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Conserved domains on  [gi|493862703|ref|WP_006809455|]
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MULTISPECIES: GrxA family glutaredoxin [Enterobacteriaceae]

Protein Classification

glutaredoxin( domain architecture ID 10013759)

glutaredoxin is a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins such as ribonucleotide reductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
grxA PRK11200
glutaredoxin 1; Provisional
 1-85 2.53e-65

glutaredoxin 1; Provisional


:

Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 190.63  E-value: 2.53e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703  1 MFAVIFGRPGCPYCVRAKELAEKLTEERDDFNFRYVDIHAEGITKADLEKTVGKPVETVPQIFLDQKHIGGCTDFEAYAK 80
Cdd:PRK11200  1 MFVVIFGRPGCPYCVRAKELAEKLSEERDDFDYRYVDIHAEGISKADLEKTVGKPVETVPQIFVDQKHIGGCTDFEAYVK 80


                ....*
gi 493862703 81 EHLGL 85
Cdd:PRK11200 81 ENLGL 85
 
Name Accession Description Interval E-value
grxA PRK11200
glutaredoxin 1; Provisional
 1-85 2.53e-65

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 190.63  E-value: 2.53e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703  1 MFAVIFGRPGCPYCVRAKELAEKLTEERDDFNFRYVDIHAEGITKADLEKTVGKPVETVPQIFLDQKHIGGCTDFEAYAK 80
Cdd:PRK11200  1 MFVVIFGRPGCPYCVRAKELAEKLSEERDDFDYRYVDIHAEGISKADLEKTVGKPVETVPQIFVDQKHIGGCTDFEAYVK 80


                ....*
gi 493862703 81 EHLGL 85
Cdd:PRK11200 81 ENLGL 85
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-87 5.13e-52

Glutaredoxin, GrxA 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 model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.


Pssm-ID: 131238 [Multi-domain]  Cd Length: 86  Bit Score: 157.30  E-value: 5.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703   2 FAVIFGRPGCPYCVRAKELAEKLTEERDDFNFRYVDIHAEGITKADLEKTVGKPVETVPQIFLDQKHIGGCTDFEAYAKE 81
Cdd:TIGR02183  1 FVVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDIHAEGISKADLEKTVGKPVETVPQIFVDEKHVGGCTDFEQLVKE 80


                 ....*.
gi 493862703  82 HLGLFA 87
Cdd:TIGR02183 81 NFDIEA 86
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 4-80 1.48e-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: 72.11  E-value: 1.48e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493862703  4 VIFGRPGCPYCVRAKELAEKLteerdDFNFRYVDIHAEGITKADLEKTVGKPveTVPQIFLDQKHIGGCTDFEAYAK 80
Cdd:cd02066   3 VVFSKSTCPYCKRAKRLLESL-----GIEFEEIDILEDGELREELKELSGWP--TVPQIFINGEFIGGYDDLKALHE 72
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
4-74 1.56e-17

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 69.46  E-value: 1.56e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493862703  4 VIFGRPGCPYCVRAKELAEKLteerdDFNFRYVDIHAEGITKADLEKTVGkpVETVPQIFLDQKHIGGCTD 74
Cdd:COG0695   3 TLYTTPGCPYCARAKRLLDEK-----GIPYEEIDVDEDPEAREELRERSG--RRTVPVIFIGGEHLGGFDE 66
Glutaredoxin pfam00462
Glutaredoxin;
4-69 2.01e-14

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 61.37  E-value: 2.01e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493862703   4 VIFGRPGCPYCVRAKELAEKLteerdDFNFRYVDIHAEGITKADLEKTVGKPveTVPQIFLDQKHI 69
Cdd:pfam00462  2 VLYTKPTCPFCKRAKRLLKSL-----GVDFEEIDVDEDPEIREELKELSGWP--TVPQVFIDGEHI 60
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 4-50 4.81e-04

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: 35.13  E-value: 4.81e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 493862703  4 VIFGRPGCPYCVRAKE-LAEKLTEerddfnFRYVDIHAEGITKADLEK 50
Cdd:NF041212  2 VIYTKPGCPYCAAAKEdLARRGIP------FEEIDVSKDPEALEEMLR 43
UPxT_UxV_star NF041114
UXX-star (seleno)protein family 1;
4-67 2.73e-03

