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Conserved domains on  [gi|28839301|gb|AAH47680|]
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Glutaredoxin 5 [Homo sapiens]

Protein Classification

monothiol glutaredoxin family protein( domain architecture ID 10122517)

monothiol glutaredoxin (GRX) family protein belonging to the thioredoxin superfamily, may be redox inactive, similar to monothiol glutaredoxin-5 that is iinvolved in mitochondrial iron-sulfur (Fe/S) cluster transfer

CATH:  3.40.30.10
Gene Ontology:  GO:0106034|GO:0051537
PubMed:  12074972|10049365|15558583|14713336
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 45-135 7.77e-60

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: 180.00  E-value: 7.77e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301  45 LDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDI 124
Cdd:cd03028   1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGV-DFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDI 79

                        90
                ....*....|.
gi 28839301 125 LLQMHQNGDLV 135
Cdd:cd03028  80 VKEMHESGELQ 90
 
Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 45-135 7.77e-60

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: 180.00  E-value: 7.77e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301  45 LDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDI 124
Cdd:cd03028   1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGV-DFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDI 79

                        90
                ....*....|.
gi 28839301 125 LLQMHQNGDLV 135
Cdd:cd03028  80 VKEMHESGELQ 90
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
43-143 5.22e-58

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 176.07  E-value: 5.22e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301  43 EQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGC 122
Cdd:COG0278   6 ERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGV-DFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFIGGC 84

                        90       100
                ....*....|....*....|.
gi 28839301 123 DILLQMHQNGDLVEELKKLGI 143
Cdd:COG0278  85 DIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 43-141 4.23e-54

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 165.72  E-value: 4.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301    43 EQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGC 122
Cdd:TIGR00365   3 ERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGV-PFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGC 81

                          90
                  ....*....|....*....
gi 28839301   123 DILLQMHQNGdlveELKKL 141
Cdd:TIGR00365  82 DIIMEMYQSG----ELQTL 96
PTZ00062 PTZ00062
glutaredoxin; Provisional
 43-138 1.60e-31

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 111.81  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301   43 EQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVRdYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGC 122
Cdd:PTZ00062 104 EKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVK-YETYNIFEDPDLREELKVYSNWPTYPQLYVNGELIGGH 182

                         90
                 ....*....|....*.
gi 28839301  123 DILLQMHQNGDLVEEL 138
Cdd:PTZ00062 183 DIIKELYESNSLRKVI 198
Glutaredoxin pfam00462
Glutaredoxin;
54-119 1.25e-22

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 84.86  E-value: 1.25e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28839301    54 VVVFLKgtpeqPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFV 119
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGV-DFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 45-135 7.77e-60

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: 180.00  E-value: 7.77e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301  45 LDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDI 124
Cdd:cd03028   1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGV-DFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDI 79

                        90
                ....*....|.
gi 28839301 125 LLQMHQNGDLV 135
Cdd:cd03028  80 VKEMHESGELQ 90
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
43-143 5.22e-58

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 176.07  E-value: 5.22e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301  43 EQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGC 122
Cdd:COG0278   6 ERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGV-DFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFIGGC 84

                        90       100
                ....*....|....*....|.
gi 28839301 123 DILLQMHQNGDLVEELKKLGI 143
Cdd:COG0278  85 DIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 43-141 4.23e-54

monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. coli, originally designated ydhD, is now designated grxD. Its protein, Grx4, is a monothiol glutaredoxin similar to Grx5 of yeast, which is involved in iron-sulfur cluster formation. [Energy metabolism, Electron transport]


Pssm-ID: 188046  Cd Length: 97  Bit Score: 165.72  E-value: 4.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301    43 EQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGC 122
Cdd:TIGR00365   3 ERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGV-PFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGGC 81

                          90
                  ....*....|....*....
gi 28839301   123 DILLQMHQNGdlveELKKL 141
Cdd:TIGR00365  82 DIIMEMYQSG----ELQTL 96
PTZ00062 PTZ00062
glutaredoxin; Provisional
 43-138 1.60e-31

