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Conserved domains on  [gi|1972431752|emb|CAE0867371|]
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unnamed protein product [Oxyrrhis marina]

Protein Classification

Glutaredoxin and Thioredoxin_like domain-containing protein( domain architecture ID 10452597)

Glutaredoxin and Thioredoxin_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glutaredoxin pfam00462
Glutaredoxin;
13-67 6.32e-21

Glutaredoxin;


:

Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 81.40  E-value: 6.32e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFI 55
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 155-187 3.70e-09

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 cd00340:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 152  Bit Score: 52.90  E-value: 3.70e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972431752 155 DLYKLAARLITGEKISLEKFRGKVTLVVNTASK 187
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASK 33
 
Name Accession Description Interval E-value
Glutaredoxin pfam00462
Glutaredoxin;
13-67 6.32e-21

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 81.40  E-value: 6.32e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFI 55
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 12-67 1.99e-20

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: 80.66  E-value: 1.99e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVD---NDEALYAALKAMTGKQTVPQIFI 67
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDqheDGSEIQDYLQELTGQRTVPNVFI 59
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
12-67 5.17e-19

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 76.78  E-value: 5.17e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFI 56
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 13-67 3.35e-17

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: 72.29  E-value: 3.35e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFI 55
PRK10638 PRK10638
glutaredoxin 3; Provisional
 10-67 1.47e-11

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 57.91  E-value: 1.47e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972431752  10 VAPVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:PRK10638    1 MANVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFI 58
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 155-187 3.70e-09

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 52.90  E-value: 3.70e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972431752 155 DLYKLAARLITGEKISLEKFRGKVTLVVNTASK 187
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASK 33
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 155-187 5.14e-09

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 52.77  E-value: 5.14e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972431752 155 DLYKLAARLITGEKISLEKFRGKVTLVVNTASK 187
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASK 35
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 13-65 4.55e-07

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 45.53  E-value: 4.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEV-DNDEALYAALKAMTGKQTVPQI 65
Cdd:NF041212    1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVsKDPEALEEMLRLTGGERIVPVI 54
GSHPx pfam00255
Glutathione peroxidase;
156-187 2.70e-06

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 44.27  E-value: 2.70e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1972431752 156 LYKLAARLITGEKISLEKFRGKVTLVVNTASK 187
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASK 32
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 155-186 9.70e-06

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 43.67  E-value: 9.70e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1972431752 155 DLYKLAARLITGEKISLEKFRGKVTLVVNTAS 186
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVAS 32
 
Name Accession Description Interval E-value
Glutaredoxin pfam00462
Glutaredoxin;
13-67 6.32e-21

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 81.40  E-value: 6.32e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFI 55
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 12-67 1.99e-20

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: 80.66  E-value: 1.99e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVD---NDEALYAALKAMTGKQTVPQIFI 67
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDqheDGSEIQDYLQELTGQRTVPNVFI 59
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
12-67 5.17e-19

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 76.78  E-value: 5.17e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFI 56
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 12-67 8.28e-18

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 73.66  E-value: 8.28e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:cd02066     1 KVVVFSKSTCPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFI 56
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 13-67 3.35e-17

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: 72.29  E-value: 3.35e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFI 55
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 12-67 1.63e-16

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: 70.31  E-value: 1.63e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGK-QTVPQIFI 67
Cdd:cd03418     1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGGrRTVPQIFI 57
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 13-67 4.37e-15

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: 66.88  E-value: 4.37e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMA----HEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKPYEvvelDQLSNGSEIQDYLEEITGQRTVPNIFI 59
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 12-67 3.61e-12

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: 59.16  E-value: 3.61e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLNGYRSVPVVVI 56
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 13-67 1.08e-11

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: 57.91  E-value: 1.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDeALYAALKAMTGKQTVPQIFI 67
Cdd:cd03029     3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKD-ITGRSLRAVTGAMTVPQVFI 56
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 13-67 1.29e-11

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: 57.93  E-value: 1.29e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDeALYAALKAMTGKQTVPQIFI 67
Cdd:TIGR02190  10 VVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGND-ARGRSLRAVTGATTVPQVFI 63
PRK10638 PRK10638
glutaredoxin 3; Provisional
 10-67 1.47e-11

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 57.91  E-value: 1.47e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972431752  10 VAPVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:PRK10638    1 MANVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFI 58
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 155-187 3.70e-09

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 52.90  E-value: 3.70e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972431752 155 DLYKLAARLITGEKISLEKFRGKVTLVVNTASK 187
Cdd:cd00340     1 SIYDFSVKDIDGEPVSLSKYKGKVLLIVNVASK 33
BtuE COG0386
Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid ...
 155-187 5.14e-09

