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Conserved domains on  [gi|30688093|ref|NP_194602|]
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Glutaredoxin family protein [Arabidopsis thaliana]

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 ...
 82-161 3.44e-37

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: 123.03  E-value: 3.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093  82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLgPQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDLE 161
Cdd:cd03419   2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQH-EDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
 
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 ...
 82-161 3.44e-37

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: 123.03  E-value: 3.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093  82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLgPQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDLE 161
Cdd:cd03419   2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQH-EDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 82-164 9.86e-31

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: 106.56  E-value: 9.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093    82 VVIYSKTWCSYCTEVKTLFKRLGVQPL-VVELDQLGPqGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDL 160
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKPYeVVELDQLSN-GSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKL 79


                  ....
gi 30688093   161 ELML 164
Cdd:TIGR02180  80 AELL 83
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
81-165 3.91e-17

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 71.77  E-value: 3.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093  81 TVVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDqlgpQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDtvklnrkGDL 160
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVD----EDPEAREELRERSGRRTVPVIFIGGEHLGGFDE-------GEL 69


                ....*
gi 30688093 161 ELMLA 165
Cdd:COG0695  70 DALLA 74
Glutaredoxin pfam00462
Glutaredoxin;
82-145 1.16e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 69.84  E-value: 1.16e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30688093    82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLgpqgPQLQKVLERLTGQHTVPNVFVCGKHI 145
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDED----PEIREELKELSGWPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
 81-164 1.16e-11

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 57.52  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093   81 TVVIYSKTWCSYCTEVKTLFKRLGV--QPLVVELDqlgpqgPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKG 158
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNSKGVsfQEIPIDGD------AAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARG 76


                 ....*.
gi 30688093  159 DLELML 164
Cdd:PRK10638  77 GLDPLL 82
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 82-142 6.12e-05

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: 39.37  E-value: 6.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30688093   82 VVIYSKTWCSYCTEVKTLFKRLGVQplVVELDQLgpQGPQLQKVLERLT-GQHTVPnVFVCG 142
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLARRGIP--FEEIDVS--KDPEALEEMLRLTgGERIVP-VIVEG 57
 
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 ...
 82-161 3.44e-37

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: 123.03  E-value: 3.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093  82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLgPQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDLE 161
Cdd:cd03419   2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQH-EDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
 82-164 9.86e-31

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: 106.56  E-value: 9.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093    82 VVIYSKTWCSYCTEVKTLFKRLGVQPL-VVELDQLGPqGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDL 160
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKPYeVVELDQLSN-GSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKL 79


                  ....
gi 30688093   161 ELML 164
Cdd:TIGR02180  80 AELL 83
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 82-156 4.19e-23

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: 86.75  E-value: 4.19e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30688093  82 VVIYSKTWCSYCTEVKTLFKRLGVQplVVELDQLgpQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNR 156
Cdd:cd02066   2 VVVFSKSTCPYCKRAKRLLESLGIE--FEEIDIL--EDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 73-168 4.36e-21

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: 82.50  E-value: 4.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093    73 IRKTVTENTVVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQlGPQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTV 152
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDK-EPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVM 79

                          90
                  ....*....|....*.
gi 30688093   153 KLNRKGDLELMLAEAN 168
Cdd:TIGR02189  80 ALHISGSLVPMLKQAG 95
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 82-164 6.17e-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: 73.83  E-value: 6.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093    82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQlgpQGPQLQKVLERlTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDLE 161
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDG---DPALRDEMMQR-SGRRTVPQIFIGDVHVGGCDDLYALDREGKLD 76


                  ...
gi 30688093   162 LML 164
Cdd:TIGR02181  77 PLL 79
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 81-158 9.88e-18

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: 73.01  E-value: 9.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093  81 TVVIYSKTWCSYCTEVKTLFKRLGVQP--LVVELDQlgpqgPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKG 158
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLDKKGVDYeeIDVDGDP-----ALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYALERKG 75
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
81-165 3.91e-17

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 71.77  E-value: 3.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093  81 TVVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDqlgpQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDtvklnrkGDL 160
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVD----EDPEAREELRERSGRRTVPVIFIGGEHLGGFDE-------GEL 69


