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Conserved domains on  [gi|10177647|dbj|BAB11109|]
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unnamed protein product [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 ...
 128-269 5.02e-78

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: 232.90  E-value: 5.02e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10177647 128 RIVVYFTSLRGIRRTYEDCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGE--KSVSLPQVFIMGKYVGGADVIKSL 205
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAelKAVSLPRVFVDGRYLGGAEEVLRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10177647 206 FEIGELAKILKEFPMRQPGFVCHCCGDIRFVPCSNCSGSKKLFDED---EDRVKRCPECNENGLIRC 269
Cdd:cd03031  81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENataAGGFLRCPECNENGLVRC 147
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 128-269 5.02e-78

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: 232.90  E-value: 5.02e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10177647 128 RIVVYFTSLRGIRRTYEDCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGE--KSVSLPQVFIMGKYVGGADVIKSL 205
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAelKAVSLPRVFVDGRYLGGAEEVLRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10177647 206 FEIGELAKILKEFPMRQPGFVCHCCGDIRFVPCSNCSGSKKLFDED---EDRVKRCPECNENGLIRC 269
Cdd:cd03031  81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENataAGGFLRCPECNENGLVRC 147
Glutaredoxin pfam00462
Glutaredoxin;
130-196 1.23e-11

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 58.67  E-value: 1.23e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10177647   130 VVYFTslrgiRRTYEDCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGEKSVslPQVFIMGKYV 196
Cdd:pfam00462   1 VVLYT-----KPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTV--PQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
145-216 8.23e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 40.18  E-value: 8.23e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10177647 145 DCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGEKSVslPQVFIMGKYVGGadvikslFEIGELAKILK 216
Cdd:COG0695  12 YCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTV--PVIFIGGEHLGG-------FDEGELDALLA 74
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 146-218 1.96e-04

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: 39.74  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10177647   146 CYAVRMIFRGFRV--WIDERDvsmDIAYRKELQIAMGEKSVS--LPQVFIMGKYVGGADVIKSLFEIGELAKILKEF 218
Cdd:TIGR02189  21 CHVVKRLLLTLGVnpAVHEID---KEPAGKDIENALSRLGCSpaVPAVFVGGKLVGGLENVMALHISGSLVPMLKQA 94
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
185-217 2.06e-03

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 37.19  E-value: 2.06e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 10177647  185 SLPQVFIMGKYVGGADVIKSLFEIGELAKILKE 217
Cdd:PRK10824  70 TFPQLWVDGELVGGCDIVIEMYQRGELQQLIKE 102
 
Name Accession Description Interval E-value
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 128-269 5.02e-78

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: 232.90  E-value: 5.02e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10177647 128 RIVVYFTSLRGIRRTYEDCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGE--KSVSLPQVFIMGKYVGGADVIKSL 205
Cdd:cd03031   1 RVVLYTTSLRGVRKTFEDCNNVRAILESFRVKFDERDVSMDSGFREELRELLGAelKAVSLPRVFVDGRYLGGAEEVLRL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10177647 206 FEIGELAKILKEFPMRQPGFVCHCCGDIRFVPCSNCSGSKKLFDED---EDRVKRCPECNENGLIRC 269
Cdd:cd03031  81 NESGELRKLLKGIRARAGGGVCEGCGGARFVPCSECNGSCKVFAENataAGGFLRCPECNENGLVRC 147
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 128-207 3.05e-18

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: 76.74  E-value: 3.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10177647 128 RIVVYFTSlrgirrTYEDCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGEKSVslPQVFIMGKYVGGADVIKSLFE 207
Cdd:cd02066   1 KVVVFSKS------TCPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTV--PQIFINGEFIGGYDDLKALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
130-196 1.23e-11

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 58.67  E-value: 1.23e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10177647   130 VVYFTslrgiRRTYEDCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGEKSVslPQVFIMGKYV 196
Cdd:pfam00462   1 VVLYT-----KPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTV--PQVFIDGEHI 60
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 187-212 1.22e-05

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 42.87  E-value: 1.22e-05
                        10        20
                ....*....|....*....|....*.
gi 10177647 187 PQVFIMGKYVGGADVIKSLFEIGELA 212
Cdd:cd03028  65 PQLYVNGELVGGCDIVKEMHESGELQ 90
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 168-214 3.23e-05

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: 41.37  E-value: 3.23e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 10177647 168 DIAYRKELQIAMGEKS--VSLPQVFIMGKYVGGADVIKSLFEIGELAKI 214
Cdd:cd03419  34 QHEDGSEIQDYLQELTgqRTVPNVFIGGKFIGGCDDLMALHKSGKLVKL 82
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
145-216 8.23e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 40.18  E-value: 8.23e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10177647 145 DCYAVRMIFRGFRVWIDERDVSMDIAYRKELQIAMGEKSVslPQVFIMGKYVGGadvikslFEIGELAKILK 216
Cdd:COG0695  12 YCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTV--PVIFIGGEHLGG-------FDEGELDALLA 74
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 146-218 1.96e-04

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: 39.74  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10177647   146 CYAVRMIFRGFRV--WIDERDvsmDIAYRKELQIAMGEKSVS--LPQVFIMGKYVGGADVIKSLFEIGELAKILKEF 218
Cdd:TIGR02189  21 CHVVKRLLLTLGVnpAVHEID---KEPAGKDIENALSRLGCSpaVPAVFVGGKLVGGLENVMALHISGSLVPMLKQA 94
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 160-215 9.38e-04

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: 37.24  E-value: 9.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 10177647   160 IDERDVSMDIAYRKELQIAMGEKSVslPQVFIMGKYVGGADVIKSLFEIGELAKIL 215
Cdd:TIGR02181  26 FTEIRVDGDPALRDEMMQRSGRRTV--PQIFIGDVHVGGCDDLYALDREGKLDPLL 79
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 128-205 1.67e-03

Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.


Pssm-ID: 239325 [Multi-domain]  Cd Length: 73  Bit Score: 36.24  E-value: 1.67e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10177647 128 RIVVYftslrgIRRTYEDCYAVRMIFRgfRVWIDERDVSMDIAYRKELQIAMGEKSVSLPQVFIMGKYVGGADVIKSL 205
Cdd:cd03027   2 RVTIY------SRLGCEDCTAVRLFLR--EKGLPYVEINIDIFPERKAELEERTGSSVVPQIFFNEKLVGGLTDLKSL 71
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
185-217 2.06e-03

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 37.19  E-value: 2.06e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 10177647  185 SLPQVFIMGKYVGGADVIKSLFEIGELAKILKE 217
Cdd:PRK10824  70 TFPQLWVDGELVGGCDIVIEMYQRGELQQLIKE 102
PTZ00062 PTZ00062
glutaredoxin; Provisional
 187-217 6.30e-03

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 37.08  E-value: 6.30e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 10177647  187 PQVFIMGKYVGGADVIKSLFEIGELAKILKE 217
Cdd:PTZ00062 170 PQLYVNGELIGGHDIIKELYESNSLRKVIPD 200
 
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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