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Conserved domains on  [gi|4504025|ref|NP_002055|]
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glutaredoxin-1 [Homo sapiens]

Protein Classification

GRX_euk family protein( domain architecture ID 10797815)

GRX_euk family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 15-99 5.91e-41

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: 130.06  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQLPIKQglLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKP--YEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78


                  ....*
gi 4504025     95 LLTRL 99
Cdd:TIGR02180  79 LAELL 83
 
Name Accession Description Interval E-value
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 15-99 5.91e-41

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: 130.06  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQLPIKQglLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKP--YEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78


                  ....*
gi 4504025     95 LLTRL 99
Cdd:TIGR02180  79 LAELL 83
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 14-96 1.60e-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: 118.80  E-value: 1.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEfVDITAtnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSG 93
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVE-LDQHE--DGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ...
gi 4504025   94 ELL 96
Cdd:cd03419  78 KLV 80
PHA03050 PHA03050
glutaredoxin; Provisional
 1-106 4.19e-29

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 100.86  E-value: 4.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025     1 MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:PHA03050   1 MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80

                         90       100
                 ....*....|....*....|....*.
gi 4504025    81 GGCSDLVSLQQSGELLTRLKQIGALQ 106
Cdd:PHA03050  81 GGYSDLLEIDNMDALGDILSSIGVLR 106
Glutaredoxin pfam00462
Glutaredoxin;
15-80 2.33e-17

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 69.46  E-value: 2.33e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITAtnhTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVD---FEEIDVDE---DPEIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
14-85 3.02e-16

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 67.15  E-value: 3.02e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITatnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSD 85
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIP---YEEIDVD---EDPEAREELRERSGRRTVPVIFIGGEHLGGFDE 66
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 15-71 1.31e-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: 37.06  E-value: 1.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504025    15 VVVFIKPTCPYCRRAQEILSqlpiKQGlLEFVDITATNHTnEIQDYLQQLTGA-RTVP 71
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLA----RRG-IPFEEIDVSKDP-EALEEMLRLTGGeRIVP 52
 
Name Accession Description Interval E-value
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 15-99 5.91e-41

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: 130.06  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQLPIKQglLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKP--YEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78


                  ....*
gi 4504025     95 LLTRL 99
Cdd:TIGR02180  79 LAELL 83
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 14-96 1.60e-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: 118.80  E-value: 1.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEfVDITAtnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSG 93
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVE-LDQHE--DGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77


                ...
gi 4504025   94 ELL 96
Cdd:cd03419  78 KLV 80
PHA03050 PHA03050
glutaredoxin; Provisional
 1-106 4.19e-29

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 100.86  E-value: 4.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025     1 MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:PHA03050   1 MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80

                         90       100
                 ....*....|....*....|....*.
gi 4504025    81 GGCSDLVSLQQSGELLTRLKQIGALQ 106
Cdd:PHA03050  81 GGYSDLLEIDNMDALGDILSSIGVLR 106
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 14-91 9.94e-25

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: 88.68  E-value: 9.94e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQ 91
Cdd:cd02066   1 KVVVFSKSTCPYCKRAKRLLESLGIE---FEEIDILEDG---ELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 15-95 8.01e-18

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: 71.14  E-value: 8.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQlpikQGLlEFVDITATNHTNEiQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGE 94
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSS----KGV-TFTEIRVDGDPAL-RDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGK 74


                  .
gi 4504025     95 L 95
Cdd:TIGR02181  75 L 75
Glutaredoxin pfam00462
Glutaredoxin;
15-80 2.33e-17

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 69.46  E-value: 2.33e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITAtnhTNEIQDYLQQLTGARTVPRVFIGKDCI 80
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVD---FEEIDVDE---DPEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 14-93 6.03e-17

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: 68.77  E-value: 6.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSqlpiKQGLlEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSG 93
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLD----KKGV-DYEEIDVDGDPALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYALERKG 75
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
14-85 3.02e-16

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 67.15  E-value: 3.02e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITatnHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSD 85
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIP---YEEIDVD---EDPEAREELRERSGRRTVPVIFIGGEHLGGFDE 66
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 15-105 2.44e-13