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 111.81  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301   43 EQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVRdYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGC 122
Cdd:PTZ00062 104 EKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVK-YETYNIFEDPDLREELKVYSNWPTYPQLYVNGELIGGH 182

                         90
                 ....*....|....*.
gi 28839301  123 DILLQMHQNGDLVEEL 138
Cdd:PTZ00062 183 DIIKELYESNSLRKVI 198
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 53-130 8.04e-29

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: 101.00  E-value: 8.04e-29
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28839301  53 KVVVFLKGTpeqpqCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQ 130
Cdd:cd02066   1 KVVVFSKST-----CPYCKRAKRLLESLGI-EFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
43-140 4.47e-28

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 100.36  E-value: 4.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301   43 EQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVRdYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGC 122
Cdd:PRK10824   6 EKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGER-FAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGGC 84

                         90
                 ....*....|....*...
gi 28839301  123 DILLQMHQNGDLVEELKK 140
Cdd:PRK10824  85 DIVIEMYQRGELQQLIKE 102
Glutaredoxin pfam00462
Glutaredoxin;
54-119 1.25e-22

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 84.86  E-value: 1.25e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28839301    54 VVVFLKgtpeqPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFV 119
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGV-DFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 53-136 7.35e-13

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: 60.25  E-value: 7.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301  53 KVVVFLKGTpeqpqCGFSNAVVQILRlhgvRDYAAYNVL------DDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILL 126
Cdd:cd03419   1 PVVVFSKSY-----CPYCKRAKSLLK----ELGVKPAVVeldqheDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLM 71

                        90
                ....*....|
gi 28839301 127 QMHQNGDLVE 136
Cdd:cd03419  72 ALHKSGKLVK 81
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
53-123 2.66e-09

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 50.97  E-value: 2.66e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28839301  53 KVVVFLKgtpeqPQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCD 123
Cdd:COG0695   1 KVTLYTT-----PGCPYCARAKRLLDEKGI-PYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD 65
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 65-134 4.35e-08

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: 47.64  E-value: 4.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301    65 PQCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQNGDL 134
Cdd:TIGR02181   7 PYCPYCTRAKALLSSKGV-TFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKL 75
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 71-142 5.34e-07

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: 46.46  E-value: 5.34e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28839301  71 NAVVQILRLHGV----RDYAAYNVLDDpELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQNGDLVEELKKLG 142
Cdd:cd03031  20 NNVRAILESFRVkfdeRDVSMDSGFRE-ELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGIR 94
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 48-142 5.40e-07

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: 45.52  E-value: 5.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301    48 LVKKDKVVVFLKGTpeqpqCGFSNAVVQILRLHGVRDyAAYNVLDDPELRQGIKDYSNW---PTIPQVYLNGEFVGGCDI 124
Cdd:TIGR02189   4 MVSEKAVVIFSRSS-----CCMCHVVKRLLLTLGVNP-AVHEIDKEPAGKDIENALSRLgcsPAVPAVFVGGKLVGGLEN 77

                          90
                  ....*....|....*...
gi 28839301   125 LLQMHQNGDLVEELKKLG 142
Cdd:TIGR02189  78 VMALHISGSLVPMLKQAG 95
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 53-132 1.00e-06

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: 44.12  E-value: 1.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839301  53 KVVVFLKGTpeqpqCGFSNAVVQILRLHGVrDYAAYNVLDDPELRQGIKDYSNW-PTIPQVYLNGEFVGGCDILLQMHQN 131
Cdd:cd03418   1 KVEIYTKPN-----CPYCVRAKALLDKKGV-DYEEIDVDGDPALREEMINRSGGrRTVPQIFIGDVHIGGCDDLYALERK 74


                .
gi 28839301 132 G 132
Cdd:cd03418  75 G 75
PRK10638 PRK10638
glutaredoxin 3; Provisional
 93-139 6.24e-04

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 36.72  E-value: 6.24e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 28839301   93 DPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQNGDLVEELK 139
Cdd:PRK10638  37 DAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDPLLK 83
 
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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