UXX-star (seleno)protein family 1;


Pssm-ID: 469037  Cd Length: 62  Bit Score: 32.93  E-value: 2.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493862703  4 VIFGRPGCPYCVRAKE-LAEKlteerddfnFRYVDIHAEgitKADLEK--TVGKPVETVPQIFLDQK 67
Cdd:NF041114  2 IIYGKDTCPYTRAAREaYAEK---------AEYIDVLKD---PEKLEEmlELSGGVRRVPVIVEDGK 56
 
Name Accession Description Interval E-value
grxA PRK11200
glutaredoxin 1; Provisional
 1-85 2.53e-65

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 190.63  E-value: 2.53e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703  1 MFAVIFGRPGCPYCVRAKELAEKLTEERDDFNFRYVDIHAEGITKADLEKTVGKPVETVPQIFLDQKHIGGCTDFEAYAK 80
Cdd:PRK11200  1 MFVVIFGRPGCPYCVRAKELAEKLSEERDDFDYRYVDIHAEGISKADLEKTVGKPVETVPQIFVDQKHIGGCTDFEAYVK 80


                ....*
gi 493862703 81 EHLGL 85
Cdd:PRK11200 81 ENLGL 85
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-87 5.13e-52

Glutaredoxin, GrxA 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 model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.


Pssm-ID: 131238 [Multi-domain]  Cd Length: 86  Bit Score: 157.30  E-value: 5.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703   2 FAVIFGRPGCPYCVRAKELAEKLTEERDDFNFRYVDIHAEGITKADLEKTVGKPVETVPQIFLDQKHIGGCTDFEAYAKE 81
Cdd:TIGR02183  1 FVVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDIHAEGISKADLEKTVGKPVETVPQIFVDEKHVGGCTDFEQLVKE 80


                 ....*.
gi 493862703  82 HLGLFA 87
Cdd:TIGR02183 81 NFDIEA 86
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 4-80 1.48e-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: 72.11  E-value: 1.48e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493862703  4 VIFGRPGCPYCVRAKELAEKLteerdDFNFRYVDIHAEGITKADLEKTVGKPveTVPQIFLDQKHIGGCTDFEAYAK 80
Cdd:cd02066   3 VVFSKSTCPYCKRAKRLLESL-----GIEFEEIDILEDGELREELKELSGWP--TVPQIFINGEFIGGYDDLKALHE 72
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
4-74 1.56e-17

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 69.46  E-value: 1.56e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493862703  4 VIFGRPGCPYCVRAKELAEKLteerdDFNFRYVDIHAEGITKADLEKTVGkpVETVPQIFLDQKHIGGCTD 74
Cdd:COG0695   3 TLYTTPGCPYCARAKRLLDEK-----GIPYEEIDVDEDPEAREELRERSG--RRTVPVIFIGGEHLGGFDE 66
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 4-81 8.93e-17

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: 67.95  E-value: 8.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703  4 VIFGRPGCPYCVRAKELAEKLteerddfNFRY----VDIHAEG--ITKAdLEKTVGKPveTVPQIFLDQKHIGGCTDFEA 77
Cdd:cd03419   3 VVFSKSYCPYCKRAKSLLKEL-------GVKPavveLDQHEDGseIQDY-LQELTGQR--TVPNVFIGGKFIGGCDDLMA 72


                ....
gi 493862703 78 YAKE 81
Cdd:cd03419  73 LHKS 76
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 4-81 3.05e-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: 64.19  E-value: 3.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703   4 VIFGRPGCPYCVRAKELAEKL------TEERDDFNfryvdiHAEGITKAdLEKTVGKpvETVPQIFLDQKHIGGCTDFEA 77
Cdd:TIGR02180  2 VVFSKSYCPYCKKAKEILAKLnvkpyeVVELDQLS------NGSEIQDY-LEEITGQ--RTVPNIFINGKFIGGCSDLLA 72


