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Conserved domains on  [gi|25147337|ref|NP_510815|]
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putative monothiol glutaredoxin F10D7.3 [Caenorhabditis elegans]

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 ...
 45-127 2.43e-34

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: 114.94  E-value: 2.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdMKIVELDRSNQTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEEKGEL 124
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVK-PAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKL 79


                ...
gi 25147337 125 RPL 127
Cdd:cd03419  80 VKL 82
 
Name Accession Description Interval E-value
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 45-127 2.43e-34

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: 114.94  E-value: 2.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdMKIVELDRSNQTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEEKGEL 124
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVK-PAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKL 79


                ...
gi 25147337 125 RPL 127
Cdd:cd03419  80 VKL 82
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 46-128 2.05e-17

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: 71.52  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337    46 VMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSNQTEEMQEILKKySGRTTVPQLFISGKFVGGHDETKAIEEKGELR 125
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVT---FTEIRVDGDPALRDEMMQR-SGRRTVPQIFIGDVHVGGCDDLYALDREGKLD 76


                  ...
gi 25147337   126 PLL 128
Cdd:TIGR02181  77 PLL 79
Glutaredoxin pfam00462
Glutaredoxin;
46-109 2.87e-17

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 70.61  E-value: 2.87e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25147337    46 VMVYSKTYCPWSKRLKAILANYEIDdMKIVELDRSnqtEEMQEILKKYSGRTTVPQLFISGKFV 109
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVD-FEEIDVDED---PEIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
45-129 4.30e-15

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 65.60  E-value: 4.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSNQTEEMQEiLKKYSGRTTVPQLFISGKFVGGHDEtkaieekGEL 124
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIP---YEEIDVDEDPEAREE-LRERSGRRTVPVIFIGGEHLGGFDE-------GEL 69


                ....*
gi 25147337 125 RPLLE 129
Cdd:COG0695  70 DALLA 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 45-129 6.41e-15

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 65.23  E-value: 6.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337   45 KVMVYSKTYCPWSKRLKAILANyeiDDMKIVELDRSNQTEEMQEILKKySGRTTVPQLFISGKFVGGHDETKAIEEKGEL 124
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNS---KGVSFQEIPIDGDAAKREEMIKR-SGRTTVPQIFIDAQHIGGCDDLYALDARGGL 78


                 ....*
gi 25147337  125 RPLLE 129
Cdd:PRK10638  79 DPLLK 83
 
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 ...
 45-127 2.43e-34

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: 114.94  E-value: 2.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdMKIVELDRSNQTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEEKGEL 124
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVK-PAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKL 79


                ...
gi 25147337 125 RPL 127
Cdd:cd03419  80 VKL 82
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 45-120 9.17e-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: 90.22  E-value: 9.17e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSnQTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEE 120
Cdd:cd02066   1 KVVVFSKSTCPYCKRAKRLLESLGIE---FEEIDIL-EDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 46-128 2.05e-17

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: 71.52  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337    46 VMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSNQTEEMQEILKKySGRTTVPQLFISGKFVGGHDETKAIEEKGELR 125
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVT---FTEIRVDGDPALRDEMMQR-SGRRTVPQIFIGDVHVGGCDDLYALDREGKLD 76


                  ...
gi 25147337   126 PLL 128
Cdd:TIGR02181  77 PLL 79
Glutaredoxin pfam00462
Glutaredoxin;
46-109 2.87e-17

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 70.61  E-value: 2.87e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25147337    46 VMVYSKTYCPWSKRLKAILANYEIDdMKIVELDRSnqtEEMQEILKKYSGRTTVPQLFISGKFV 109
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVD-FEEIDVDED---PEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 45-122 1.18e-16

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: 69.54  E-value: 1.18e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSNQTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEEKG 122
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLDKKGVD---YEEIDVDGDPALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYALERKG 75
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
45-129 4.30e-15

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 65.60  E-value: 4.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSNQTEEMQEiLKKYSGRTTVPQLFISGKFVGGHDEtkaieekGEL 124
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIP---YEEIDVDEDPEAREE-LRERSGRRTVPVIFIGGEHLGGFDE-------GEL 69


                ....*
gi 25147337 125 RPLLE 129
Cdd:COG0695  70 DALLA 74
PRK10638 PRK10638
glutaredoxin 3; Provisional
 45-129 6.41e-15

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 65.23  E-value: 6.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337   45 KVMVYSKTYCPWSKRLKAILANyeiDDMKIVELDRSNQTEEMQEILKKySGRTTVPQLFISGKFVGGHDETKAIEEKGEL 124
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNS---KGVSFQEIPIDGDAAKREEMIKR-SGRTTVPQIFIDAQHIGGCDDLYALDARGGL 78


                 ....*
gi 25147337  125 RPLLE 129
Cdd:PRK10638  79 DPLLK 83
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
32-131 2.82e-14

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 64.37  E-value: 2.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  32 DLEDKIVNDVMTHKVMVYSK-T----YCPWSKR----LKAILANYE----IDDMKIveldRSNqteemqeiLKKYSGRTT 98
Cdd:COG0278   3 DVQERIKQQIKSNPVVLFMKgTpqfpQCGFSARavqiLNACGVDFAtvnvLEDPEI----RQG--------LKEYSNWPT 70

