NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|300643534|emb|CBU94387|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 4-101 1.18e-40

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: 129.50  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534    4 ISNLLEDKPVVIFSKTSCCMSHSIKSLISGYGANSTVYELDEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMS 83
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80

                          90
                  ....*....|....*...
gi 300643534   84 LQVRNQLASLLRRAGAIW 101
Cdd:TIGR02189  81 LHISGSLVPMLKQAGALW 98
 
Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 4-101 1.18e-40

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: 129.50  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534    4 ISNLLEDKPVVIFSKTSCCMSHSIKSLISGYGANSTVYELDEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMS 83
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80

                          90
                  ....*....|....*...
gi 300643534   84 LQVRNQLASLLRRAGAIW 101
Cdd:TIGR02189  81 LHISGSLVPMLKQAGALW 98
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 12-93 3.02e-37

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: 120.34  E-value: 3.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534  12 PVVIFSKTSCCMSHSIKSLISGYGANSTVYELDEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMSLQVRNQLA 91
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80


                 ..
gi 300643534  92 SL 93
Cdd:cd03419   81 KL 82
Glutaredoxin pfam00462
Glutaredoxin;
13-75 3.94e-15

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 63.68  E-value: 3.94e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300643534   13 VVIFSKTSCCMSHSIKSLISGYGANSTVYELDEMsngPEIERALVELGCKPTVPAVFIGQELV 75
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDED---PEIREELKELSGWPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
 13-95 2.42e-07

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 44.43  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534  13 VVIFSKTSCCMSHSIKSLISGYGAnsTVYELdEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMSLQVRNQLAS 92
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALLNSKGV--SFQEI-PIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80


                 ...
gi 300643534  93 LLR 95
Cdd:PRK10638  81 LLK 83
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
12-77 7.54e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.87  E-value: 7.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300643534  12 PVVIFSKTSC--CmsHSIKSLISGYGANSTVYELDEMsngPEIERALVELGCKPTVPAVFIGQELVGG 77
Cdd:COG0695    1 KVTLYTTPGCpyC--ARAKRLLDEKGIPYEEIDVDED---PEAREELRERSGRRTVPVIFIGGEHLGG 63
 
Name Accession Description Interval E-value
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 4-101 1.18e-40

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: 129.50  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534    4 ISNLLEDKPVVIFSKTSCCMSHSIKSLISGYGANSTVYELDEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMS 83
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80

                          90
                  ....*....|....*...
gi 300643534   84 LQVRNQLASLLRRAGAIW 101
Cdd:TIGR02189  81 LHISGSLVPMLKQAGALW 98
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 12-93 3.02e-37

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: 120.34  E-value: 3.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534  12 PVVIFSKTSCCMSHSIKSLISGYGANSTVYELDEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMSLQVRNQLA 91
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80


                 ..
gi 300643534  92 SL 93
Cdd:cd03419   81 KL 82
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 12-84 1.15e-20

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: 77.89  E-value: 1.15e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300643534  12 PVVIFSKTSCCMSHSIKSLISGYGAnsTVYELDEMSNGpEIERALVELGCKPTVPAVFIGQELVGGANQLMSL 84
Cdd:cd02066    1 KVVVFSKSTCPYCKRAKRLLESLGI--EFEEIDILEDG-ELREELKELSGWPTVPQIFINGEFIGGYDDLKAL 70
Glutaredoxin pfam00462
Glutaredoxin;
13-75 3.94e-15

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 63.68  E-value: 3.94e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300643534   13 VVIFSKTSCCMSHSIKSLISGYGANSTVYELDEMsngPEIERALVELGCKPTVPAVFIGQELV 75
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDED---PEIREELKELSGWPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
 13-95 2.42e-07

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 44.43  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534  13 VVIFSKTSCCMSHSIKSLISGYGAnsTVYELdEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMSLQVRNQLAS 92
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALLNSKGV--SFQEI-PIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80


                 ...
gi 300643534  93 LLR 95
Cdd:PRK10638  81 LLK 83
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 13-94 3.99e-07

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: 43.79  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534   13 VVIFSKTSCCMSHSIKSLISGYGAnstVYELDEMSNGPEIERALVELGCKPTVPAVFIGQELVGGANQLMSLQVRNQLAS 92
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGV---TFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77


                  ..
gi 300643534   93 LL 94
Cdd:TIGR02181  78 LL 79
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 12-85 1.53e-05

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial 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 E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 39.49  E-value: 1.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300643534  12 PVVIFSKTSCCMSHSIKSLIsgyGANSTVYELDEMSNGPEIERALVEL-GCKPTVPAVFIGQELVGGANQLMSLQ 85
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALL---DKKGVDYEEIDVDGDPALREEMINRsGGRRTVPQIFIGDVHIGGCDDLYALE 72
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 11-81 2.09e-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: 39.44  E-value: 2.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300643534   11 KPVVIFSKTSCCMSHSIKSLISGYGanstvYELDEMSNGPEIE-RALVELGCKPTVPAVFIGQELVGGANQL 81
Cdd:TIGR02190   8 ESVVVFTKPGCPFCAKAKATLKEKG-----YDFEEIPLGNDARgRSLRAVTGATTVPQVFIGGKLIGGSDEL 74
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
12-77 7.54e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.87  E-value: 7.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300643534  12 PVVIFSKTSC--CmsHSIKSLISGYGANSTVYELDEMsngPEIERALVELGCKPTVPAVFIGQELVGG 77
Cdd:COG0695    1 KVTLYTTPGCpyC--ARAKRLLDEKGIPYEEIDVDED---PEAREELRERSGRRTVPVIFIGGEHLGG 63
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 13-81 2.87e-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: 36.34  E-value: 2.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534  13 VVIFSKTSCCMSHSIKSLISGYGanstvYELDEMSNGPEIE-RALVELGCKPTVPAVFIGQELVGGANQL 81
Cdd:cd03029    3 VSLFTKPGCPFCARAKAALQENG-----ISYEEIPLGKDITgRSLRAVTGAMTVPQVFIDGELIGGSDDL 67
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
1-99 2.90e-04

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 37.19  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534   1 MEKISNLLEDKPVVIFSKTS-----CCMSHSIKSLISGYGANSTVyeLDEMSNgPEIERALVELGCKPTVPAVFIGQELV 75
Cdd:PRK10824   5 IEKIQRQIAENPILLYMKGSpklpsCGFSAQAVQALSACGERFAY--VDILQN-PDIRAELPKYANWPTFPQLWVDGELV 81

                         90       100
                 ....*....|....*....|....
gi 300643534  76 GGANQLMSLQVRNQLASLLRRAGA 99
Cdd:PRK10824  82 GGCDIVIEMYQRGELQQLIKETAA 105
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 21-99 3.10e-04

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: 37.22  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300643534  21 CCMshsIKSLISGYGAnsTVYELD-EMSNG--PEIERALVELGCKPTVPAVFIGQELVGGANQLMSLQVRNQLASLLRRA 97
Cdd:cd03031   19 CNN---VRAILESFRV--KFDERDvSMDSGfrEELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGI 93


                 ..
gi 300643534  98 GA 99
Cdd:cd03031   94 RA 95
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH