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Conserved domains on  [gi|518335188|ref|WP_019505395|]
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Grx4 family monothiol glutaredoxin [Pleurocapsa sp. PCC 7319]

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];
2-106 2.03e-68

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


:

Pssm-ID: 440047  Cd Length: 105  Bit Score: 199.96  E-value: 2.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   2 NSETKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEF 81
Cdd:COG0278    1 MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEF 80

                         90       100
                 ....*....|....*....|....*
gi 518335188  82 VGGSDIAIELYQSGELQQMVEVALA 106
Cdd:COG0278   81 IGGCDIIREMYESGELQKLLEEAGA 105
 
Name Accession Description Interval E-value
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
2-106 2.03e-68

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 199.96  E-value: 2.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   2 NSETKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEF 81
Cdd:COG0278    1 MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEF 80

                         90       100
                 ....*....|....*....|....*
gi 518335188  82 VGGSDIAIELYQSGELQQMVEVALA 106
Cdd:COG0278   81 IGGCDIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 5-101 1.20e-63

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: 187.67  E-value: 1.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188    5 TKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGG 84
Cdd:TIGR00365   1 TIERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGG 80

                          90
                  ....*....|....*..
gi 518335188   85 SDIAIELYQSGELQQMV 101
Cdd:TIGR00365  81 CDIIMEMYQSGELQTLL 97
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 9-98 2.12e-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: 179.23  E-value: 2.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   9 IDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGSDIA 88
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 518335188  89 IELYQSGELQ 98
Cdd:cd03028   81 KEMHESGELQ 90
PTZ00062 PTZ00062
glutaredoxin; Provisional
 3-101 4.85e-38

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 126.45  E-value: 4.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   3 SETKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFV 82
Cdd:PTZ00062 100 EDTVEKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNGELI 179

                         90
                 ....*....|....*....
gi 518335188  83 GGSDIAIELYQSGELQQMV 101
Cdd:PTZ00062 180 GGHDIIKELYESNSLRKVI 198
Glutaredoxin pfam00462
Glutaredoxin;
18-82 9.03e-28

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 96.03  E-value: 9.03e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518335188   18 IMVFMKgsklmPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFV 82
Cdd:pfam00462   1 VVLYTK-----PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREELKELSGWPTVPQVFIDGEHI 60
 
Name Accession Description Interval E-value
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
2-106 2.03e-68

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


Pssm-ID: 440047  Cd Length: 105  Bit Score: 199.96  E-value: 2.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   2 NSETKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEF 81
Cdd:COG0278    1 MMDVQERIKQQIKSNPVVLFMKGTPQFPQCGFSARAVQILNACGVDFATVNVLEDPEIRQGLKEYSNWPTIPQLYVKGEF 80

                         90       100
                 ....*....|....*....|....*
gi 518335188  82 VGGSDIAIELYQSGELQQMVEVALA 106
Cdd:COG0278   81 IGGCDIIREMYESGELQKLLEEAGA 105
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
 5-101 1.20e-63

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: 187.67  E-value: 1.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188    5 TKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGG 84
Cdd:TIGR00365   1 TIERIKEQIAENPVVLYMKGTPQFPQCGFSARAVQILNACGVPFAYVNVLEDPEIRQGIKEYSNWPTIPQLYVKGEFVGG 80

                          90
                  ....*....|....*..
gi 518335188   85 SDIAIELYQSGELQQMV 101
Cdd:TIGR00365  81 CDIIMEMYQSGELQTLL 97
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
 9-98 2.12e-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: 179.23  E-value: 2.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   9 IDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGSDIA 88
Cdd:cd03028    1 IKKLIKENPVVLFMKGTPEEPRCGFSRKVVQILNQLGVDFGTFDILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCDIV 80

                         90
                 ....*....|
gi 518335188  89 IELYQSGELQ 98
Cdd:cd03028   81 KEMHESGELQ 90
PTZ00062 PTZ00062
glutaredoxin; Provisional
 3-101 4.85e-38

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 126.45  E-value: 4.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   3 SETKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFV 82
Cdd:PTZ00062 100 EDTVEKIERLIRNHKILLFMKGSKTFPFCRFSNAVVNMLNSSGVKYETYNIFEDPDLREELKVYSNWPTYPQLYVNGELI 179

                         90
                 ....*....|....*....
gi 518335188  83 GGSDIAIELYQSGELQQMV 101
Cdd:PTZ00062 180 GGHDIIKELYESNSLRKVI 198
PRK10824 PRK10824
Grx4 family monothiol glutaredoxin;
3-102 5.02e-37

Grx4 family monothiol glutaredoxin;


Pssm-ID: 182759  Cd Length: 115  Bit Score: 121.16  E-value: 5.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   3 SETKAKIDKLVNENKIMVFMKGSKLMPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFV 82
Cdd:PRK10824   2 STTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALSACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELV 81

                         90       100
                 ....*....|....*....|
gi 518335188  83 GGSDIAIELYQSGELQQMVE 102
Cdd:PRK10824  82 GGCDIVIEMYQRGELQQLIK 101
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 17-93 1.89e-32

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: 107.94  E-value: 1.89e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518335188  17 KIMVFMKGSklmpqCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGSDIAIELYQ 93
Cdd:cd02066    1 KVVVFSKST-----CPYCKRAKRLLESLGIEFEEIDILEDGELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
18-82 9.03e-28

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 96.03  E-value: 9.03e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518335188   18 IMVFMKgsklmPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFV 82
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 ...
 17-100 2.22e-16