                        90       100       110
                ....*....|....*....|....*....|...
gi 25147337  99 VPQLFISGKFVGGHDETKAIEEKGELRPLLEKA 131
Cdd:COG0278  71 IPQLYVKGEFIGGCDIIREMYESGELQKLLEEA 103
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 37-125 1.86e-13

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: 61.74  E-value: 1.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  37 IVNDVMTHKVMVYSK-----TYCPWSKRLKAILANYEID----DmkiVELDrsnqtEEMQEILKKYSGRTTVPQLFISGK 107
Cdd:cd03028   1 IKKLIKENPVVLFMKgtpeePRCGFSRKVVQILNQLGVDfgtfD---ILED-----EEVRQGLKEYSNWPTFPQLYVNGE 72

                        90
                ....*....|....*...
gi 25147337 108 FVGGHDETKAIEEKGELR 125
Cdd:cd03028  73 LVGGCDIVKEMHESGELQ 90
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 45-131 2.24e-11

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: 57.63  E-value: 2.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337  45 KVMVYS-------KTY--CpwsKRLKAILANYEID-DMKIVELDRSNQtEEMQEILKKYSGRTTVPQLFISGKFVGGHDE 114
Cdd:cd03031   1 RVVLYTtslrgvrKTFedC---NNVRAILESFRVKfDERDVSMDSGFR-EELRELLGAELKAVSLPRVFVDGRYLGGAEE 76

                        90
                ....*....|....*..
gi 25147337 115 TKAIEEKGELRPLLEKA 131
Cdd:cd03031  77 VLRLNESGELRKLLKGI 93
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 41-134 6.57e-11

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: 55.54  E-value: 6.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337    41 VMTHKVMVYSKTYCPWSKRLKAILANYEIDDMkIVELDRSNQTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEE 120
Cdd:TIGR02189   5 VSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPA-VHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHI 83

                          90
                  ....*....|....
gi 25147337   121 KGELRPLLEKAHAL 134
Cdd:TIGR02189  84 SGSLVPMLKQAGAL 97
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 46-114 1.77e-09

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: 1.77e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25147337  46 VMVYSKTYCPWSKRLKAILANYEIDDMKIVeLDRSNQTEEMQEIlkkySGRTTVPQLFISGKFVGGHDE 114
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALQENGISYEEIP-LGKDITGRSLRAV----TGAMTVPQVFIDGELIGGSDD 66
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 45-116 2.21e-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: 2.21e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147337    45 KVMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSNQTEEMQEILKKYSGRtTVPQLFISGKFVGGHDETK 116
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVA---FEEIDVEKDAAAREELLKVYGQR-GVPVIVIGHKIVVGFDPEK 68
PTZ00062 PTZ00062
glutaredoxin; Provisional
 35-125 2.69e-07

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 47.87  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337   35 DKIVNDVMTHKVMVY---SKTYcPWSKRLKAILanYEIDDMKiVELDRSN--QTEEMQEILKKYSGRTTVPQLFISGKFV 109
Cdd:PTZ00062 104 EKIERLIRNHKILLFmkgSKTF-PFCRFSNAVV--NMLNSSG-VKYETYNifEDPDLREELKVYSNWPTYPQLYVNGELI 179

                         90
                 ....*....|....*.
gi 25147337  110 GGHDETKAIEEKGELR 125
Cdd:PTZ00062 180 GGHDIIKELYESNSLR 195
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
82-131 1.17e-04

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 39.12  E-value: 1.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 25147337   82 QTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEEKGELRPLLEKA 131
Cdd:PRK10824  54 QNPDIRAELPKYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLIKET 103
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 45-120 1.94e-04

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: 37.78  E-value: 1.94e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEIDdmkIVELDRSNQTEEMQEiLKKYSGRTTVPQLFISGKFVGGHDETKAIEE 120
Cdd:cd03027   2 RVTIYSRLGCEDCTAVRLFLREKGLP---YVEINIDIFPERKAE-LEERTGSSVVPQIFFNEKLVGGLTDLKSLEE 73
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 45-115 5.31e-04

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 36.43  E-value: 5.31e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25147337  45 KVMVYSKTYCPWSKRLKAILANYEID-DMKIVELDrsnqtEEMQEILKKYSGRTTVPQLFISGK-FVGGHDET 115
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDERGIPfEEVDVDED-----PEALEELKKLNGYRSVPVVVIGDEhLSGFRPDK 68
PHA03050 PHA03050
glutaredoxin; Provisional
 34-136 3.61e-03

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 34.99  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147337   34 EDKIVNDVMTHKVMVYSKTYCPWSKRLKAILANYEIDD--MKIVELDRSNQTEEMQEILKKYSGRTTVPQLFISGKFVGG 111
Cdd:PHA03050   3 EEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRgaYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGG 82

                         90       100
                 ....*....|....*....|....*
gi 25147337  112 HDETKAIEEKGELRPLLEKAHALFT 136
Cdd:PHA03050  83 YSDLLEIDNMDALGDILSSIGVLRT 107
 
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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