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Conserved domains on  [gi|71997014|ref|NP_001021848|]
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Glutaredoxin domain-containing protein [Caenorhabditis elegans]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 117-200 4.62e-13

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03419:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 82  Bit Score: 62.17  E-value: 4.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014 117 PVMMYTLIQCVPCQRAKHLLATTYgdIPSHFLELVGDEDwQRQLQVDLLKVTRQATFPYVFVCGNFIGGSSDLFNMHHSG 196
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELG--VKPAVVELDQHED-GSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ....
gi 71997014 197 QLRQ 200
Cdd:cd03419  78 KLVK 81
 
Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 117-200 4.62e-13

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: 62.17  E-value: 4.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014 117 PVMMYTLIQCVPCQRAKHLLATTYgdIPSHFLELVGDEDwQRQLQVDLLKVTRQATFPYVFVCGNFIGGSSDLFNMHHSG 196
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELG--VKPAVVELDQHED-GSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ....
gi 71997014 197 QLRQ 200
Cdd:cd03419  78 KLVK 81
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 118-202 7.74e-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: 45.33  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014   118 VMMYTLIQCVPCQRAKHLLAT---TYGDI-----PSHFLELVgdedwQRqlqvdllkvTRQATFPYVFVCGNFIGGSSDL 189
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSkgvTFTEIrvdgdPALRDEMM-----QR---------SGRRTVPQIFIGDVHVGGCDDL 66

                          90
                  ....*....|...
gi 71997014   190 FNMHHSGQLRQAL 202
Cdd:TIGR02181  67 YALDREGKLDPLL 79
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
117-203 6.11e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 39.80  E-value: 6.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014 117 PVMMYTLIQCVPCQRAKHLLA------TTYgDIpshflelvgDEDwqRQLQVDLLKVTRQATFPYVFVCGNFIGGSSDlf 190
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDekgipyEEI-DV---------DED--PEAREELRERSGRRTVPVIFIGGEHLGGFDE-- 66

                        90
                ....*....|...
gi 71997014 191 nmhhsGQLRQALN 203
Cdd:COG0695  67 -----GELDALLA 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 118-198 2.24e-04

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 38.65  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014  118 VMMYTLIQCVPCQRAKHLLaTTYGdipSHFLELVGDEDWQRQLQvdLLKVTRQATFPYVFVCGNFIGGSSDLFNMHHSGQ 197
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALL-NSKG---VSFQEIPIDGDAAKREE--MIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGG 77


                 .
gi 71997014  198 L 198
Cdd:PRK10638  78 L 78
Glutaredoxin pfam00462
Glutaredoxin;
118-183 2.93e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 37.87  E-value: 2.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71997014   118 VMMYTLIQCVPCQRAKHLLaTTYGdIPSHFLELVGDEDWQRQLQvdllKVTRQATFPYVFVCGNFI 183
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLL-KSLG-VDFEEIDVDEDPEIREELK----ELSGWPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 117-200 4.62e-13

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: 62.17  E-value: 4.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014 117 PVMMYTLIQCVPCQRAKHLLATTYgdIPSHFLELVGDEDwQRQLQVDLLKVTRQATFPYVFVCGNFIGGSSDLFNMHHSG 196
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELG--VKPAVVELDQHED-GSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ....
gi 71997014 197 QLRQ 200
Cdd:cd03419  78 KLVK 81
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 117-193 1.91e-08

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: 49.39  E-value: 1.91e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71997014 117 PVMMYTLIQCVPCQRAKHLLATTYGDipshFLELVGDEDwqRQLQVDLLKVTRQATFPYVFVCGNFIGGSSDLFNMH 193
Cdd:cd02066   1 KVVVFSKSTCPYCKRAKRLLESLGIE----FEEIDILED--GELREELKELSGWPTVPQIFINGEFIGGYDDLKALH 71
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 118-202 7.74e-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: 45.33  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014   118 VMMYTLIQCVPCQRAKHLLAT---TYGDI-----PSHFLELVgdedwQRqlqvdllkvTRQATFPYVFVCGNFIGGSSDL 189
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSkgvTFTEIrvdgdPALRDEMM-----QR---------SGRRTVPQIFIGDVHVGGCDDL 66

