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Conserved domains on  [gi|148223615|ref|NP_001083654|]
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glutaredoxin [Xenopus laevis]

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List of domain hits

Name Accession Description Interval E-value
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
15-99 7.73e-37

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: 121.58  E-value: 7.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   15 VTMFEKSSCPFCVRAKGILTKYKFKEghLEIIDISKLDFMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKP--YEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78

                  ....*
gi 148223615   95 LEKAL 99
Cdd:TIGR02180  79 LAELL 83
 
Name Accession Description Interval E-value
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
15-99 7.73e-37

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: 121.58  E-value: 7.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   15 VTMFEKSSCPFCVRAKGILTKYKFKEghLEIIDISKLDFMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKP--YEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78

                  ....*
gi 148223615   95 LEKAL 99
Cdd:TIGR02180  79 LAELL 83
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
14-97 1.45e-30

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: 105.31  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  14 KVTMFEKSSCPFCVRAKGILTKYKFKEGHLEIIDISKldfMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENSG 93
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHED---GSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77

                 ....
gi 148223615  94 ELEK 97
Cdd:cd03419   78 KLVK 81
PHA03050 PHA03050
glutaredoxin; Provisional
1-105 6.71e-27

glutaredoxin; Provisional


Pssm-ID: 165343  Cd Length: 108  Bit Score: 97.01  E-value: 6.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   1 MAQNFVQSKVKPSKVTMFEKSSCPFCVRAKGILTKYKFKEGHLEIIDISKLDFMSSLQQYFMQTTGESTVPRIYIGEKCI 80
Cdd:PHA03050   1 MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80
                         90       100
                 ....*....|....*....|....*
gi 148223615  81 GGCSDLVPLENSGELEKALESMGAL 105
Cdd:PHA03050  81 GGYSDLLEIDNMDALGDILSSIGVL 105
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
13-96 1.48e-15

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223767  Cd Length: 80  Bit Score: 66.57  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  13 SKVTMFEKSSCPFCVRAKGILTKYKFKeghLEIIDISKLDfMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENS 92
Cdd:COG0695    1 ANVTIYTKPGCPYCKRAKRLLDRKGVD---YEEIDVDDDE-PEEAREMVKRGKGQRTVPQIFIGGKHVGGCDDLDALEAK 76

                 ....
gi 148223615  93 GELE 96
Cdd:COG0695   77 GKLD 80
Glutaredoxin pfam00462
Glutaredoxin;
15-80 1.11e-14

Glutaredoxin;


Pssm-ID: 278868  Cd Length: 60  Bit Score: 63.67  E-value: 1.11e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223615   15 VTMFEKSSCPFCVRAKGILTKYKFKeghLEIIDISKldfMSSLQQYFMQTTGESTVPRIYIGEKCI 80
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLDSLGVK---FEEIDVDE---DPEIREELKELSGWPTVPQVFIDGEHI 60
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
14-95 2.02e-03

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 34.62  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  14 KVTMFEKSSCPFCVRAKGIL--TKYKFKEGHLEiIDISKLDFMSSLQQYFMQTTGE-STVPRIYIGEKCIGGCSDLvpLE 90
Cdd:PRK12759   3 EVRIYTKTNCPFCDLAKSWFgaNDIPFTQISLD-DDVKRAEFYAEVNKNILLVEEHiRTVPQIFVGDVHIGGYDNL--MA 79

                 ....*
gi 148223615  91 NSGEL 95
Cdd:PRK12759  80 RAGEV 84
 
Name Accession Description Interval E-value
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
15-99 7.73e-37

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: 121.58  E-value: 7.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   15 VTMFEKSSCPFCVRAKGILTKYKFKEghLEIIDISKLDFMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENSGE 94
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKLNVKP--YEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGK 78

                  ....*
gi 148223615   95 LEKAL 99
Cdd:TIGR02180  79 LAELL 83
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
14-97 1.45e-30

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: 105.31  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  14 KVTMFEKSSCPFCVRAKGILTKYKFKEGHLEIIDISKldfMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENSG 93
Cdd:cd03419    1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHED---GSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSG 77

                 ....
gi 148223615  94 ELEK 97
Cdd:cd03419   78 KLVK 81
PHA03050 PHA03050
glutaredoxin; Provisional
1-105 6.71e-27

glutaredoxin; Provisional


Pssm-ID: 165343  Cd Length: 108  Bit Score: 97.01  E-value: 6.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   1 MAQNFVQSKVKPSKVTMFEKSSCPFCVRAKGILTKYKFKEGHLEIIDISKLDFMSSLQQYFMQTTGESTVPRIYIGEKCI 80
Cdd:PHA03050   1 MAEEFVQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSI 80
                         90       100
                 ....*....|....*....|....*
gi 148223615  81 GGCSDLVPLENSGELEKALESMGAL 105
Cdd:PHA03050  81 GGYSDLLEIDNMDALGDILSSIGVL 105
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
14-90 2.34e-20

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: 78.66  E-value: 2.34e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148223615  14 KVTMFEKSSCPFCVRAKGILTKYKFKeghLEIIDISKLDfmsSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLE 90
Cdd:cd02066    1 KVVVFSKSTCPYCKRAKRLLESLGIE---FEEIDILEDG---ELREELKELSGWPTVPQIFINGEFIGGYDDLKALH 71
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
15-99 3.87e-20

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: 78.46  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   15 VTMFEKSSCPFCVRAKGILTKykfKEGHLEIIDIsklDFMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENSGE 94
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSS---KGVTFTEIRV---DGDPALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGK 74

