAD----------INDRLHLEVKNFVNDK 94
Cdd:pfam13728 105 SNLARKAY-LAQRKEEREAALKSLAEEFGLIFF-YRGDCPYCEAQAPILQAFADkygwtvrpvsVDGRPLPGFPNYRVDN 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2124041428  95 ADAEKYGVDKIPATVLLDENGKDYgiryygIPSGYEFASL--LED 137
Cdd:pfam13728 183 GQAARLGVKRTPALFLVNPPSGDV------VPVAAGVLSLdeLEE 221
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 150-243 5.06e-06

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: 44.04  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 150 QEIEEEVKKIDKPVhMQVFVTPTCPYCPQ------AVITAH----KFAYLNdniksdmveATEFPHLSQKYNVRGVPrTV 219
Cdd:COG3118     8 ENFEEEVLESDKPV-LVDFWAPWCGPCKMlapvleELAAEYggkvKFVKVD---------VDENPELAAQFGVRSIP-TL 76

                          90       100
                  ....*....|....*....|....*....
gi 2124041428 220 I-----NESAFLEGAAPEQTVLEKVKEAL 243
Cdd:COG3118    77 LlfkdgQPVDRFVGALPKEQLREFLDKVL 105
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 167-233 1.01e-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: 42.37  E-value: 1.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124041428 167 VFVTPTCPYCPQA--VITAHKFAYLNDNIKSDMVEATEfphLSQKYNVRGVPRTVINESAfLEGAAPEQ 233
Cdd:TIGR02196   4 VYTTPWCPPCVKAkeYLTSKGVAFEEIDVEKDAAAREE---LLKVYGQRGVPVIVIGHKI-VVGFDPEK 68
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 63-138 3.34e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 39.67  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  63 CQYCRETKGILTELADINDRLHL----------EVKNFVNDKAD------------AEKYGVDKIPATVLLDENGKdygI 120
Cdd:COG0526    40 CPPCRAEMPVLKELAEEYGGVVFvgvdvdenpeAVKAFLKELGLpypvlldpdgelAKAYGVRGIPTTVLIDKDGK---I 116

                          90       100
                  ....*....|....*....|
gi 2124041428 121 RY--YGIPSGYEFASLLEDI 138
Cdd:COG0526   117 VArhVGPLSPEELEEALEKL 136
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
167-222 6.82e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.48  E-value: 6.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2124041428 167 VFVTPTCPYCPQA--VITAHKFAYLNDNIKSDMVEATEfphLSQKYNVRGVPRTVINE 222
Cdd:COG0695     4 LYTTPGCPYCARAkrLLDEKGIPYEEIDVDEDPEAREE---LRERSGRRTVPVIFIGG 58
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 165-221 9.82e-04

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 36.91  E-value: 9.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 165 MQVFVTPTCPYCPQAVITAHKFAYLNDNIKSDMVEATEFPHL---SQKYNVRGVPRTVIN 221
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALekeLKRYGVGGVPTLVVF 60
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 55-120 1.20e-03

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: 36.39  E-value: 1.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124041428  55 VFFTqeLECQYCRETKGILTELADINDRLHLEVKNFVNDKADAEKYGVDKIPATVLldeNGKDYGI 120
Cdd:cd02973     5 VFVS--PTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVI---NGKVEFV 65
Thioredoxin_3 pfam13192
Thioredoxin domain;
63-136 2.26e-03

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 35.65  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124041428  63 CQYCRETKGILTELADiNDRLHLEVKNfVNDKADAEKYGVDKIPATVLldeNGKdygIRYYG-IPSGYEFASLLE 136
Cdd:pfam13192   5 CPKCPQLEKAVKEAAA-ELGIDAEVEK-VTDFPEIAKYGVMSTPALVI---NGK---VVSSGkVPSEEEIRKLLE 71
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 167-225 2.37e-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: 35.66  E-value: 2.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124041428 167 VFVTPTCPYCPQA--VITAHKFAYLNDNIKSDMVEATEfphLSQKYNVRGVPRTVINESAF 225
Cdd:cd02976     4 VYTKPDCPYCKATkrFLDERGIPFEEVDVDEDPEALEE---LKKLNGYRSVPVVVIGDEHL 61
Glutaredoxin pfam00462
Glutaredoxin;
167-222 3.09e-03

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 35.17  E-value: 3.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2124041428 167 VFVTPTCPYCPQAV--ITAHKFAYLNDNIKSDMVEATEfphLSQKYNVRGVPRTVINE 222
Cdd:pfam00462   3 LYTKPTCPFCKRAKrlLKSLGVDFEEIDVDEDPEIREE---LKELSGWPTVPQVFIDG 57
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 54-139 7.62e-03

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 36.04  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428  54 IVFFTQElECQYCRET-KGILT--ELAD-INDRLHL---------EVKNF----VNDKADAEKYGVDKIPATVLLDENGK 116
Cdd:COG2143    44 LLFFESD-WCPYCKKLhKEVFSdpEVAAyLKENFVVvqldaegdkEVTDFdgetLTEKELARKYGVRGTPTLVFFDAEGK 122

                          90       100
                  ....*....|....*....|...
gi 2124041428 117 DYGiRYYGIPSGYEFASLLEDIK 139
Cdd:COG2143   123 EIA-RIPGYLKPETFLALLKYVA 144
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 150-240 8.07e-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: 34.84  E-value: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124041428 150 QEIEEEVKKiDKPVhmqV--FVTPTCPYCPQA--VItaHKFAYLNDNIKSDMVEATEFPHLSQKYNVRGVPrTVI----- 220
Cdd:cd02947     1 EEFEELIKS-AKPV---VvdFWAPWCGPCKAIapVL--EELAEEYPKVKFVKVDVDENPELAEEYGVRSIP-TFLffkng 73

                          90       100
                  ....*....|....*....|
gi 2124041428 221 NESAFLEGAAPEQTVLEKVK 240
Cdd:cd02947    74 KEVDRVVGADPKEELEEFLE 93
 
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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