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: 67.56  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188  17 KIMVFMKGSklmpqCGFSNNVVQILNTLGVPYETV--DILAD-PEIRQGIKEYSNWPTIPQIYINGEFVGGSDIAIELYQ 93
Cdd:cd03419    1 PVVVFSKSY-----CPYCKRAKSLLKELGVKPAVVelDQHEDgSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHK 75


                 ....*..
gi 518335188  94 SGELQQM 100
Cdd:cd03419   76 SGKLVKL 82
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
17-102 7.85e-15

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 63.29  E-value: 7.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188  17 KIMVFMKgsklmPQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGSDiaielyqSGE 96
Cdd:COG0695    1 KVTLYTT-----PGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD-------EGE 68


                 ....*.
gi 518335188  97 LQQMVE 102
Cdd:COG0695   69 LDALLA 74
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 29-100 9.02e-10

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: 50.72  E-value: 9.02e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518335188   29 PQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGSDIAIELYQSGELQQM 100
Cdd:TIGR02181   7 PYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDPL 78
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 29-95 1.90e-09

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: 49.89  E-value: 1.90e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518335188  29 PQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNW-PTIPQIYINGEFVGGSDIAIELYQSG 95
Cdd:cd03418    8 PNCPYCVRAKALLDKKGVDYEEIDVDGDPALREEMINRSGGrRTVPQIFIGDVHIGGCDDLYALERKG 75
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 35-102 2.33e-08

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: 48.39  E-value: 2.33e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518335188  35 NNVVQILNTLGVPYETVDILAD----PEIRQGIKEYSNWPTIPQIYINGEFVGGSDIAIELYQSGELQQMVE 102
Cdd:cd03031   20 NNVRAILESFRVKFDERDVSMDsgfrEELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLK 91
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
 9-106 3.48e-08

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: 47.06  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188    9 IDKLVNENKIMVFMKGSklmpqCGFSNNVVQILNTLGV-P--YETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGS 85
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSS-----CCMCHVVKRLLLTLGVnPavHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGL 75

                          90       100
                  ....*....|....*....|.
gi 518335188   86 DIAIELYQSGELQQMVEVALA 106
Cdd:TIGR02189  76 ENVMALHISGSLVPMLKQAGA 96
PRK10638 PRK10638
glutaredoxin 3; Provisional
 31-102 7.08e-08

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 45.97  E-value: 7.08e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518335188  31 CGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGSDIAIELYQSGELQQMVE 102
Cdd:PRK10638  12 CPFCHRAKALLNSKGVSFQEIPIDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDPLLK 83
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 29-88 1.48e-06

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: 42.37  E-value: 1.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518335188   29 PQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGGSDIA 88
Cdd:TIGR02196   8 PWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAREELLKVYGQRGVPVIVIGHKIVVGFDPE 67
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 29-90 1.61e-05

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: 39.52  E-value: 1.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518335188  29 PQCGFSNNVVQILNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGE-FVGGSDIAIE 90
Cdd:cd02976    8 PDCPYCKATKRFLDERGIPFEEVDVDEDPEALEELKKLNGYRSVPVVVIGDEhLSGFRPDKLR 70
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 18-86 4.08e-05

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: 38.65  E-value: 4.08e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518335188  18 IMVFMKgsklmPQCGFSNNVVQILNTLGVPYETVDILADPEIRQgIKEYSNWPTIPQIYINGEFVGGSD 86
Cdd:cd03029    3 VSLFTK-----PGCPFCARAKAALQENGISYEEIPLGKDITGRS-LRAVTGAMTVPQVFIDGELIGGSD 65
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 41-84 6.93e-05

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: 38.16  E-value: 6.93e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 518335188  41 LNTLGVPYETVDILADPEIRQGIKEYSNWPTIPQIYINGEFVGG 84
Cdd:cd03027   21 LREKGLPYVEINIDIFPERKAELEERTGSSVVPQIFFNEKLVGG 64
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
 18-92 1.89e-04

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: 37.13  E-value: 1.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518335188   18 IMVFMKgsklmPQCGFSNNVVQILNTLGVPYEtvDILADPEIR-QGIKEYSNWPTIPQIYINGEFVGGSDiAIELY 92
Cdd:TIGR02190  10 VVVFTK-----PGCPFCAKAKATLKEKGYDFE--EIPLGNDARgRSLRAVTGATTVPQVFIGGKLIGGSD-ELEAY 77
SH3BGR pfam04908
SH3-binding, glutamic acid-rich protein;
37-86 8.65e-04

SH3-binding, glutamic acid-rich protein;


Pssm-ID: 398530 [Multi-domain]  Cd Length: 92  Bit Score: 35.52  E-value: 8.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 518335188   37 VVQILNTLGVPYETVDILADPEIRQGIKEYSN--WPTIPQIYINGEFVGGSD 86
Cdd:pfam04908  23 VLMILDANKIPFDEVDITKDEEQRRWMRENPPngAPLPPQIFNEDQYCGDYD 74
GRX_SH3BGR cd03030
Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a ...
 37-99 1.38e-03

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.


Pssm-ID: 239328 [Multi-domain]  Cd Length: 92  Bit Score: 34.94  E-value: 1.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518335188  37 VVQILNTLGVPYETVDILADPEIRQ----GIKEYSNWPTIPQIYINGEFVGGSDIAIELYQSGELQQ 99
Cdd:cd03030   22 VLGFLEAKKIEFEEVDISMNEENRQwmreNVPNENGKPLPPQIFNGDEYCGDYEAFFEAKENNTLEE 88
 
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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