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Conserved domains on  [gi|115532750|ref|NP_001040891|]
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Glutaredoxin domain-containing protein [Caenorhabditis elegans]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 21-102 1.97e-17

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03418:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 75  Bit Score: 70.69  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTlkasQPDDYLGIVNglvYTTRQTSVPQIFVCGRFIGGYTELDALRN 100
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDG----DPALREEMIN---RSGGRRTVPQIFIGDVHIGGCDDLYALER 73


                 ..
gi 115532750 101 SG 102
Cdd:cd03418   74 KG 75
 
Name Accession Description Interval E-value
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 21-102 1.97e-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: 70.69  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTlkasQPDDYLGIVNglvYTTRQTSVPQIFVCGRFIGGYTELDALRN 100
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDG----DPALREEMIN---RSGGRRTVPQIFIGDVHIGGCDDLYALER 73


                 ..
gi 115532750 101 SG 102
Cdd:cd03418   74 KG 75
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 22-104 3.69e-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: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750   22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTlkasQPDDYLGIVNglvyTTRQTSVPQIFVCGRFIGGYTELDALRNS 101
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDG----DPALRDEMMQ----RSGRRTVPQIFIGDVHVGGCDDLYALDRE 72


                  ...
gi 115532750  102 GHL 104
Cdd:TIGR02181  73 GKL 75
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
21-98 3.87e-14

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 62.14  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQpdDYLGIVNGlvyttrQTSVPQIFVCGRFIGGYT--ELDAL 98
Cdd:COG0695    1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAR--EELRERSG------RRTVPVIFIGGEHLGGFDegELDAL 72
Glutaredoxin pfam00462
Glutaredoxin;
22-89 3.59e-13

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 59.44  E-value: 3.59e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115532750   22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQpdDYLGIVNGlvyttrQTSVPQIFVCGRFI 89
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIR--EELKELSG------WPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
 22-104 3.32e-12

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 57.52  E-value: 3.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQPDdylgivngLVYTTRQTSVPQIFVCGRFIGGYTELDALRNS 101
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREE--------MIKRSGRTTVPQIFIDAQHIGGCDDLYALDAR 75


                 ...
gi 115532750 102 GHL 104
Cdd:PRK10638  76 GGL 78
 
Name Accession Description Interval E-value
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 21-102 1.97e-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: 70.69  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTlkasQPDDYLGIVNglvYTTRQTSVPQIFVCGRFIGGYTELDALRN 100
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDG----DPALREEMIN---RSGGRRTVPQIFIGDVHIGGCDDLYALER 73


                 ..
gi 115532750 101 SG 102
Cdd:cd03418   74 KG 75
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 21-98 2.84e-17

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: 70.19  E-value: 2.84e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLdtlkasqpDDYLGIVNGLVYTTRQTSVPQIFVCGRFIGGYTELDAL 98
Cdd:cd02066    1 KVVVFSKSTCPYCKRAKRLLESLGIEFEEIDI--------LEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKAL 70
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 21-104 4.34e-17

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.


Pssm-ID: 239511 [Multi-domain]  Cd Length: 82  Bit Score: 69.88  E-value: 4.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKA-SQPDDYLGIVNGlvyttrQTSVPQIFVCGRFIGGYTELDALR 99
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDgSEIQDYLQELTG------QRTVPNVFIGGKFIGGCDDLMALH 74


                 ....*
gi 115532750 100 NSGHL 104
Cdd:cd03419   75 KSGKL 79
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 22-104 3.69e-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: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750   22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTlkasQPDDYLGIVNglvyTTRQTSVPQIFVCGRFIGGYTELDALRNS 101
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDG----DPALRDEMMQ----RSGRRTVPQIFIGDVHVGGCDDLYALDRE 72


                  ...
gi 115532750  102 GHL 104
Cdd:TIGR02181  73 GKL 75
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
21-98 3.87e-14

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 62.14  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQpdDYLGIVNGlvyttrQTSVPQIFVCGRFIGGYT--ELDAL 98
Cdd:COG0695    1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAR--EELRERSG------RRTVPVIFIGGEHLGGFDegELDAL 72
Glutaredoxin pfam00462
Glutaredoxin;
22-89 3.59e-13

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 59.44  E-value: 3.59e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115532750   22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQpdDYLGIVNGlvyttrQTSVPQIFVCGRFI 89
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIR--EELKELSG------WPTVPQVFIDGEHI 60
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 18-97 1.34e-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: 58.31  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750   18 KKDPVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDtlkasqpDDYLGIVNGLVytTRQTSVPQIFVCGRFIGGYTELDA 97
Cdd:TIGR02190   6 KPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLG-------NDARGRSLRAV--TGATTVPQVFIGGKLIGGSDELEA 76
PRK10638 PRK10638
glutaredoxin 3; Provisional
 22-104 3.32e-12

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 57.52  E-value: 3.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQPDdylgivngLVYTTRQTSVPQIFVCGRFIGGYTELDALRNS 101
Cdd:PRK10638   4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREE--------MIKRSGRTTVPQIFIDAQHIGGCDDLYALDAR 75


