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Conserved domains on  [gi|1280040005|gb|ATY36134|]
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glutaredoxin, partial [Conus monile]

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 ...
 16-104 2.17e-36

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: 118.41  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLLENgelssedYEVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIGGGSEVADL 95
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKELGVK-------PAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMAL 73


                  ....*....
gi 1280040005  96 HKNKKLVPL 104
Cdd:cd03419    74 HKSGKLVKL 82
 
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 ...
 16-104 2.17e-36

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: 118.41  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLLENgelssedYEVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIGGGSEVADL 95
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKELGVK-------PAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMAL 73


                  ....*....
gi 1280040005  96 HKNKKLVPL 104
Cdd:cd03419    74 HKSGKLVKL 82
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 17-105 1.77e-33

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: 111.18  E-value: 1.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  17 VMMFSKTTCPFCEMAKNVFNKLLengelsSEDYEVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIGGGSEVADLH 96
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLN------VKPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALY 74


                  ....*....
gi 1280040005  97 KNKKLVPLL 105
Cdd:TIGR02180  75 KNGKLAELL 83
Glutaredoxin pfam00462
Glutaredoxin;
17-86 1.17e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 67.91  E-value: 1.17e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  17 VMMFSKTTCPFCEMAKNVFNKLlengelsSEDYEVMELDRDPncaAYQDYFKTLTGAKTVPRVFINGKCI 86
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSL-------GVDFEEIDVDEDP---EIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
16-106 1.52e-14

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 62.91  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLlengelsSEDYEVMELDRDPncaAYQDYFKTLTGAKTVPRVFINGKCIGGGSEvadl 95
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEK-------GIPYEEIDVDEDP---EAREELRERSGRRTVPVIFIGGEHLGGFDE---- 66

                          90
                  ....*....|.
gi 1280040005  96 hknKKLVPLLK 106
Cdd:COG0695    67 ---GELDALLA 74
PHA03050 PHA03050
glutaredoxin; Provisional
 8-107 4.69e-14

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 62.73  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005   8 VDEKIKNKKVMMFSKTTCPFCEMAKNVFNKLlengELSSEDYEVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIG 87
Cdd:PHA03050    6 VQQRLANNKVTIFVKFTCPFCRNALDILNKF----SFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIG 81

                          90       100
                  ....*....|....*....|
gi 1280040005  88 GGSEVADLHKNKKLVPLLKS 107
Cdd:PHA03050   82 GYSDLLEIDNMDALGDILSS 101
 
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 ...
 16-104 2.17e-36

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: 118.41  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLLENgelssedYEVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIGGGSEVADL 95
Cdd:cd03419     1 PVVVFSKSYCPYCKRAKSLLKELGVK-------PAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMAL 73


                  ....*....
gi 1280040005  96 HKNKKLVPL 104
Cdd:cd03419    74 HKSGKLVKL 82
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 17-105 1.77e-33

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: 111.18  E-value: 1.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  17 VMMFSKTTCPFCEMAKNVFNKLLengelsSEDYEVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIGGGSEVADLH 96
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLN------VKPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALY 74


                  ....*....
gi 1280040005  97 KNKKLVPLL 105
Cdd:TIGR02180  75 KNGKLAELL 83
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 16-97 4.22e-22

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: 81.74  E-value: 4.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLlengelsseDYEVMELDRDPNcAAYQDYFKTLTGAKTVPRVFINGKCIGGGSEVADL 95
Cdd:cd02066     1 KVVVFSKSTCPYCKRAKRLLESL---------GIEFEEIDILED-GELREELKELSGWPTVPQIFINGEFIGGYDDLKAL 70


                  ..
gi 1280040005  96 HK 97
Cdd:cd02066    71 HE 72
Glutaredoxin pfam00462
Glutaredoxin;
17-86 1.17e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 67.91  E-value: 1.17e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  17 VMMFSKTTCPFCEMAKNVFNKLlengelsSEDYEVMELDRDPncaAYQDYFKTLTGAKTVPRVFINGKCI 86
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSL-------GVDFEEIDVDEDP---EIREELKELSGWPTVPQVFIDGEHI 60
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 12-106 7.54e-15

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: 64.40  E-value: 7.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  12 IKNKKVMMFSKTTCPFCEMAKNVFNKLLENGElssedyeVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIGGGSE 91
Cdd:TIGR02189   5 VSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPA-------VHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLEN 77

                          90
                  ....*....|....*
gi 1280040005  92 VADLHKNKKLVPLLK 106
Cdd:TIGR02189  78 VMALHISGSLVPMLK 92
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
16-106 1.52e-14

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 62.91  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLlengelsSEDYEVMELDRDPncaAYQDYFKTLTGAKTVPRVFINGKCIGGGSEvadl 95
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEK-------GIPYEEIDVDEDP---EAREELRERSGRRTVPVIFIGGEHLGGFDE---- 66

                          90
                  ....*....|.
gi 1280040005  96 hknKKLVPLLK 106
Cdd:COG0695    67 ---GELDALLA 74
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 13-94 2.14e-14

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: 62.55  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  13 KNKKVMMFSKTTCPFCEMAKNVfnkLLENGElsseDYEVMELDRDpncaAYQDYFKTLTGAKTVPRVFINGKCIGGGSEV 92
Cdd:TIGR02190   6 KPESVVVFTKPGCPFCAKAKAT---LKEKGY----DFEEIPLGND----ARGRSLRAVTGATTVPQVFIGGKLIGGSDEL 74


                  ..
gi 1280040005  93 AD 94
Cdd:TIGR02190  75 EA 76
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 17-105 2.67e-14

