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Conserved domains on  [gi|259466685|emb|CBF61763|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

glutaredoxin( domain architecture ID 10020367)

glutaredoxin is a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 4-102 3.80e-58

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


:

Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 173.79  E-value: 3.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685    4 IQKMISEKSVVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMS 83
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80

                          90
                  ....*....|....*....
gi 259466685   84 LHLNRSLIPMLKRFGALWL 102
Cdd:TIGR02189  81 LHISGSLVPMLKQAGALWL 99
 
Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 4-102 3.80e-58

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 173.79  E-value: 3.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685    4 IQKMISEKSVVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMS 83
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80

                          90
                  ....*....|....*....
gi 259466685   84 LHLNRSLIPMLKRFGALWL 102
Cdd:TIGR02189  81 LHISGSLVPMLKQAGALWL 99
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 13-93 2.85e-35

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 115.33  E-value: 2.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685  13 VVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMSLHLNRSLIP 92
Cdd:cd03419    2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVK 81


                 .
gi 259466685  93 M 93
Cdd:cd03419   82 L 82
Glutaredoxin pfam00462
Glutaredoxin;
13-75 3.55e-13

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 58.67  E-value: 3.55e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259466685   13 VVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEInrgKEIEYALAQLGCSPTVPVVFIGGQLV 75
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDED---PEIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
13-77 1.89e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 36.71  E-value: 1.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259466685  13 VVIFSNNSC--CmsHTIKTLFLDLGVNPTIYELDEINRGKEieyALAQLGCSPTVPVVFIGGQLVGG 77
Cdd:COG0695    2 VTLYTTPGCpyC--ARAKRLLDEKGIPYEEIDVDEDPEARE---ELRERSGRRTVPVIFIGGEHLGG 63
PRK10638 PRK10638
glutaredoxin 3; Provisional
 12-95 5.27e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 33.25  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685  12 SVVIFSNNSCCMSHTIKTLFLDLGVnpTIYELDEINRGKEIEYALAQLGcSPTVPVVFIGGQLVGGANQVMSLHLNRSLI 91
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNSKGV--SFQEIPIDGDAAKREEMIKRSG-RTTVPQIFIDAQHIGGCDDLYALDARGGLD 79


                 ....
gi 259466685  92 PMLK 95
Cdd:PRK10638  80 PLLK 83
 
Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 4-102 3.80e-58

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.


Pssm-ID: 274023 [Multi-domain]  Cd Length: 99  Bit Score: 173.79  E-value: 3.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685    4 IQKMISEKSVVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMS 83
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80

                          90
                  ....*....|....*....
gi 259466685   84 LHLNRSLIPMLKRFGALWL 102
Cdd:TIGR02189  81 LHISGSLVPMLKQAGALWL 99
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 13-93 2.85e-35

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 115.33  E-value: 2.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685  13 VVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMSLHLNRSLIP 92
Cdd:cd03419    2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVK 81


                 .
gi 259466685  93 M 93
Cdd:cd03419   82 L 82
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 13-85 4.11e-16

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 66.34  E-value: 4.11e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259466685  13 VVIFSNNSCCMSHTIKTLFLDLGVnpTIYELDEINRGkEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMSLH 85
Cdd:cd02066    2 VVVFSKSTCPYCKRAKRLLESLGI--EFEEIDILEDG-ELREELKELSGWPTVPQIFINGEFIGGYDDLKALH 71
Glutaredoxin pfam00462
Glutaredoxin;
13-75 3.55e-13

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 58.67  E-value: 3.55e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259466685   13 VVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEInrgKEIEYALAQLGCSPTVPVVFIGGQLV 75
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDED---PEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 49-99 1.21e-06

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 43.76  E-value: 1.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259466685  49 GKEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMSLHLNRSLIPMLKRFGA 99
Cdd:cd03031   45 REELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGIRA 95
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 13-94 2.37e-05

Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]


Pssm-ID: 274017 [Multi-domain]  Cd Length: 79  Bit Score: 39.16  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685   13 VVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEYALAqlGCSpTVPVVFIGGQLVGGANQVMSLHLNRSLIP 92
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRS--GRR-TVPQIFIGDVHVGGCDDLYALDREGKLDP 77


                  ..
gi 259466685   93 ML 94
Cdd:TIGR02181  78 LL 79
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 11-81 3.80e-05

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.


Pssm-ID: 131245 [Multi-domain]  Cd Length: 79  Bit Score: 38.67  E-value: 3.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259466685   11 KSVVIFSNNSCCMSHTIKTLFLDLGvnptiYELDEINRGKEIE-YALAQLGCSPTVPVVFIGGQLVGGANQV 81
Cdd:TIGR02190   8 ESVVVFTKPGCPFCAKAKATLKEKG-----YDFEEIPLGNDARgRSLRAVTGATTVPQVFIGGKLIGGSDEL 74
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 11-81 1.07e-04

Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.


Pssm-ID: 239327 [Multi-domain]  Cd Length: 72  Bit Score: 37.50  E-value: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259466685  11 KSVVIFSNNSCCMSHTIKTLFLDLGvnptiYELDEINRGKEIE-YALAQLGCSPTVPVVFIGGQLVGGANQV 81
Cdd:cd03029    1 ESVSLFTKPGCPFCARAKAALQENG-----ISYEEIPLGKDITgRSLRAVTGAMTVPQVFIDGELIGGSDDL 67
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
13-77 1.89e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 36.71  E-value: 1.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259466685  13 VVIFSNNSC--CmsHTIKTLFLDLGVNPTIYELDEINRGKEieyALAQLGCSPTVPVVFIGGQLVGG 77
Cdd:COG0695    2 VTLYTTPGCpyC--ARAKRLLDEKGIPYEEIDVDEDPEARE---ELRERSGRRTVPVIFIGGEHLGG 63
PRK10638 PRK10638
glutaredoxin 3; Provisional
 12-95 5.27e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 33.25  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259466685  12 SVVIFSNNSCCMSHTIKTLFLDLGVnpTIYELDEINRGKEIEYALAQLGcSPTVPVVFIGGQLVGGANQVMSLHLNRSLI 91
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNSKGV--SFQEIPIDGDAAKREEMIKRSG-RTTVPQIFIDAQHIGGCDDLYALDARGGLD 79


                 ....
gi 259466685  92 PMLK 95
Cdd:PRK10638  80 PLLK 83
 
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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