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Conserved domains on  [gi|7293857|gb|AAF49222|]
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glutaredoxin 1, isoform A [Drosophila melanogaster]

Protein Classification

GRX_GRXh_1_2_like domain-containing protein (domain architecture ID 10130685)

GRX_GRXh_1_2_like domain-containing protein

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 ...
31-111 6.18e-45

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  Cd Length: 82  Bit Score: 139.98  E-value: 6.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQ 110
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80

                .
gi 7293857  111 K 111
Cdd:cd03419  81 K 81
 
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 ...
31-111 6.18e-45

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  Cd Length: 82  Bit Score: 139.98  E-value: 6.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQ 110
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80

                .
gi 7293857  111 K 111
Cdd:cd03419  81 K 81
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
32-111 3.80e-38

Glutaredoxin; 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 model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016  Cd Length: 83  Bit Score: 123.12  E-value: 3.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857     32 VVIFSKTYCPYCTMAKEPFKKLNVD-ATIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQ 110
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKpYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80

                  .
gi 7293857    111 K 111
Cdd:TIGR02180  81 E 81
Glutaredoxin pfam00462
Glutaredoxin;
32-94 4.26e-23

Glutaredoxin;


Pssm-ID: 334091  Cd Length: 60  Bit Score: 84.08  E-value: 4.26e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7293857     32 VVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPdgnEIQAVLGEITGARTVPRVFIDGKFI 94
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVKFEEIDVDEDP---EIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
31-110 6.97e-20

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223767  Cd Length: 80  Bit Score: 76.58  E-value: 6.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPdGNEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQ 110
Cdd:COG0695   2 NVTIYTKPGCPYCKRAKRLLDRKGVDYEEIDVDDDE-PEEAREMVKRGKGQRTVPQIFIGGKHVGGCDDLDALEAKGKLD 80
PHA03050 PHA03050
glutaredoxin; Provisional
21-109 6.05e-10

glutaredoxin; Provisional


Pssm-ID: 165343  Cd Length: 108  Bit Score: 51.94  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857    21 KFVENTIASNKVVIFSKTYCPYCTMAKEPFKKLNVDA---TIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGGG 97
Cdd:PHA03050   4 EFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRgayEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGGY 83
                         90
                 ....*....|..
gi 7293857    98 TDIKRMFETGAL 109
Cdd:PHA03050  84 SDLLEIDNMDAL 95
 
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 ...
31-111 6.18e-45

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  Cd Length: 82  Bit Score: 139.98  E-value: 6.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQ 110
Cdd:cd03419   1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80

                .
gi 7293857  111 K 111
Cdd:cd03419  81 K 81
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
32-111 3.80e-38

Glutaredoxin; 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 model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.


Pssm-ID: 274016  Cd Length: 83  Bit Score: 123.12  E-value: 3.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857     32 VVIFSKTYCPYCTMAKEPFKKLNVD-ATIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQ 110
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKpYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80

                  .
gi 7293857    111 K 111
Cdd:TIGR02180  81 E 81
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
31-105 1.31e-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  Cd Length: 72  Bit Score: 93.30  E-value: 1.31e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDatIIELDGNPDGnEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFE 105
Cdd:cd02066   1 KVVVFSKSTCPYCKRAKRLLESLGIE--FEEIDILEDG-ELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
Glutaredoxin pfam00462
Glutaredoxin;
32-94 4.26e-23

Glutaredoxin;


Pssm-ID: 334091  Cd Length: 60  Bit Score: 84.08  E-value: 4.26e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7293857     32 VVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPdgnEIQAVLGEITGARTVPRVFIDGKFI 94
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVKFEEIDVDEDP---EIREELKELSGWPTVPQVFIDGEHI 60
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
31-110 6.97e-20

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223767  Cd Length: 80  Bit Score: 76.58  E-value: 6.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPdGNEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQ 110
Cdd:COG0695   2 NVTIYTKPGCPYCKRAKRLLDRKGVDYEEIDVDDDE-PEEAREMVKRGKGQRTVPQIFIGGKHVGGCDDLDALEAKGKLD 80
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
32-111 5.30e-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  Cd Length: 79  Bit Score: 69.21  E-value: 5.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857     32 VVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNEIQAvlgEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQK 111
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDPALRDEMM---QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
23-96 1.97e-16

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  Cd Length: 99  Bit Score: 68.25  E-value: 1.97e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7293857     23 VENTIASNKVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGG 96
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGG 74
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
31-107 5.05e-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  Cd Length: 75  Bit Score: 66.46  E-value: 5.05e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDG-NEIQAVLGeitGARTVPRVFIDGKFIGGGTDIKRMFETG 107
Cdd:cd03418   1 KVEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPALrEEMINRSG---GRRTVPQIFIGDVHIGGCDDLYALERKG 75
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
32-104 1.30e-14