                ....*
gi 30688093 161 ELMLA 165
Cdd:COG0695  70 DALLA 74
Glutaredoxin pfam00462
Glutaredoxin;
82-145 1.16e-16

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 69.84  E-value: 1.16e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30688093    82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLgpqgPQLQKVLERLTGQHTVPNVFVCGKHI 145
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDED----PEIREELKELSGWPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
 81-164 1.16e-11

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 57.52  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093   81 TVVIYSKTWCSYCTEVKTLFKRLGV--QPLVVELDqlgpqgPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKG 158
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNSKGVsfQEIPIDGD------AAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARG 76


                 ....*.
gi 30688093  159 DLELML 164
Cdd:PRK10638  77 GLDPLL 82
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 82-154 6.42e-10

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: 52.80  E-value: 6.42e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30688093  82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLgpqgPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKL 154
Cdd:cd03027   3 VTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIF----PERKAELEERTGSSVVPQIFFNEKLVGGLTDLKSL 71
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 78-147 2.03e-09

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: 51.76  E-value: 2.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093    78 TENTVVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQlGPQGpqlqKVLERLTGQHTVPNVFVCGKHIGG 147
Cdd:TIGR02190   6 KPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGN-DARG----RSLRAVTGATTVPQVFIGGKLIGG 70
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 81-147 8.43e-09

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: 49.92  E-value: 8.43e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30688093  81 TVVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDqlgpQGPQLQKVLERLTGQHTVPNVFVCGKHIGG 147
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVD----EDPEALEELKKLNGYRSVPVVVIGDEHLSG 63
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 82-153 6.56e-08

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: 47.51  E-value: 6.56e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30688093  82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQlgpqgPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVK 153
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGK-----DITGRSLRAVTGAMTVPQVFIDGELIGGSDDLEK 69
PHA03050 PHA03050
glutaredoxin; Provisional
 70-155 3.61e-07

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 46.55  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688093   70 EESIRKTVTENTVVIYSKTWCSYCTEV-----KTLFKRLGVQplVVELDQLGPQGpQLQKVLERLTGQHTVPNVFVCGKH 144
Cdd:PHA03050   3 EEFVQQRLANNKVTIFVKFTCPFCRNAldilnKFSFKRGAYE--IVDIKEFKPEN-ELRDYFEQITGGRTVPRIFFGKTS 79

                         90
                 ....*....|.
gi 30688093  145 IGGCTDTVKLN 155
Cdd:PHA03050  80 IGGYSDLLEID 90
grxA PRK11200
glutaredoxin 1; Provisional
 82-150 3.35e-06

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 43.10  E-value: 3.35e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30688093   82 VVIYSKTWCSYCTEVKTLFKRLgvqplVVELDQLG-------PQGPQLQKvLERLTGQ--HTVPNVFVCGKHIGGCTD 150
Cdd:PRK11200   3 VVIFGRPGCPYCVRAKELAEKL-----SEERDDFDyryvdihAEGISKAD-LEKTVGKpvETVPQIFVDQKHIGGCTD 74
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 81-147 3.24e-05

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: 40.44  E-value: 3.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30688093    81 TVVIYSKTWCSYCTEVKTLFKRLGVQplVVELDQlgPQGPQLQKVLERLTGQHTVPNVFVCGKHIGG 147
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVA--FEEIDV--EKDAAAREELLKVYGQRGVPVIVIGHKIVVG 63
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 82-142 6.12e-05

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: 39.37  E-value: 6.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30688093   82 VVIYSKTWCSYCTEVKTLFKRLGVQplVVELDQLgpQGPQLQKVLERLT-GQHTVPnVFVCG 142
Cdd:NF041212   1 VVIYTKPGCPYCAAAKEDLARRGIP--FEEIDVS--KDPEALEEMLRLTgGERIVP-VIVEG 57
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 82-150 9.20e-05

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: 39.43  E-value: 9.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30688093    82 VVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLGPQGPQLQKV-LERLTGQ--HTVPNVFVCGKHIGGCTD 150
Cdd:TIGR02183   2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDIHAEGISKAdLEKTVGKpvETVPQIFVDEKHVGGCTD 73
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 119-167 2.98e-03

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: 36.45  E-value: 2.98e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 30688093 119 GPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDLELMLAEA 167
Cdd:cd03031  45 REELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGI 93
 
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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