                 ....
gi 493862703  78 YAKE 81
Cdd:TIGR02180 73 LYKN 76
Glutaredoxin pfam00462
Glutaredoxin;
4-69 2.01e-14

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 61.37  E-value: 2.01e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493862703   4 VIFGRPGCPYCVRAKELAEKLteerdDFNFRYVDIHAEGITKADLEKTVGKPveTVPQIFLDQKHI 69
Cdd:pfam00462  2 VLYTKPTCPFCKRAKRLLKSL-----GVDFEEIDVDEDPEIREELKELSGWP--TVPQVFIDGEHI 60
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 2-78 3.78e-13

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: 58.68  E-value: 3.78e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493862703  2 FAVIFGRPGCPYCVRAKE-LAEKlteerddfNFRYVDIH-AEGITKADLEKTVGKpvETVPQIFLDQKHIGGCTDFEAY 78
Cdd:cd03029   2 SVSLFTKPGCPFCARAKAaLQEN--------GISYEEIPlGKDITGRSLRAVTGA--MTVPQVFIDGELIGGSDDLEKY 70
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 4-81 2.27e-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: 56.44  E-value: 2.27e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493862703  4 VIFGRPGCPYCVRAKELAEKlteerDDFNFRYVDIHAEGITKADLEKTVGKpVETVPQIFLDQKHIGGCTDFEAYAKE 81
Cdd:cd03418   3 EIYTKPNCPYCVRAKALLDK-----KGVDYEEIDVDGDPALREEMINRSGG-RRTVPQIFIGDVHIGGCDDLYALERK 74
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 4-78 4.31e-12

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: 56.00  E-value: 4.31e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493862703   4 VIFGRPGCPYCVRAKE-LAEKlteerddfNFRYVDIH-AEGITKADLEKTVGKpvETVPQIFLDQKHIGGCTDFEAY 78
Cdd:TIGR02190 11 VVFTKPGCPFCAKAKAtLKEK--------GYDFEEIPlGNDARGRSLRAVTGA--TTVPQVFIGGKLIGGSDELEAY 77
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 4-74 4.59e-11

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: 53.42  E-value: 4.59e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493862703   4 VIFGRPGCPYCVRAKELaekLTEERDDFNfryvDIHAEGITKADLE--KTVGKpvETVPQIFLDQKHIGGCTD 74
Cdd:TIGR02181  2 TIYTKPYCPYCTRAKAL---LSSKGVTFT----EIRVDGDPALRDEmmQRSGR--RTVPQIFIGDVHVGGCDD 65
PRK10638 PRK10638
glutaredoxin 3; Provisional
 5-77 2.62e-10

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 51.74  E-value: 2.62e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493862703  5 IFGRPGCPYCVRAKELAEklteeRDDFNFRYVDIHAEGITKADLEKTVGKpvETVPQIFLDQKHIGGCTDFEA 77
Cdd:PRK10638  6 IYTKATCPFCHRAKALLN-----SKGVSFQEIPIDGDAAKREEMIKRSGR--TTVPQIFIDAQHIGGCDDLYA 71
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 4-76 2.38e-09

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: 2.38e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493862703  4 VIFGRPGCPYCVRAKELaekLTEERDDFNFRYVDIHAEgiTKADLEKTVGKpvETVPQIFLDQKHIGGCTDFE 76
Cdd:cd03027   4 TIYSRLGCEDCTAVRLF---LREKGLPYVEINIDIFPE--RKAELEERTGS--SVVPQIFFNEKLVGGLTDLK 69
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 4-70 2.08e-04

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: 36.14  E-value: 2.08e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493862703  4 VIFGRPGCPYCVRAKELAEKLTEERDDFNFRYVDIHAEGITKADLEKtvgKPVETVPQIFLDQKHIG 70
Cdd:cd01659   2 VLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKR---YGVGGVPTLVVFGPGIG 65
Glrx-like pfam05768
Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This ...
 4-65 4.42e-04

Glutaredoxin-like domain (DUF836); These proteins are related to the pfam00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterized member is G4L from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L.