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  Cd Length: 72  Bit Score: 62.92  E-value: 1.30e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7293857   32 VVIFSKTYCPYCTMAKEPFKKLNVDATIIELdgnpdGNEIQA-VLGEITGARTVPRVFIDGKFIGGGTDIKRMF 104
Cdd:cd03029   3 VSLFTKPGCPFCARAKAALQENGISYEEIPL-----GKDITGrSLRAVTGAMTVPQVFIDGELIGGSDDLEKYF 71
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
32-104 2.29e-13

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: 60.24  E-value: 2.29e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7293857     32 VVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGneiqAVLGEITGARTVPRVFIDGKFIGGGTDIKRMF 104
Cdd:TIGR02190  10 VVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARG----RSLRAVTGATTVPQVFIGGKLIGGSDELEAYL 78
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
31-103 1.66e-12

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  Cd Length: 73  Bit Score: 57.81  E-value: 1.66e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPdgnEIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRM 103
Cdd:cd03027   2 RVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFP---ERKAELEERTGSSVVPQIFFNEKLVGGLTDLKSL 71
PHA03050 PHA03050
glutaredoxin; Provisional
21-109 6.05e-10

glutaredoxin; Provisional


Pssm-ID: 165343  Cd Length: 108  Bit Score: 51.94  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857    21 KFVENTIASNKVVIFSKTYCPYCTMAKEPFKKLNVDA---TIIELDGNPDGNEIQAVLGEITGARTVPRVFIDGKFIGGG 97
Cdd:PHA03050   4 EFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRgayEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGGY 83
                         90
                 ....*....|..
gi 7293857    98 TDIKRMFETGAL 109
Cdd:PHA03050  84 SDLLEIDNMDAL 95
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
31-101 2.64e-09

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  Cd Length: 73  Bit Score: 49.53  E-value: 2.64e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7293857   31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPdgnEIQAVLGEITGARTVPRVFIDGKFIGGGTDIK 101
Cdd:cd02976   1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDP---EALEELKKLNGYRSVPVVVIGDEHLSGFRPDK 68
PRK10638 PRK10638
glutaredoxin 3; Provisional
31-109 3.04e-09

glutaredoxin 3; Provisional


Pssm-ID: 182607  Cd Length: 83  Bit Score: 49.43  E-value: 3.04e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7293857    31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNEiqaVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGAL 109
Cdd:PRK10638   3 NVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKRE---EMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGL 78
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
70-111 3.76e-09

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  Cd Length: 147  Bit Score: 50.70  E-value: 3.76e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 7293857   70 EIQAVLGEITGARTVPRVFIDGKFIGGGTDIKRMFETGALQK 111
Cdd:cd03031  47 ELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRK 88
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
31-96 2.30e-08

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  Cd Length: 74  Bit Score: 46.99  E-value: 2.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7293857     31 KVVIFSKTYCPYCTMAKEPFKKLNVDatIIELDGNPDGNEIQAVLgEITGARTVPRVFIDGKFIGG 96
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKGVA--FEEIDVEKDAAAREELL-KVYGQRGVPVIVIGHKIVVG 63
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
21-114 6.82e-08

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


Pssm-ID: 223355  Cd Length: 105  Bit Score: 46.51  E-value: 6.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857   21 KFVENTIASNKVVIFSK-----TYCPYCTMAKEPFKKLNVD--ATIIELDgNPdgnEIQAVLGEITGARTVPRVFIDGKF 93
Cdd:COG0278   6 DRIQKQIKENPVVLFMKgtpefPQCGFSAQAVQILSACGVVdfAYVDVLQ-DP---EIRQGLKEYSNWPTFPQLYVNGEF 81
                        90       100
                ....*....|....*....|.
gi 7293857   94 IGGGTDIKRMFETGALQKYFQ 114
Cdd:COG0278  82 VGGCDIVREMYQSGELQTLLK 102
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
23-110 1.36e-06

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: 42.87  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857   23 VENTIASNKVVIFSK-----TYCPYCTMAKEPFKKLNVDATIIELDGNPdgnEIQAVLGEITGARTVPRVFIDGKFIGGG 97
Cdd:cd03028   1 IKKLIKENPVVLFMKgtpeePRCGFSRKVVQILNQLGVDFGTFDILEDE---EVRQGLKEYSNWPTFPQLYVNGELVGGC 77
                        90
                ....*....|...
gi 7293857   98 TDIKRMFETGALQ 110
Cdd:cd03028  78 DIVKEMHESGELQ 90
TIGR00365 TIGR00365
monothiol glutaredoxin, Grx4 family; The gene for the member of this glutaredoxin family in E. ...
21-113 1.89e-06