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: 62.28  E-value: 2.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  17 VMMFSKTTCPFCEMAKnvfnKLLENGELSSEDYEVmelDRDPncAAYQDYFKtLTGAKTVPRVFINGKCIGGGSEVADLH 96
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAK----ALLSSKGVTFTEIRV---DGDP--ALRDEMMQ-RSGRRTVPQIFIGDVHVGGCDDLYALD 70


                  ....*....
gi 1280040005  97 KNKKLVPLL 105
Cdd:TIGR02181  71 REGKLDPLL 79
PHA03050 PHA03050
glutaredoxin; Provisional
 8-107 4.69e-14

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 62.73  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005   8 VDEKIKNKKVMMFSKTTCPFCEMAKNVFNKLlengELSSEDYEVMELDRDPNCAAYQDYFKTLTGAKTVPRVFINGKCIG 87
Cdd:PHA03050    6 VQQRLANNKVTIFVKFTCPFCRNALDILNKF----SFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIG 81

                          90       100
                  ....*....|....*....|
gi 1280040005  88 GGSEVADLHKNKKLVPLLKS 107
Cdd:PHA03050   82 GYSDLLEIDNMDALGDILSS 101
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 15-94 3.24e-12

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: 56.76  E-value: 3.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  15 KKVMMFSKTTCPFCEMAKNVfnkLLENGElsseDYEVMELDRDPNCAAyqdyFKTLTGAKTVPRVFINGKCIGGGSEVAD 94
Cdd:cd03029     1 ESVSLFTKPGCPFCARAKAA---LQENGI----SYEEIPLGKDITGRS----LRAVTGAMTVPQVFIDGELIGGSDDLEK 69
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 16-95 2.09e-11

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: 54.90  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKlleNGElsseDYEVMELDRDPncAAYQDYFKTLTGAKTVPRVFINGKCIGGGSEVADL 95
Cdd:cd03418     1 KVEIYTKPNCPYCVRAKALLDK---KGV----DYEEIDVDGDP--ALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYAL 71
PRK10638 PRK10638
glutaredoxin 3; Provisional
 16-106 4.25e-10

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 51.74  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVfnkllengeLSSEDYEVMELDRDPNCAAYQDYFKTlTGAKTVPRVFINGKCIGGGSEVADL 95
Cdd:PRK10638    3 NVEIYTKATCPFCHRAKAL---------LNSKGVSFQEIPIDGDAAKREEMIKR-SGRTTVPQIFIDAQHIGGCDDLYAL 72

                          90
                  ....*....|.
gi 1280040005  96 HKNKKLVPLLK 106
Cdd:PRK10638   73 DARGGLDPLLK 83
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 47-106 2.56e-06

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 42.99  E-value: 2.56e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1280040005  47 EDYEVMELDRDPNC-AAYQDYFKTLTGAK----TVPRVFINGKCIGGGSEVADLHKNKKLVPLLK 106
Cdd:cd03031    27 ESFRVKFDERDVSMdSGFREELRELLGAElkavSLPRVFVDGRYLGGAEEVLRLNESGELRKLLK 91
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 16-91 3.00e-06

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: 41.44  E-value: 3.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLlengelsSEDYEVMELDRDPncaAYQDYFKTLTGAKTVPRVFINGKCIGGGSE 91
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDER-------GIPFEEVDVDEDP---EALEELKKLNGYRSVPVVVIGDEHLSGFRP 66
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 8-102 2.68e-05

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: 39.40  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005   8 VDEKIKNKKVMMFSKTT--CPFCEMAKNVFNKLLENGeLSSEDYEVMEldrDPNcaaYQDYFKTLTGAKTVPRVFINGKC 85
Cdd:cd03028     1 IKKLIKENPVVLFMKGTpeEPRCGFSRKVVQILNQLG-VDFGTFDILE---DEE---VRQGLKEYSNWPTFPQLYVNGEL 73

                          90
                  ....*....|....*..
gi 1280040005  86 IGGGSEVADLHKNKKLV 102
Cdd:cd03028    74 VGGCDIVKEMHESGELQ 90
grxA PRK11200
glutaredoxin 1; Provisional
 16-99 3.62e-04

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 36.55  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKLLENGElsseDYEVMELDRDPNCAAYQDYFKTLTGA-KTVPRVFINGKCIGGGSEVAD 94
Cdd:PRK11200    2 FVVIFGRPGCPYCVRAKELAEKLSEERD----DFDYRYVDIHAEGISKADLEKTVGKPvETVPQIFVDQKHIGGCTDFEA 77


                  ....*
gi 1280040005  95 LHKNK 99
Cdd:PRK11200   78 YVKEN 82
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 16-95 1.67e-03

Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.


Pssm-ID: 239325 [Multi-domain]  Cd Length: 73  Bit Score: 34.31  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  16 KVMMFSKTTCPFCEMAKNVFNKllengelSSEDYEVMELDRDPNCAAYqdyFKTLTGAKTVPRVFINGKCIGGGSEVADL 95
Cdd:cd03027     2 RVTIYSRLGCEDCTAVRLFLRE-------KGLPYVEINIDIFPERKAE---LEERTGSSVVPQIFFNEKLVGGLTDLKSL 71
PTZ00062 PTZ00062
glutaredoxin; Provisional
 12-101 2.91e-03

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 35.16  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280040005  12 IKNKKVMMFSK--TTCPFCEMAKNVFNKLLENGeLSSEDYEVMEldrDPNCaayQDYFKTLTGAKTVPRVFINGKCIGGG 89
Cdd:PTZ00062  110 IRNHKILLFMKgsKTFPFCRFSNAVVNMLNSSG-VKYETYNIFE---DPDL---REELKVYSNWPTYPQLYVNGELIGGH 182

                          90
                  ....*....|..
gi 1280040005  90 SEVADLHKNKKL 101
Cdd:PTZ00062  183 DIIKELYESNSL 194
 
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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