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: 60.55  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGE 94
Cdd:TIGR02189  10 VVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGK---DIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHISGS 86

                          90
                  ....*....|.
gi 4504025     95 LLTRLKQIGAL 105
Cdd:TIGR02189  87 LVPMLKQAGAL 97
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 12-86 2.75e-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: 57.16  E-value: 2.75e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504025     12 PGKVVVFIKPTCPYCRRAQEILsqlpiKQGLLEFVDITATNHTNEIQdyLQQLTGARTVPRVFIGKDCIGGCSDL 86
Cdd:TIGR02190   7 PESVVVFTKPGCPFCAKAKATL-----KEKGYDFEEIPLGNDARGRS--LRAVTGATTVPQVFIGGKLIGGSDEL 74
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 15-86 5.23e-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: 56.37  E-value: 5.23e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504025   15 VVVFIKPTCPYCRRAQEILSQlpikQGLlEFVDITATNHTNEIQdyLQQLTGARTVPRVFIGKDCIGGCSDL 86
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALQE----NGI-SYEEIPLGKDITGRS--LRAVTGAMTVPQVFIDGELIGGSDDL 67
grxA PRK11200
glutaredoxin 1; Provisional
 14-85 4.33e-11

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 54.27  E-value: 4.33e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504025    14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLEF--VDITATNHTNEiqDyLQQLTG--ARTVPRVFIGKDCIGGCSD 85
Cdd:PRK11200   2 FVVIFGRPGCPYCVRAKELAEKLSEERDDFDYryVDIHAEGISKA--D-LEKTVGkpVETVPQIFVDQKHIGGCTD 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 14-100 2.33e-10

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 52.51  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025    14 KVVVFIKPTCPYCRRAQEILSQlpikQGLlEFVDItATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSG 93
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNS----KGV-SFQEI-PIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARG 76


                 ....*..
gi 4504025    94 ELLTRLK 100
Cdd:PRK10638  77 GLDPLLK 83
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 14-78 1.20e-08

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: 47.60  E-value: 1.20e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSQLPIkqgllEFVDITATNHTNEIqDYLQQLTGARTVPRVFIGKD 78
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDERGI-----PFEEVDVDEDPEAL-EELKKLNGYRSVPVVVIGDE 59
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 13-89 3.92e-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: 46.25  E-value: 3.92e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504025   13 GKVVVFIKPTCPYCRRAQEILSQLPIKqglleFVDITATNHTnEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSL 89
Cdd:cd03027   1 GRVTIYSRLGCEDCTAVRLFLREKGLP-----YVEINIDIFP-ERKAELEERTGSSVVPQIFFNEKLVGGLTDLKSL 71
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 10-95 3.99e-08

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: 46.72  E-value: 3.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025   10 IQPGKVVVFIK-----PTCPYCRRAQEILSQLPIKqglLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKDCIGGCS 84
Cdd:cd03028   5 IKENPVVLFMKgtpeePRCGFSRKVVQILNQLGVD---FGTFDILEDE---EVRQGLKEYSNWPTFPQLYVNGELVGGCD 78

                        90
                ....*....|.
gi 4504025   85 DLVSLQQSGEL 95
Cdd:cd03028  79 IVKEMHESGEL 89
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 15-89 5.83e-08

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: 46.36  E-value: 5.83e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504025     15 VVVFIKPTCPYCRRAQEILSQLPIKQGLLEF--VDITATNHTNEiqdYLQQLTG--ARTVPRVFIGKDCIGGCSDLVSL 89
Cdd:TIGR02183   2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFryIDIHAEGISKA---DLEKTVGkpVETVPQIFVDEKHVGGCTDFEQL 77
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 14-82 1.01e-07

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: 45.45  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504025     14 KVVVFIKPTCPYCRRAQEILSQLPIKqglLEFVDITAtnhTNEIQDYLQQLTGARTVPRVFIGKDCIGG 82
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVA---FEEIDVEK---DAAAREELLKVYGQRGVPVIVIGHKIVVG 63
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 15-81 1.28e-06