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: 42.45  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857     21 KFVENTIASNKVVIFSK--TYCPYC----------TMAKEPFKKLNVdatiieLDgNPdgnEIQAVLGEITGARTVPRVF 88
Cdd:TIGR00365   3 ERIKEQIAENPVVLYMKgtPQFPQCgfsaravqilNACGVPFAYVNV------LE-DP---EIRQGIKEYSNWPTIPQLY 72
                          90       100
                  ....*....|....*....|....*
gi 7293857     89 IDGKFIGGGTDIKRMFETGALQKYF 113
Cdd:TIGR00365  73 VKGEFVGGCDIIMEMYQSGELQTLL 97
grxA PRK11200
glutaredoxin 1; Provisional
31-99 3.36e-06

glutaredoxin 1; Provisional


Pssm-ID: 183036  Cd Length: 85  Bit Score: 41.56  E-value: 3.36e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7293857    31 KVVIFSKTYCPYCTMAKEPFKKLNvdatiIELDgNPDGNEIQAVLGEITGA----------RTVPRVFIDGKFIGGGTD 99
Cdd:PRK11200   2 FVVIFGRPGCPYCVRAKELAEKLS-----EERD-DFDYRYVDIHAEGISKAdlektvgkpvETVPQIFVDQKHIGGCTD 74
GlrX_actino TIGR02200
Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the ...
31-93 2.03e-04

Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the Actinobacteria and contains the conserved CxxC motif.


Pssm-ID: 131255  Cd Length: 77  Bit Score: 36.75  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7293857     31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNE-IQAVLGeitGARTVPRV-FIDGKF 93
Cdd:TIGR02200   1 TITVYGTTWCGYCAQLMRTLDKLGAAYEWVDIEEDEGAADrVVSVNN---GNMTVPTVkFADGSF 62
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
32-99 2.22e-04

Glutaredoxin, GrxA 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 model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.


Pssm-ID: 131238  Cd Length: 86  Bit Score: 37.11  E-value: 2.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7293857     32 VVIFSKTYCPYCTMAKEPFKKLNVDATIIE---LDGNPDGNEiQAVLGEITG--ARTVPRVFIDGKFIGGGTD 99
Cdd:TIGR02183   2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEfryIDIHAEGIS-KADLEKTVGkpVETVPQIFVDEKHVGGCTD 73
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
31-96 2.33e-04

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 38.85  E-value: 2.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7293857    31 KVVIFSKTYCPYCTMAKEPFKKLNVDATIIELDGNPDGNEIQA-----VLGEITGARTVPRVFIDGKFIGG 96
Cdd:PRK12759   3 EVRIYTKTNCPFCDLAKSWFGANDIPFTQISLDDDVKRAEFYAevnknILLVEEHIRTVPQIFVGDVHIGG 73
PTZ00062 PTZ00062
glutaredoxin; Provisional
16-113 4.59e-04

glutaredoxin; Provisional


Pssm-ID: 240250 [Multi-domain]  Cd Length: 204  Bit Score: 37.47  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857    16 STKQAKFVENTIASNKVVIF---SKTYcPYCTMAKEPFKKLNvdATIIELDGNP--DGNEIQAVLGEITGARTVPRVFID 90
Cdd:PTZ00062  99 SEDTVEKIERLIRNHKILLFmkgSKTF-PFCRFSNAVVNMLN--SSGVKYETYNifEDPDLREELKVYSNWPTYPQLYVN 175
                         90       100
                 ....*....|....*....|...
gi 7293857    91 GKFIGGGTDIKRMFETGALQKYF 113
Cdd:PTZ00062 176 GELIGGHDIIKELYESNSLRKVI 198
PRK10824 PRK10824
glutaredoxin-4; Provisional
15-111 4.83e-04

glutaredoxin-4; Provisional


Pssm-ID: 182759  Cd Length: 115  Bit Score: 36.80  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7293857    15 MSTKQAKfVENTIASNKVVIFSK--TYCPYCTMAKEPFKKLNVDA---TIIELDGNPDgneIQAVLGEITGARTVPRVFI 89
Cdd:PRK10824   1 MSTTIEK-IQRQIAENPILLYMKgsPKLPSCGFSAQAVQALSACGerfAYVDILQNPD---IRAELPKYANWPTFPQLWV 76
                         90       100
                 ....*....|....*....|..
gi 7293857    90 DGKFIGGGTDIKRMFETGALQK 111
Cdd:PRK10824  77 DGELVGGCDIVIEMYQRGELQQ 98
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
31-97 4.60e-03

Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.


Pssm-ID: 239271 [Multi-domain]  Cd Length: 67  Bit Score: 32.93  E-value: 4.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7293857   31 KVVIFSKTYCPYCTMAKEP---FKKLN--VDATIIELDGNPDgneiqavLGEITGARTVPRVFIDGKFIGGG 97
Cdd:cd02973   2 NIEVFVSPTCPYCPDAVQAanrIAALNpnISAEMIDAAEFPD-------LADEYGVMSVPAIVINGKVEFVG 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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