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Conserved domains on  [gi|6320193|ref|NP_010274|]
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glutathione-disulfide reductase GRX6 [Saccharomyces cerevisiae S288C]

Protein Classification

glutaredoxin( domain architecture ID 10130685)

glutaredoxin is a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035|GO:0015038
PubMed:  15706083|14713336|15558583|12074972|30367780

Graphical summary

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List of domain hits

 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 ...
 127-210 8.09e-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: 119.18  E-value: 8.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193  127 PIIIFSKSTCSYSKGMKELLENEYQfipNYYIIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLHTQG 206
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGV---KPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ....
gi 6320193  207 KLLE 210
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 ...
 127-210 8.09e-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: 119.18  E-value: 8.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193  127 PIIIFSKSTCSYSKGMKELLENEYQfipNYYIIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLHTQG 206
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGV---KPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ....
gi 6320193  207 KLLE 210
Cdd:cd03419  78 KLVK 81
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 128-212 9.71e-35

Glutaredoxin; 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 model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016 [Multi-domain]  Cd Length: 83  Bit Score: 118.89  E-value: 9.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193    128 IIIFSKSTCSYSKGMKELLENEYqfIPNYYIIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLHTQGK 207
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLN--VKPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78


                  ....*
gi 6320193    208 LLESL 212
Cdd:TIGR02180  79 LAELL 83
Glutaredoxin pfam00462
Glutaredoxin;
128-190 1.20e-10

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 55.20  E-value: 1.20e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320193    128 IIIFSKSTCSYSKGMKELLEneyQFIPNYYIIELDKHghgEELQEYIKLVTGRGTVPNLLVNG 190
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLK---SLGVDFEEIDVDED---PEIREELKELSGWPTVPQVFIDG 57
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
127-202 3.88e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 40.57  E-value: 3.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193  127 PIIIFSKSTCSYSKGMKELLEN---EYQFIPnyyiIELDkhghgEELQEYIKLVTGRGTVPNLLVNGVSRGG--NEEIKK 201
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEkgiPYEEID----VDED-----PEAREELRERSGRRTVPVIFIGGEHLGGfdEGELDA 71


                .
gi 6320193  202 L 202
Cdd:COG0695  72 L 72
PHA03050 PHA03050
glutaredoxin; Provisional
 128-214 1.44e-03

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 37.30  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193   128 IIIFSKSTCSYSKGMKELLeNEYQFIPNYY-IIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNE---EIKKLH 203
Cdd:PHA03050  15 VTIFVKFTCPFCRNALDIL-NKFSFKRGAYeIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGGYSdllEIDNMD 93

                         90
                 ....*....|.
gi 6320193   204 TQGKLLESLQV 214
Cdd:PHA03050  94 ALGDILSSIGV 104
 
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 ...
 127-210 8.09e-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: 119.18  E-value: 8.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193  127 PIIIFSKSTCSYSKGMKELLENEYQfipNYYIIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLHTQG 206
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGV---KPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ....
gi 6320193  207 KLLE 210
Cdd:cd03419  78 KLVK 81
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 128-212 9.71e-35

Glutaredoxin; 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 model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016 [Multi-domain]  Cd Length: 83  Bit Score: 118.89  E-value: 9.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193    128 IIIFSKSTCSYSKGMKELLENEYqfIPNYYIIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLHTQGK 207
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLN--VKPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78


                  ....*
gi 6320193    208 LLESL 212
Cdd:TIGR02180  79 LAELL 83
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 127-203 1.46e-19

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: 79.43  E-value: 1.46e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320193  127 PIIIFSKSTCSYSKGMKELLENEyqfipNYYIIELDKHGHgEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLH 203
Cdd:cd02066   1 KVVVFSKSTCPYCKRAKRLLESL-----GIEFEEIDILED-GELREELKELSGWPTVPQIFINGEFIGGYDDLKALH 71
Glutaredoxin pfam00462
Glutaredoxin;
128-190 1.20e-10

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 55.20  E-value: 1.20e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320193    128 IIIFSKSTCSYSKGMKELLEneyQFIPNYYIIELDKHghgEELQEYIKLVTGRGTVPNLLVNG 190
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLK---SLGVDFEEIDVDED---PEIREELKELSGWPTVPQVFIDG 57
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 128-208 1.71e-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: 47.25  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193    128 IIIFSKSTCSYSKGMKELLEN---EYQFIPnyyiIELDKhghgEELQEYIKLvTGRGTVPNLLVNGVSRGGNEEIKKLHT 204
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSkgvTFTEIR----VDGDP----ALRDEMMQR-SGRRTVPQIFIGDVHVGGCDDLYALDR 71


