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Conserved domains on  [gi|18413101|ref|NP_567336|]
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Thioredoxin superfamily protein [Arabidopsis thaliana]

Protein Classification

glutaredoxin family protein( domain architecture ID 10530477)

glutaredoxin/thioredoxin family protein functions as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein thiol or disulfide bonds using an active site disulfide or dithiol, present in a CXXC motif

CATH:  3.40.30.10
PubMed:  11441809|11012661|14713336
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 35-122 3.53e-26

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


:

Pssm-ID: 399055  Cd Length: 80  Bit Score: 93.12  E-value: 3.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413101    35 LVLYSKPGCCLCDGLKEKLHAAFTLStgpdslnDVTLQVRDITTNPEWERAYQYEIPVLAKENSDgKEEVLPRLSPRLSA 114
Cdd:pfam05768   1 LTLYGKPGCGLCEGAEEVLEPLALEL-------GFELEVIDIDGDPELLAKYGLEIPVLAFVGIS-KFFNLEILSWRLDE 72


                  ....*...
gi 18413101   115 ELIQKKLL 122
Cdd:pfam05768  73 EQLAAELE 80
 
Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 35-122 3.53e-26

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


Pssm-ID: 399055  Cd Length: 80  Bit Score: 93.12  E-value: 3.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413101    35 LVLYSKPGCCLCDGLKEKLHAAFTLStgpdslnDVTLQVRDITTNPEWERAYQYEIPVLAKENSDgKEEVLPRLSPRLSA 114
Cdd:pfam05768   1 LTLYGKPGCGLCEGAEEVLEPLALEL-------GFELEVIDIDGDPELLAKYGLEIPVLAFVGIS-KFFNLEILSWRLDE 72


                  ....*...
gi 18413101   115 ELIQKKLL 122
Cdd:pfam05768  73 EQLAAELE 80
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
34-93 6.57e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 35.94  E-value: 6.57e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18413101  34 KLVLYSKPGCCLCDGLKEKLHAaftlstgpdslNDVTLQVRDITTNPE-----WERAYQYEIPVL 93
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDE-----------KGIPYEEIDVDEDPEareelRERSGRRTVPVI 54
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 34-93 9.57e-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: 32.58  E-value: 9.57e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18413101  34 KLVLYSKPGCCLCDGLKEKLhaaftlstgpDSLNdVTLQVRDITTNPEWERAYQYE-----IPVL 93
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFL----------DERG-IPFEEVDVDEDPEALEELKKLngyrsVPVV 54
 
Name Accession Description Interval E-value
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 35-122 3.53e-26

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


Pssm-ID: 399055  Cd Length: 80  Bit Score: 93.12  E-value: 3.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413101    35 LVLYSKPGCCLCDGLKEKLHAAFTLStgpdslnDVTLQVRDITTNPEWERAYQYEIPVLAKENSDgKEEVLPRLSPRLSA 114
Cdd:pfam05768   1 LTLYGKPGCGLCEGAEEVLEPLALEL-------GFELEVIDIDGDPELLAKYGLEIPVLAFVGIS-KFFNLEILSWRLDE 72


                  ....*...
gi 18413101   115 ELIQKKLL 122
Cdd:pfam05768  73 EQLAAELE 80
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
34-93 6.57e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 35.94  E-value: 6.57e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18413101  34 KLVLYSKPGCCLCDGLKEKLHAaftlstgpdslNDVTLQVRDITTNPE-----WERAYQYEIPVL 93
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDE-----------KGIPYEEIDVDEDPEareelRERSGRRTVPVI 54
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 34-93 9.57e-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: 32.58  E-value: 9.57e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18413101  34 KLVLYSKPGCCLCDGLKEKLhaaftlstgpDSLNdVTLQVRDITTNPEWERAYQYE-----IPVL 93
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFL----------DERG-IPFEEVDVDEDPEALEELKKLngyrsVPVV 54
 
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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