                          90
                  ....*....|...
gi 71997014   190 FNMHHSGQLRQAL 202
Cdd:TIGR02181  67 YALDREGKLDPLL 79
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
117-203 6.11e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 39.80  E-value: 6.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014 117 PVMMYTLIQCVPCQRAKHLLA------TTYgDIpshflelvgDEDwqRQLQVDLLKVTRQATFPYVFVCGNFIGGSSDlf 190
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDekgipyEEI-DV---------DED--PEAREELRERSGRRTVPVIFIGGEHLGGFDE-- 66

                        90
                ....*....|...
gi 71997014 191 nmhhsGQLRQALN 203
Cdd:COG0695  67 -----GELDALLA 74
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 109-202 7.32e-05

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: 40.52  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014   109 INRQARRYPVMMYTLIQCVPCQRAKHLLaTTYGDIPShFLELVGDEDwQRQLQVDLLKVTRQATFPYVFVCGNFIGGSSD 188
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLL-LTLGVNPA-VHEIDKEPA-GKDIENALSRLGCSPAVPAVFVGGKLVGGLEN 77

                          90
                  ....*....|....
gi 71997014   189 LFNMHHSGQLRQAL 202
Cdd:TIGR02189  78 VMALHISGSLVPML 91
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 118-189 1.86e-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: 38.65  E-value: 1.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71997014 118 VMMYTLIQCVPCQRAKHLLAT---TYGDIPshflelVGDEDWQRQLQVdllkVTRQATFPYVFVCGNFIGGSSDL 189
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALQEngiSYEEIP------LGKDITGRSLRA----VTGAMTVPQVFIDGELIGGSDDL 67
PRK10638 PRK10638
glutaredoxin 3; Provisional
 118-198 2.24e-04

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 38.65  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014  118 VMMYTLIQCVPCQRAKHLLaTTYGdipSHFLELVGDEDWQRQLQvdLLKVTRQATFPYVFVCGNFIGGSSDLFNMHHSGQ 197
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALL-NSKG---VSFQEIPIDGDAAKREE--MIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGG 77


                 .
gi 71997014  198 L 198
Cdd:PRK10638  78 L 78
Glutaredoxin pfam00462
Glutaredoxin;
118-183 2.93e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 37.87  E-value: 2.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71997014   118 VMMYTLIQCVPCQRAKHLLaTTYGdIPSHFLELVGDEDWQRQLQvdllKVTRQATFPYVFVCGNFI 183
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLL-KSLG-VDFEEIDVDEDPEIREELK----ELSGWPTVPQVFIDGEHI 60
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 172-199 2.08e-03

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: 35.93  E-value: 2.08e-03
                        10        20
                ....*....|....*....|....*...
gi 71997014 172 TFPYVFVCGNFIGGSSDLFNMHHSGQLR 199
Cdd:cd03028  63 TFPQLYVNGELVGGCDIVKEMHESGELQ 90
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 117-196 2.33e-03

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: 35.64  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71997014 117 PVMMYTLIQCVPCQRAKHLLAT---TYGDI-----PSHFLELVGdedwqrqlqvdllKVTRQATFPYVFVCGNFIGGSSD 188
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLDKkgvDYEEIdvdgdPALREEMIN-------------RSGGRRTVPQIFIGDVHIGGCDD 67


                ....*...
gi 71997014 189 LFNMHHSG 196
Cdd:cd03418  68 LYALERKG 75
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
172-203 2.60e-03

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 36.25  E-value: 2.60e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 71997014 172 TFPYVFVCGNFIGGSSDLFNMHHSGQLRQALN 203
Cdd:COG0278  70 TIPQLYVKGEFIGGCDIIREMYESGELQKLLE 101
 
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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