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Conserved domains on  [gi|15228503|ref|NP_189527|]
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Glutaredoxin family protein [Arabidopsis thaliana]

Protein Classification

glutaredoxin family protein( domain architecture ID 10122541)

glutaredoxin (GRX) family protein belonging to the thioredoxin superfamily, may function as a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  11441809|12074972|9099998|10049365|15558583|14713336
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 252-423 4.93e-64

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: 202.47  E-value: 4.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 252 RVILYFTSLRGIRKTYEESCDVRVILKSLGIRVDERDVSMHSGFKDELKELLGEKFnkgVGITLPRVFLGRKYIGGAEEI 331
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAEL---KAVSLPRVFVDGRYLGGAEEV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 332 RKLNEDGKLEKLLGGCERVEEnqngnGLECEACGDVRFVPCETCSGSCKVyyeyedddddddegdddESVKEEREYGFQT 411
Cdd:cd03031  78 LRLNESGELRKLLKGIRARAG-----GGVCEGCGGARFVPCSECNGSCKV-----------------FAENATAAGGFLR 135

                       170
                ....*....|..
gi 15228503 412 CPDCNENGLIRC 423
Cdd:cd03031 136 CPECNENGLVRC 147
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 252-423 4.93e-64

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: 202.47  E-value: 4.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 252 RVILYFTSLRGIRKTYEESCDVRVILKSLGIRVDERDVSMHSGFKDELKELLGEKFnkgVGITLPRVFLGRKYIGGAEEI 331
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAEL---KAVSLPRVFVDGRYLGGAEEV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 332 RKLNEDGKLEKLLGGCERVEEnqngnGLECEACGDVRFVPCETCSGSCKVyyeyedddddddegdddESVKEEREYGFQT 411
Cdd:cd03031  78 LRLNESGELRKLLKGIRARAG-----GGVCEGCGGARFVPCSECNGSCKV-----------------FAENATAAGGFLR 135

                       170
                ....*....|..
gi 15228503 412 CPDCNENGLIRC 423
Cdd:cd03031 136 CPECNENGLVRC 147
Glutaredoxin pfam00462
Glutaredoxin;
254-325 4.45e-09

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 52.12  E-value: 4.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228503   254 ILYFTslrgiRKTYEESCDVRVILKSLGIRVDERDVSMHSGFKDELKELLGEKfnkgvgiTLPRVFLGRKYI 325
Cdd:pfam00462   1 VVLYT-----KPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWP-------TVPQVFIDGEHI 60
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 277-344 2.87e-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: 42.25  E-value: 2.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228503   277 LKSLGIRVDERDVSMHSGFKDELKELLGekfnkgvGITLPRVFLGRKYIGGAEEIRKLNEDGKLEKLL 344
Cdd:TIGR02181  19 LSSKGVTFTEIRVDGDPALRDEMMQRSG-------RRTVPQIFIGDVHVGGCDDLYALDREGKLDPLL 79
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
271-345 1.21e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 40.18  E-value: 1.21e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228503 271 CD-VRVILKSLGIRVDERDVSMHSGFKDELKELLGekfnkgvGITLPRVFLGRKYIGGAeeirklnEDGKLEKLLG 345
Cdd:COG0695  13 CArAKRLLDEKGIPYEEIDVDEDPEAREELRERSG-------RRTVPVIFIGGEHLGGF-------DEGELDALLA 74
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 252-423 4.93e-64

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: 202.47  E-value: 4.93e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 252 RVILYFTSLRGIRKTYEESCDVRVILKSLGIRVDERDVSMHSGFKDELKELLGEKFnkgVGITLPRVFLGRKYIGGAEEI 331
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAEL---KAVSLPRVFVDGRYLGGAEEV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 332 RKLNEDGKLEKLLGGCERVEEnqngnGLECEACGDVRFVPCETCSGSCKVyyeyedddddddegdddESVKEEREYGFQT 411
Cdd:cd03031  78 LRLNESGELRKLLKGIRARAG-----GGVCEGCGGARFVPCSECNGSCKV-----------------FAENATAAGGFLR 135

                       170
                ....*....|..
gi 15228503 412 CPDCNENGLIRC 423
Cdd:cd03031 136 CPECNENGLVRC 147
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 252-336 4.56e-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: 72.50  E-value: 4.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 252 RVILYFTSlrgirkTYEESCDVRVILKSLGIRVDERDVSMHSGFKDELKELLGEKfnkgvgiTLPRVFLGRKYIGGAEEI 331
Cdd:cd02066   1 KVVVFSKS------TCPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWP-------TVPQIFINGEFIGGYDDL 67


                ....*
gi 15228503 332 RKLNE 336
Cdd:cd02066  68 KALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
254-325 4.45e-09

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 52.12  E-value: 4.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228503   254 ILYFTslrgiRKTYEESCDVRVILKSLGIRVDERDVSMHSGFKDELKELLGEKfnkgvgiTLPRVFLGRKYI 325
Cdd:pfam00462   1 VVLYT-----KPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWP-------TVPQVFIDGEHI 60
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 265-343 1.84e-07

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: 48.30  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 265 KTYEESCD-VRVILKSLGIR--VDERDVSMH-SGFKDELKELLGEKfnkgvgiTLPRVFLGRKYIGGAEEIRKLNEDGKL 340
Cdd:cd03419   7 KSYCPYCKrAKSLLKELGVKpaVVELDQHEDgSEIQDYLQELTGQR-------TVPNVFIGGKFIGGCDDLMALHKSGKL 79


                ...
gi 15228503 341 EKL 343
Cdd:cd03419  80 VKL 82
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 253-345 1.60e-06

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.


Pssm-ID: 239328 [Multi-domain]  Cd Length: 92  Bit Score: 46.11  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228503 253 VILYFTSLRGIRKTYEESCDVRVILKSLGIRVDERDVSMHSGFKDELKELLGEKFNKGVGitlPRVFLGRKYIGGAEEIR 332
Cdd:cd03030   2 IKVYIASSSGSTEIKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNENGKPLP---PQIFNGDEYCGDYEAFF 78

                        90
                ....*....|...
gi 15228503 333 KLNEDGKLEKLLG 345
Cdd:cd03030  79 EAKENNTLEEFLK 91
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 277-344 2.87e-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: 42.25  E-value: 2.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228503   277 LKSLGIRVDERDVSMHSGFKDELKELLGekfnkgvGITLPRVFLGRKYIGGAEEIRKLNEDGKLEKLL 344
Cdd:TIGR02181  19 LSSKGVTFTEIRVDGDPALRDEMMQRSG-------RRTVPQIFIGDVHVGGCDDLYALDREGKLDPLL 79
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
271-345 1.21e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 40.18  E-value: 1.21e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228503 271 CD-VRVILKSLGIRVDERDVSMHSGFKDELKELLGekfnkgvGITLPRVFLGRKYIGGAeeirklnEDGKLEKLLG 345
Cdd:COG0695  13 CArAKRLLDEKGIPYEEIDVDEDPEAREELRERSG-------RRTVPVIFIGGEHLGGF-------DEGELDALLA 74
 
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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