Thioredoxin/glutathione peroxidase BtuE, reduces lipid peroxides [Defense mechanisms, Lipid transport and metabolism];


Pssm-ID: 440155 [Multi-domain]  Cd Length: 161  Bit Score: 52.77  E-value: 5.14e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972431752 155 DLYKLAARLITGEKISLEKFRGKVTLVVNTASK 187
Cdd:COG0386     3 SIYDFSVTTLDGEPVSLSDYKGKVLLIVNTASK 35
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 12-67 5.57e-09

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: 50.46  E-value: 5.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFI 67
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAREELLKVYGQRGVPVIVI 56
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 13-66 2.37e-08

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: 48.95  E-value: 2.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIF 66
Cdd:cd03027     3 VTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPERKAELEERTGSSVVPQIF 56
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 13-65 4.55e-07

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 45.53  E-value: 4.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEV-DNDEALYAALKAMTGKQTVPQI 65
Cdd:NF041212    1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVsKDPEALEEMLRLTGGERIVPVI 54
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 12-67 5.15e-07

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: 45.91  E-value: 5.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972431752  12 PVVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALY---AALKAMTGKQTVPQIFI 67
Cdd:TIGR02189   9 AVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKdieNALSRLGCSPAVPAVFV 67
GSHPx pfam00255
Glutathione peroxidase;
156-187 2.70e-06

Glutathione peroxidase;


Pssm-ID: 395197  Cd Length: 108  Bit Score: 44.27  E-value: 2.70e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1972431752 156 LYKLAARLITGEKISLEKFRGKVTLVVNTASK 187
Cdd:pfam00255   1 IYEFSAKDIDGEPVPFDQYRGKVVLIVNVASK 32
gpx7 TIGR02540
putative glutathione peroxidase Gpx7; This model represents one of several families of known ...
 155-186 9.70e-06

putative glutathione peroxidase Gpx7; This model represents one of several families of known and probable glutathione peroxidases. This family is restricted to animals and designated GPX7.


Pssm-ID: 131592 [Multi-domain]  Cd Length: 153  Bit Score: 43.67  E-value: 9.70e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1972431752 155 DLYKLAARLITGEKISLEKFRGKVTLVVNTAS 186
Cdd:TIGR02540   1 DFYSFEVKDARGRTVSLEKYRGKVSLVVNVAS 32
grxA PRK11200
glutaredoxin 1; Provisional
 13-67 1.96e-04

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 38.48  E-value: 1.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972431752  13 VVIFSKPSCPFCKGAKA---TFTEAGVPFMAHEVD-NDEALYAA-LKAMTGK--QTVPQIFI 67
Cdd:PRK11200    3 VVIFGRPGCPYCVRAKElaeKLSEERDDFDYRYVDiHAEGISKAdLEKTVGKpvETVPQIFV 64
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 11-68 3.62e-04

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: 37.86  E-value: 3.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972431752  11 APVVIFSK-----PSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVPQIFIG 68
Cdd:cd03028     8 NPVVLFMKgtpeePRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVN 70
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 13-63 7.67e-04

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 36.78  E-value: 7.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALYAALKAMTGKQTVP 63
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVP 51
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 13-67 1.33e-03

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 38.47  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEA---LYAA-----LKAMTGKQTVPQIFI 67
Cdd:PRK12759    4 VRIYTKTNCPFCDLAKSWFGANDIPFTQISLDDDVKraeFYAEvnkniLLVEEHIRTVPQIFV 66
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 13-67 2.52e-03

Thioredoxin (TRX) superfamily; 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 TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 35.37  E-value: 2.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEA-----GVPFMAHEVDNDEALyAALKAMTGKQTVPQIFI 67
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELallnkGVKFEAVDVDEDPAL-EKELKRYGVGGVPTLVV 59
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
16-63 2.52e-03

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 35.28  E-value: 2.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1972431752  16 FSKPSCPFCKGAKATFTEAGVPFMAHEVDNDEALyAALKAMTGKQTVP 63
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHP-PELLAKNPLGKVP 48
PHA03050 PHA03050
glutaredoxin; Provisional
 13-66 8.37e-03

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 34.61  E-value: 8.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972431752  13 VVIFSKPSCPFCKGAKATFTEAGVPFMAHEVDN------DEALYAALKAMTGKQTVPQIF 66
Cdd:PHA03050   15 VTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDikefkpENELRDYFEQITGGRTVPRIF 74
 
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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