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Conserved domains on  [gi|480339789|gb|ENX59980|]
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Grx4 family monothiol glutaredoxin [Acinetobacter higginsii]

Protein Classification

glutaredoxin family protein( domain architecture ID 10000959)

glutaredoxin (GRX) family protein belonging to the thioredoxin superfamily, may function as a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  12074972|9099998|10049365|15558583|14713336|14962389|17415523
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
7-106 7.01e-67

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


:

Pssm-ID: 440047  Cd Length: 105  Bit Score: 196.49  E-value: 7.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789   7 DTVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIG 86
Cdd:COG0278    3 DVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFIG 82

                         90       100
                 ....*....|....*....|
gi 480339789  87 GSDIMLEMFQNGELKPLVEQ 106
Cdd:COG0278   83 GCDIIREMYESGELQKLLEE 102
 
Name Accession Description Interval E-value
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
7-106 7.01e-67

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 196.49  E-value: 7.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789   7 DTVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIG 86
Cdd:COG0278    3 DVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFIG 82

                         90       100
                 ....*....|....*....|
gi 480339789  87 GSDIMLEMFQNGELKPLVEQ 106
Cdd:COG0278   83 GCDIIREMYESGELQKLLEE 102
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 8-104 3.15e-64

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: 189.60  E-value: 3.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789    8 TVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGG 87
Cdd:TIGR00365   1 TIERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGG 80

                          90
                  ....*....|....*..
gi 480339789   88 SDIMLEMFQNGELKPLV 104
Cdd:TIGR00365  81 CDIIMEMYQSGELQTLL 97
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 12-101 6.88e-54

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: 163.05  E-value: 6.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789  12 IRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGGSDIM 91
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 480339789  92 LEMFQNGELK 101
Cdd:cd03028   81 KEMHESGELQ 90
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
8-106 4.93e-50

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 154.29  E-value: 4.93e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789   8 TVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGG 87
Cdd:PRK10824   4 TIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGG 83

                         90
                 ....*....|....*....
gi 480339789  88 SDIMLEMFQNGELKPLVEQ 106
Cdd:PRK10824  84 CDIVIEMYQRGELQQLIKE 102
Glutaredoxin pfam00462
Glutaredoxin;
21-85 1.34e-22

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 82.94  E-value: 1.34e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480339789   21 VLLYMKgtpqfPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELI 85
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
7-106 7.01e-67

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 196.49  E-value: 7.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789   7 DTVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIG 86
Cdd:COG0278    3 DVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEFIG 82

                         90       100
                 ....*....|....*....|
gi 480339789  87 GSDIMLEMFQNGELKPLVEQ 106
Cdd:COG0278   83 GCDIIREMYESGELQKLLEE 102
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 8-104 3.15e-64

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: 189.60  E-value: 3.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789    8 TVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGG 87
Cdd:TIGR00365   1 TIERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGG 80

                          90
                  ....*....|....*..
gi 480339789   88 SDIMLEMFQNGELKPLV 104
Cdd:TIGR00365  81 CDIIMEMYQSGELQTLL 97
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 12-101 6.88e-54

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: 163.05  E-value: 6.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789  12 IRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGGSDIM 91
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 480339789  92 LEMFQNGELK 101
Cdd:cd03028   81 KEMHESGELQ 90
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
8-106 4.93e-50

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 154.29  E-value: 4.93e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789   8 TVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGG 87
Cdd:PRK10824   4 TIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGG 83

                         90
                 ....*....|....*....
gi 480339789  88 SDIMLEMFQNGELKPLVEQ 106
Cdd:PRK10824  84 CDIVIEMYQRGELQQLIKE 102
PTZ00062 PTZ00062
glutaredoxin; Provisional
 8-101 1.16e-31

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 110.66  E-value: 1.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789   8 TVALIRDQIAKHPVLLYMKGTPQFPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGG 87
Cdd:PTZ00062 102 TVEKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNGELIGG 181