Pssm-ID: 399055  Cd Length: 80  Bit Score: 35.34  E-value: 4.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493862703   4 VIFGRPGCPYCVRAKELAEKLTEErDDFNFRYVDIhaegITKADLEKTVGkpvETVPQIFLD 65
Cdd:pfam05768  2 TLYGKPGCGLCEGAEEVLEPLALE-LGFELEVIDI----DGDPELLAKYG---LEIPVLAFV 55
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 4-50 4.81e-04

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: 35.13  E-value: 4.81e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 493862703  4 VIFGRPGCPYCVRAKE-LAEKLTEerddfnFRYVDIHAEGITKADLEK 50
Cdd:NF041212  2 VIYTKPGCPYCAAAKEdLARRGIP------FEEIDVSKDPEALEEMLR 43
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 4-71 7.22e-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: 34.89  E-value: 7.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493862703  4 VIFGRPGCPYCVRAKELaekLTEERDDFNFRYVDIHAEGItkADLEKTVGKPveTVPQIFLDQKHIGG 71
Cdd:cd02976   3 TVYTKPDCPYCKATKRF---LDERGIPFEEVDVDEDPEAL--EELKKLNGYR--SVPVVVIGDEHLSG 63
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
7-72 1.71e-03

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 34.49  E-value: 1.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493862703   7 GRPGCPYCVRAKELAEKLTE--ERddfnFRYVDIHAEGITKADLEKTVGKPveTVPQIFLDQKHIGGC 72
Cdd:PRK10824  23 GSPKLPSCGFSAQAVQALSAcgER----FAYVDILQNPDIRAELPKYANWP--TFPQLWVDGELVGGC 84
SoxW cd02951
SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, ...
 1-54 2.22e-03

SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, encoded by a genetic locus (sox operon) involved in thiosulfate oxidation. Sulfur bacteria oxidize sulfur compounds to provide reducing equivalents for carbon dioxide fixation during autotrophic growth and the respiratory electron transport chain. It is unclear what the role of SoxW is, since it has been found to be dispensable in the oxidation of thiosulfate to sulfate. SoxW is specifically kept in the reduced state by SoxV, which is essential in thiosulfate oxidation.


Pssm-ID: 239249 [Multi-domain]  Cd Length: 125  Bit Score: 34.60  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493862703   1 MFAVIFGRPGCPYCVRAKE--LAEKLTEE--RDDFNFRYVDIHAEGI-TKADLEKTVGK 54
Cdd:cd02951   16 PLLLLFSQPGCPYCDKLKRdyLNDPAVQAyiRAHFVVVYINIDGDKEvTDFDGEALSEK 74
UPxT_UxV_star NF041114
UXX-star (seleno)protein family 1;
4-67 2.73e-03

UXX-star (seleno)protein family 1;


Pssm-ID: 469037  Cd Length: 62  Bit Score: 32.93  E-value: 2.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493862703  4 VIFGRPGCPYCVRAKE-LAEKlteerddfnFRYVDIHAEgitKADLEK--TVGKPVETVPQIFLDQK 67
Cdd:NF041114  2 IIYGKDTCPYTRAAREaYAEK---------AEYIDVLKD---PEKLEEmlELSGGVRRVPVIVEDGK 56
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
2-80 5.14e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 33.17  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862703    2 FAVIFGRPGCPYCVRAKELAEKLTE----ERDDFNFRYVDI-----HAEGITKADLEKTVGK--PVETVPQI-FLDQK-- 67
Cdd:pfam13098   7 VLVVFTDPDCPYCKKLKKELLEDPDvtvyLGPNFVFIAVNIwcakeVAKAFTDILENKELGRkyGVRGTPTIvFFDGKge 86

                          90
                  ....*....|....*
gi 493862703   68 --HIGGCTDFEAYAK 80
Cdd:pfam13098  87 llRLPGYVPAEEFLA 101
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 4-71 7.07e-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: 32.35  E-value: 7.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493862703   4 VIFGRPGCPYCVRAKELAEKLteerdDFNFRYVDIHAEGITKADLEKTVGKpvETVPQIFLDQKHIGG 71
Cdd:TIGR02196  3 KVYTTPWCPPCVKAKEYLTSK-----GVAFEEIDVEKDAAAREELLKVYGQ--RGVPVIVIGHKIVVG 63
 
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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