                  ....
gi 6320193    205 QGKL 208
Cdd:TIGR02181  72 EGKL 75
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 127-206 9.21e-07

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: 45.27  E-value: 9.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193  127 PIIIFSKSTCSYSKGMKELLEN---EYQFIpnyyIIELDKhghgEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLH 203
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLDKkgvDYEEI----DVDGDP----ALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYALE 72


                ...
gi 6320193  204 TQG 206
Cdd:cd03418  73 RKG 75
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 126-212 1.73e-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: 42.44  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193    126 SPIIIFSKSTCSYSKGMKELLeneYQFIPNYYIIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLHTQ 205
Cdd:TIGR02189   8 KAVVIFSRSSCCMCHVVKRLL---LTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHIS 84


                  ....*..
gi 6320193    206 GKLLESL 212
Cdd:TIGR02189  85 GSLVPML 91
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
127-202 3.88e-05

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 40.57  E-value: 3.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193  127 PIIIFSKSTCSYSKGMKELLEN---EYQFIPnyyiIELDkhghgEELQEYIKLVTGRGTVPNLLVNGVSRGG--NEEIKK 201
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEkgiPYEEID----VDED-----PEAREELRERSGRRTVPVIFIGGEHLGGfdEGELDA 71


                .
gi 6320193  202 L 202
Cdd:COG0695  72 L 72
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 165-213 6.51e-05

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: 41.84  E-value: 6.51e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6320193  165 GHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNEEIKKLHTQGKLLESLQ 213
Cdd:cd03031  43 GFREELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLK 91
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 128-201 2.43e-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: 2.43e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320193  128 IIIFSKSTCSYSKGMKELL-ENEYQFIPnyyiIELDKHGHGEELqeyiKLVTGRGTVPNLLVNGVSRGGNEEIKK 201
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALqENGISYEE----IPLGKDITGRSL----RAVTGAMTVPQVFIDGELIGGSDDLEK 69
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 128-202 1.43e-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: 1.43e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320193  128 IIIFSKSTCSYSKGMKELLENEyqFIPnYYIIELDKH-GHGEELQEyiklVTGRGTVPNLLVNGVSRGGNEEIKKL 202
Cdd:cd03027   3 VTIYSRLGCEDCTAVRLFLREK--GLP-YVEINIDIFpERKAELEE----RTGSSVVPQIFFNEKLVGGLTDLKSL 71
PHA03050 PHA03050
glutaredoxin; Provisional
 128-214 1.44e-03

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 37.30  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193   128 IIIFSKSTCSYSKGMKELLeNEYQFIPNYY-IIELDKHGHGEELQEYIKLVTGRGTVPNLLVNGVSRGGNE---EIKKLH 203
Cdd:PHA03050  15 VTIFVKFTCPFCRNALDIL-NKFSFKRGAYeIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGGYSdllEIDNMD 93

                         90
                 ....*....|.
gi 6320193   204 TQGKLLESLQV 214
Cdd:PHA03050  94 ALGDILSSIGV 104
PRK10638 PRK10638
glutaredoxin 3; Provisional
 128-208 2.14e-03

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 35.95  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193   128 IIIFSKSTCSYSKGMKELLENE---YQFIPnyyiieLDkhGHGEELQEYIKLvTGRGTVPNLLVNGVSRGGNEEIKKLHT 204
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALLNSKgvsFQEIP------ID--GDAAKREEMIKR-SGRTTVPQIFIDAQHIGGCDDLYALDA 74


                 ....
gi 6320193   205 QGKL 208
Cdd:PRK10638  75 RGGL 78
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 127-202 7.32e-03

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 34.12  E-value: 7.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320193  127 PIIIFSKSTCSYSKGMKELLEN---EYQFIPnyyiIELDkhghgEELQEYIKLVTGRGTVPNLLVNG--VSRGGNEEIKK 201
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDErgiPFEEVD----VDED-----PEALEELKKLNGYRSVPVVVIGDehLSGFRPDKLRA 71


                .
gi 6320193  202 L 202
Cdd:cd02976  72 L 72
 
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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