                         90
                 ....*....|....
gi 480339789  88 SDIMLEMFQNGELK 101
Cdd:PTZ00062 182 HDIIKELYESNSLR 195
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 20-96 4.47e-26

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: 92.14  E-value: 4.47e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480339789  20 PVLLYMKGTpqfpqCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGGSDIMLEMFQ 96
Cdd:cd02066    1 KVVVFSKST-----CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
21-85 1.34e-22

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 82.94  E-value: 1.34e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480339789   21 VLLYMKgtpqfPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELI 85
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
 20-103 1.13e-12

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: 58.32  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789  20 PVLLYMKGTpqfpqCGFSARAVEALSQIGRPFAYVNILEN---QDIRATLPQIANWPTFPQLWINGELIGGSDIMLEMFQ 96
Cdd:cd03419    1 PVVVFSKSY-----CPYCKRAKSLLKELGVKPAVVELDQHedgSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHK 75


                 ....*..
gi 480339789  97 NGELKPL 103
Cdd:cd03419   76 SGKLVKL 82
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
20-105 4.40e-12

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 56.74  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789  20 PVLLYMKgtpqfPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGGsdimlemFQNGE 99
Cdd:COG0695    1 KVTLYTT-----PGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGG-------FDEGE 68


                 ....*.
gi 480339789 100 LKPLVE 105
Cdd:COG0695   69 LDALLA 74
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 32-89 2.62e-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: 49.44  E-value: 2.62e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 480339789  32 PQCGFSARAVEALSQIGrpFAYVNILENQDIRAT-LPQIANWPTFPQLWINGELIGGSD 89
Cdd:cd03029    9 PGCPFCARAKAALQENG--ISYEEIPLGKDITGRsLRAVTGAMTVPQVFIDGELIGGSD 65
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 32-89 3.65e-08

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: 46.76  E-value: 3.65e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 480339789   32 PQCGFSARAVEALSQIGrpFAYVNILENQDIRA-TLPQIANWPTFPQLWINGELIGGSD 89
Cdd:TIGR02190  16 PGCPFCAKAKATLKEKG--YDFEEIPLGNDARGrSLRAVTGATTVPQVFIGGKLIGGSD 72
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 21-103 6.21e-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: 46.10  E-value: 6.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789   21 VLLYMKgtpqfPQCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGGSDIMLEMFQNGEL 100
Cdd:TIGR02181   1 VTIYTK-----PYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKL 75


                  ...
gi 480339789  101 KPL 103
Cdd:TIGR02181  76 DPL 78
PRK10638 PRK10638
glutaredoxin 3; Provisional
 21-105 8.71e-07

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 43.27  E-value: 8.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789  21 VLLYMKGTpqfpqCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIANWPTFPQLWINGELIGGSDIMLEMFQNGEL 100
Cdd:PRK10638   4 VEIYTKAT-----CPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGL 78


                 ....*
gi 480339789 101 KPLVE 105
Cdd:PRK10638  79 DPLLK 83
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 20-98 1.23e-04

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: 37.57  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339789  20 PVLLYMKGTpqfpqCGFSARAVEALSQIGRPFAYVNILENQDIRATLPQIAN-WPTFPQLWINGELIGGSDIMLEMFQNG 98
Cdd:cd03418    1 KVEIYTKPN-----CPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGgRRTVPQIFIGDVHIGGCDDLYALERKG 75
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 73-111 2.18e-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: 37.99  E-value: 2.18e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 480339789  73 PTFPQLWINGELIGGSDIMLEMFQNGELKPLVEQYSPAP 111
Cdd:cd03031   59 VSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGIRARA 97
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 58-106 1.21e-03

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: 35.51  E-value: 1.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 480339789   58 ENQDIRATLPQIANWPTFPQLWINGELIGGSDIMLEMFQNGELKPLVEQ 106
Cdd:TIGR02189  45 AGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHISGSLVPMLKQ 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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