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Conserved domains on  [gi|6319814|ref|NP_009895|]
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dithiol glutaredoxin GRX1 [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 ...
 19-92 3.42e-31

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: 105.31  E-value: 3.42e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319814   19 IFVASKTYCPYCHAALNtLFEKLKVprsKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:cd03419   2 VVVFSKSYCPYCKRAKS-LLKELGV---KPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLM 71
 
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 ...
 19-92 3.42e-31

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: 105.31  E-value: 3.42e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319814   19 IFVASKTYCPYCHAALNtLFEKLKVprsKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:cd03419   2 VVVFSKSYCPYCKRAKS-LLKELGV---KPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLM 71
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 19-92 9.61e-30

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: 101.55  E-value: 9.61e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319814     19 IFVASKTYCPYCHAALNtLFEKLKVPRSKVLvlQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKE-ILAKLNVKPYEVV--ELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLL 71
Glutaredoxin pfam00462
Glutaredoxin;
19-85 1.37e-14

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 62.52  E-value: 1.37e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319814     19 IFVASKTYCPYCHAALNTLfEKLKVPRSKVLVLQLndmkegADIQAALYEINGQRTVPNIYINGKHI 85
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLL-KSLGVDFEEIDVDED------PEIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
23-90 2.41e-12

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 57.13  E-value: 2.41e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319814   23 SKTYCPYCHAALNtLFEKLKVPRSKVlvlqlnDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDD 90
Cdd:COG0695   6 TTPGCPYCARAKR-LLDEKGIPYEEI------DVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFDE 66
PRK10638 PRK10638
glutaredoxin 3; Provisional
 14-91 2.82e-09

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 49.82  E-value: 2.82e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319814    14 IAENEIFvaSKTYCPYCHAALNTLfeklkvpRSKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDL 91
Cdd:PRK10638   1 MANVEIY--TKATCPFCHRAKALL-------NSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDL 69
 
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 ...
 19-92 3.42e-31

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: 105.31  E-value: 3.42e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319814   19 IFVASKTYCPYCHAALNtLFEKLKVprsKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:cd03419   2 VVVFSKSYCPYCKRAKS-LLKELGV---KPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLM 71
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 19-92 9.61e-30

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: 101.55  E-value: 9.61e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319814     19 IFVASKTYCPYCHAALNtLFEKLKVPRSKVLvlQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKE-ILAKLNVKPYEVV--ELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLL 71
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 19-91 9.28e-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: 75.97  E-value: 9.28e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319814   19 IFVASKTYCPYCHAALNtLFEKLKVPrskvlVLQLNDMKEGaDIQAALYEINGQRTVPNIYINGKHIGGNDDL 91
Cdd:cd02066   2 VVVFSKSTCPYCKRAKR-LLESLGIE-----FEEIDILEDG-ELREELKELSGWPTVPQIFINGEFIGGYDDL 67
Glutaredoxin pfam00462
Glutaredoxin;
19-85 1.37e-14

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 62.52  E-value: 1.37e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319814     19 IFVASKTYCPYCHAALNTLfEKLKVPRSKVLVLQLndmkegADIQAALYEINGQRTVPNIYINGKHI 85
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLL-KSLGVDFEEIDVDED------PEIREELKELSGWPTVPQVFIDGEHI 60
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 23-92 3.11e-13

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: 59.58  E-value: 3.11e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319814     23 SKTYCPYCHAALNTL------FEKLKVPRSKVLvlqlndmkegadiQAALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:TIGR02181   5 TKPYCPYCTRAKALLsskgvtFTEIRVDGDPAL-------------RDEMMQRSGRRTVPQIFIGDVHVGGCDDLY 67
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 18-91 1.35e-12

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: 57.98  E-value: 1.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319814   18 EIFVASKTYCPYCHAALNTL------FEKLKVPRSKVLvlqLNDMKEGAdiqaalyeiNGQRTVPNIYINGKHIGGNDDL 91
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLdkkgvdYEEIDVDGDPAL---REEMINRS---------GGRRTVPQIFIGDVHIGGCDDL 68
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
23-90 2.41e-12

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 57.13  E-value: 2.41e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319814   23 SKTYCPYCHAALNtLFEKLKVPRSKVlvlqlnDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDD 90
Cdd:COG0695   6 TTPGCPYCARAKR-LLDEKGIPYEEI------DVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFDE 66
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 10-91 1.47e-10