                 ...
gi 115532750 102 GHL 104
Cdd:PRK10638  76 GGL 78
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 20-97 8.08e-10

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: 50.98  E-value: 8.08e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115532750  20 DPVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQPddyLGIVNGlvyttrQTSVPQIFVCGRFIGGYTELDA 97
Cdd:cd03029    1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRS---LRAVTG------AMTVPQVFIDGELIGGSDDLEK 69
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 13-104 1.15e-09

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: 51.30  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750   13 VQEQVKKDPVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQpddylGIVNGLVYTTRQTSVPQIFVCGRFIGGY 92
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGK-----DIENALSRLGCSPAVPAVFVGGKLVGGL 75

                          90
                  ....*....|..
gi 115532750   93 TELDALRNSGHL 104
Cdd:TIGR02189  76 ENVMALHISGSL 87
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 22-100 2.01e-09

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


Pssm-ID: 239325 [Multi-domain]  Cd Length: 73  Bit Score: 50.10  E-value: 2.01e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115532750  22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQPDdylgivngLVYTTRQTSVPQIFVCGRFIGGYTELDALRN 100
Cdd:cd03027    3 VTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPERKAE--------LEERTGSSVVPQIFFNEKLVGGLTDLKSLEE 73
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 21-98 2.12e-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: 45.06  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750   21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQpddylgivNGLVYTTRQTSVPQIFVCGRFIGGYT--ELDAL 98
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAR--------EELLKVYGQRGVPVIVIGHKIVVGFDpeKLDQL 72
grxA PRK11200
glutaredoxin 1; Provisional
 22-98 4.83e-07

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 44.25  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  22 VVMYTKTSCTFCNRAKDLfsdvrvaykevnLDTLKASQPD-DYL-------GI--------VNGLVYTtrqtsVPQIFVC 85
Cdd:PRK11200   3 VVIFGRPGCPYCVRAKEL------------AEKLSEERDDfDYRyvdihaeGIskadlektVGKPVET-----VPQIFVD 65

                         90
                 ....*....|...
gi 115532750  86 GRFIGGYTELDAL 98
Cdd:PRK11200  66 QKHIGGCTDFEAY 78
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 21-98 1.70e-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: 42.60  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  21 PVVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDTLKASQpdDYLGIVNGlvyttrQTSVPQIFVCGRFIGGYT--ELDAL 98
Cdd:cd02976    1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEAL--EELKKLNG------YRSVPVVVIGDEHLSGFRpdKLRAL 72
PHA03050 PHA03050
glutaredoxin; Provisional
 11-100 6.48e-06

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 41.93  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  11 DVVQEQVKKDPVVMYTKTSCTFCNRAKDL---FSDVRVAYKEVNLDTLKA-SQPDDYLGIVNGlvyttrQTSVPQIFVCG 86
Cdd:PHA03050   4 EFVQQRLANNKVTIFVKFTCPFCRNALDIlnkFSFKRGAYEIVDIKEFKPeNELRDYFEQITG------GRTVPRIFFGK 77

                         90
                 ....*....|....
gi 115532750  87 RFIGGYTELDALRN 100
Cdd:PHA03050  78 TSIGGYSDLLEIDN 91
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
 22-97 8.58e-06

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 43.09  E-value: 8.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115532750  22 VVMYTKTSCTFCNRAKDLFSDVRVAYKEVNLDtlKASQPDDYLGIVNG--LVYTTRQTSVPQIFVCGRFIGGYTELDA 97
Cdd:PRK12759   4 VRIYTKTNCPFCDLAKSWFGANDIPFTQISLD--DDVKRAEFYAEVNKniLLVEEHIRTVPQIFVGDVHIGGYDNLMA 79
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 13-104 1.30e-04

Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.


Pssm-ID: 239326  Cd Length: 90  Bit Score: 37.86  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  13 VQEQVKKDPVVMYTKTS-----CTFCNRAKDLFSDVRVAYKEVN-LDtlkasqpDDylGIVNGL-VYTTRQTsVPQIFVC 85
Cdd:cd03028    1 IKKLIKENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDFGTFDiLE-------DE--EVRQGLkEYSNWPT-FPQLYVN 70

                         90
                 ....*....|....*....
gi 115532750  86 GRFIGGYTELDALRNSGHL 104
Cdd:cd03028   71 GELVGGCDIVKEMHESGEL 89
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 22-111 2.04e-04

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: 38.37  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532750  22 VVMYTkTSC-----TF--CNRAKDLFSDVRVAYKE--VNLDTLKASQPDDYLGIVnglvytTRQTSVPQIFVCGRFIGGY 92
Cdd:cd03031    2 VVLYT-TSLrgvrkTFedCNNVRAILESFRVKFDErdVSMDSGFREELRELLGAE------LKAVSLPRVFVDGRYLGGA 74

                         90
                 ....*....|....*....
gi 115532750  93 TELDALRNSGHLFEAIAQC 111
Cdd:cd03031   75 EEVLRLNESGELRKLLKGI 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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