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: 42.30  E-value: 1.28e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504025   15 VVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQltGARTVPRVFIGKDCIG 81
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELKRY--GVGGVPTLVVFGPGIG 65
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
14-104 1.31e-06

Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440047  Cd Length: 105  Bit Score: 43.18  E-value: 1.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025   14 KVVVFIK-----PTCPYCRRAQEILSQLPIKqglLEFVDITATNhtnEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVS 88
Cdd:COG0278  16 PVVLFMKgtpqfPQCGFSARAVQILNACGVD---FATVNVLEDP---EIRQGLKEYSNWPTIPQLYVKGEFIGGCDIIRE 89

                        90
                ....*....|....*.
gi 4504025   89 LQQSGELLTRLKQIGA 104
Cdd:COG0278  90 MYESGELQKLLEEAGA 105
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 14-106 4.18e-05

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


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 39.91  E-value: 4.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025   14 KVVVF------IKPTCPYCRRAQEILSQLPIKqgllefVDITATNHTNEIQDYLQQLTGAR----TVPRVFIGKDCIGGC 83
Cdd:cd03031   1 RVVLYttslrgVRKTFEDCNNVRAILESFRVK------FDERDVSMDSGFREELRELLGAElkavSLPRVFVDGRYLGGA 74

                        90       100
                ....*....|....*....|...
gi 4504025   84 SDLVSLQQSGELLTRLKQIGALQ 106
Cdd:cd03031  75 EEVLRLNESGELRKLLKGIRARA 97
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 15-71 1.31e-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: 37.06  E-value: 1.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504025    15 VVVFIKPTCPYCRRAQEILSqlpiKQGlLEFVDITATNHTnEIQDYLQQLTGA-RTVP 71
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLA----RRG-IPFEEIDVSKDP-EALEEMLRLTGGeRIVP 52
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 14-100 2.66e-04

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 38.47  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504025    14 KVVVFIKPTCPYCRRAQEIL--SQLPIKQGLLEfVDITATNHTNEI-QDYLQQLTGARTVPRVFIGKDCIGGCSDLVSlq 90
Cdd:PRK12759   3 EVRIYTKTNCPFCDLAKSWFgaNDIPFTQISLD-DDVKRAEFYAEVnKNILLVEEHIRTVPQIFVGDVHIGGYDNLMA-- 79

                         90
                 ....*....|
gi 4504025    91 QSGELLTRLK 100
Cdd:PRK12759  80 RAGEVIARVK 89
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 14-36 5.65e-04

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 36.90  E-value: 5.65e-04
                        10        20
                ....*....|....*....|...
gi 4504025   14 KVVVFIKPTCPYCRRAQEILSQL 36
Cdd:COG1651   3 TVVEFFDYQCPYCARFHPELPEL 25
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 12-36 1.28e-03

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 36.14  E-value: 1.28e-03
                        10        20
                ....*....|....*....|....*
gi 4504025   12 PGKVVVFIKPTCPYCRRAQEILSQL 36
Cdd:cd03020  78 KRVVYVFTDPDCPYCRKLEKELKPN 102
redox_disulf_1 TIGR00411
small redox-active disulfide protein 1; This protein is homologous to a family of proteins ...
 14-78 9.37e-03

small redox-active disulfide protein 1; This protein is homologous to a family of proteins that includes thioredoxins, glutaredoxins, protein-disulfide isomerases, and others, some of which have several such domains. The sequence of this protein at the redox-active disufide site, CPYC, matches glutaredoxins rather than thioredoxins, although its overall sequence seems closer to thioredoxins. It is suggested to be a ribonucleotide-reducing system component distinct from thioredoxin or glutaredoxin. [Unknown function, General]


Pssm-ID: 129505 [Multi-domain]  Cd Length: 82  Bit Score: 32.55  E-value: 9.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504025     14 KVVVFIKPTCPYCRRAQEILSQLPIKQGLLefVDITATNHTNEIQDYLQqlTGARTVPRVFIGKD 78
Cdd:TIGR00411   2 KIELFTSPTCPYCPAAKRVVEEVAKEMGDA--VEVEYINVMENPQKAME--YGIMAVPAIVINGD 62
 
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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