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: 53.23  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319814     10 VKDLIAENEIFVASKTYCPYCHAAlNTLFEKLKV-PrskvLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGN 88
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVV-KRLLLTLGVnP----AVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGL 75


                  ...
gi 6319814     89 DDL 91
Cdd:TIGR02189  76 ENV 78
PRK10638 PRK10638
glutaredoxin 3; Provisional
 14-91 2.82e-09

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 49.82  E-value: 2.82e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319814    14 IAENEIFvaSKTYCPYCHAALNTLfeklkvpRSKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDL 91
Cdd:PRK10638   1 MANVEIY--TKATCPFCHRAKALL-------NSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDL 69
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 15-92 4.99e-08

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: 46.37  E-value: 4.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319814     15 AENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLvlqlndmkeGADIQA-ALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:TIGR02190   6 KPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPL---------GNDARGrSLRAVTGATTVPQVFIGGKLIGGSDELE 75
PHA03050 PHA03050
glutaredoxin; Provisional
 10-91 4.39e-07

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 44.62  E-value: 4.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319814    10 VKDLIAENEIFVASKTYCPYCHAALNTLfEKLKVPRSKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGND 89
Cdd:PHA03050   6 VQQRLANNKVTIFVKFTCPFCRNALDIL-NKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGGYS 84


                 ..
gi 6319814    90 DL 91
Cdd:PHA03050  85 DL 86
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 19-92 1.44e-06

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: 42.50  E-value: 1.44e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319814   19 IFVASKTYCPYCHAALNTLFEKlkvprskvlVLQLNDMKEGADIQA-ALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALQEN---------GISYEEIPLGKDITGrSLRAVTGAMTVPQVFIDGELIGGSDDLE 68
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 19-92 1.34e-05

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: 40.09  E-value: 1.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319814   19 IFVASKTYCPYChAALNTLFEKLKVPRSKVlvlqlnDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQ 92
Cdd:cd03027   3 VTIYSRLGCEDC-TAVRLFLREKGLPYVEI------NIDIFPERKAELEERTGSSVVPQIFFNEKLVGGLTDLK 69
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 18-87 1.77e-04

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: 36.82  E-value: 1.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319814   18 EIFVASKTYCPYCHAALNTLfEKLKVPrskvlvLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGG 87
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFL-DERGIP------FEEVDVDEDPEALEELKKLNGYRSVPVVVIGDEHLSG 63
grxA PRK11200
glutaredoxin 1; Provisional
 27-92 5.63e-04

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 35.78  E-value: 5.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319814    27 CPYCHAALNtLFEKLKVPRSKVLVLQLNDMKEGADiQAALYEINGQ--RTVPNIYINGKHIGGNDDLQ 92
Cdd:PRK11200  11 CPYCVRAKE-LAEKLSEERDDFDYRYVDIHAEGIS-KADLEKTVGKpvETVPQIFVDQKHIGGCTDFE 76
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 10-89 1.08e-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: 35.16  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319814   10 VKDLIAENEIFV-----ASKTYCPYCHAALNTLfEKLKVPRSKVLVLQLNDMKEGadiqaaLYEINGQRTVPNIYINGKH 84
Cdd:cd03028   1 IKKLIKENPVVLfmkgtPEEPRCGFSRKVVQIL-NQLGVDFGTFDILEDEEVRQG------LKEYSNWPTFPQLYVNGEL 73


                ....*
gi 6319814   85 IGGND 89
Cdd:cd03028  74 VGGCD 78
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 18-91 2.16e-03

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 36.16  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319814    18 EIFVASKTYCPYCHAAlNTLFEKLKVPRSKVlvlQLNDMKEGADIQAalyEINGQ--------RTVPNIYINGKHIGGND 89
Cdd:PRK12759   3 EVRIYTKTNCPFCDLA-KSWFGANDIPFTQI---SLDDDVKRAEFYA---EVNKNillveehiRTVPQIFVGDVHIGGYD 75


                 ..
gi 6319814    90 DL 91
Cdd:PRK12759  76 NL 77
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 21-89 2.87e-03

Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.


Pssm-ID: 274027 [Multi-domain]  Cd Length: 74  Bit Score: 33.89  E-value: 2.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319814     21 VASKTYCPYCHAAlNTLFEKLKVPRSKVlvlqlnDMKEGADIQAALYEINGQRTVPNIYINGKHIGGND 89
Cdd:TIGR02196   4 VYTTPWCPPCVKA-KEYLTSKGVAFEEI------DVEKDAAAREELLKVYGQRGVPVIVIGHKIVVGFD 65
 
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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