                  ....*
gi 148223615   95 LEKAL 99
Cdd:TIGR02181  75 LDPLL 79
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
14-93 1.94e-18

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: 73.78  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  14 KVTMFEKSSCPFCVRAKGILTK--YKFKEghleiIDISKLDfmsSLQQYFMQTTG-ESTVPRIYIGEKCIGGCSDLVPLE 90
Cdd:cd03418    1 KVEIYTKPNCPYCVRAKALLDKkgVDYEE-----IDVDGDP---ALREEMINRSGgRRTVPQIFIGDVHIGGCDDLYALE 72

                 ...
gi 148223615  91 NSG 93
Cdd:cd03418   73 RKG 75
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
13-96 1.48e-15

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223767  Cd Length: 80  Bit Score: 66.57  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  13 SKVTMFEKSSCPFCVRAKGILTKYKFKeghLEIIDISKLDfMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENS 92
Cdd:COG0695    1 ANVTIYTKPGCPYCKRAKRLLDRKGVD---YEEIDVDDDE-PEEAREMVKRGKGQRTVPQIFIGGKHVGGCDDLDALEAK 76

                 ....
gi 148223615  93 GELE 96
Cdd:COG0695   77 GKLD 80
Glutaredoxin pfam00462
Glutaredoxin;
15-80 1.11e-14

Glutaredoxin;


Pssm-ID: 278868  Cd Length: 60  Bit Score: 63.67  E-value: 1.11e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223615   15 VTMFEKSSCPFCVRAKGILTKYKFKeghLEIIDISKldfMSSLQQYFMQTTGESTVPRIYIGEKCI 80
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLDSLGVK---FEEIDVDE---DPEIREELKELSGWPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
13-100 2.06e-13

glutaredoxin 3; Provisional


Pssm-ID: 182607  Cd Length: 83  Bit Score: 60.60  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  13 SKVTMFEKSSCPFCVRAKGILTKYKFKEGHLEIidisklDFMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLENS 92
Cdd:PRK10638   2 ANVEIYTKATCPFCHRAKALLNSKGVSFQEIPI------DGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDAR 75

                 ....*...
gi 148223615  93 GELEKALE 100
Cdd:PRK10638  76 GGLDPLLK 83
grxA PRK11200
glutaredoxin 1; Provisional
14-85 6.88e-10

glutaredoxin 1; Provisional


Pssm-ID: 183036  Cd Length: 85  Bit Score: 51.19  E-value: 6.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  14 KVTMFEKSSCPFCVRAKGILTKYK-----FKEGHLEIID--ISKLDfmsslqqyFMQTTGE--STVPRIYIGEKCIGGCS 84
Cdd:PRK11200   2 FVVIFGRPGCPYCVRAKELAEKLSeerddFDYRYVDIHAegISKAD--------LEKTVGKpvETVPQIFVDQKHIGGCT 73

                 .
gi 148223615  85 D 85
Cdd:PRK11200  74 D 74
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
13-86 1.13e-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  Cd Length: 72  Bit Score: 50.21  E-value: 1.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148223615  13 SKVTMFEKSSCPFCVRAKGILTK--YKFKEghleiIDISKLDFMSSLQqyfmQTTGESTVPRIYIGEKCIGGCSDL 86
Cdd:cd03029    1 ESVSLFTKPGCPFCARAKAALQEngISYEE-----IPLGKDITGRSLR----AVTGAMTVPQVFIDGELIGGSDDL 67
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
11-86 1.45e-09

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.


Pssm-ID: 131245  Cd Length: 79  Bit Score: 50.22  E-value: 1.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223615   11 KPSKVTMFEKSSCPFCVRAKGILTK--YKFKEghleiIDISKLDFMSSLQqyfmQTTGESTVPRIYIGEKCIGGCSDL 86
Cdd:TIGR02190   6 KPESVVVFTKPGCPFCAKAKATLKEkgYDFEE-----IPLGNDARGRSLR----AVTGATTVPQVFIGGKLIGGSDEL 74
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
14-91 1.99e-08

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: 46.64  E-value: 1.99e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148223615  14 KVTMFEKSSCPFCVRAKGILtkykfKEGHLEIIDISkLDFMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSDLVPLEN 91
Cdd:cd03027    2 RVTIYSRLGCEDCTAVRLFL-----REKGLPYVEIN-IDIFPERKAELEERTGSSVVPQIFFNEKLVGGLTDLKSLEE 73
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
6-105 7.38e-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  Cd Length: 99  Bit Score: 45.52  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615    6 VQSKVKPSKVTMFEKSSCPFCVRAKGILTKYKFkegHLEIIDISKLDFMSSLQQYFMQTTGESTVPRIYIGEKCIGGCSD 85
Cdd:TIGR02189   1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGV---NPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLEN 77
                          90       100
                  ....*....|....*....|
gi 148223615   86 LVPLENSGELEKALESMGAL 105
Cdd:TIGR02189  78 VMALHISGSLVPMLKQAGAL 97
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
15-85 4.74e-07

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: 42.89  E-value: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   15 VTMFEKSSCPFCVRAKGILTK---------YKFKEGHLEiiDISKLDFMSSLQQYFmqttgeSTVPRIYIGEKCIGGCSD 85
Cdd:TIGR02183   2 VVIFGRPGCPYCVRAKQLAEKlaieradfeFRYIDIHAE--GISKADLEKTVGKPV------ETVPQIFVDEKHVGGCTD 73
GrxD COG0278
Glutaredoxin-related protein [Posttranslational modification, protein turnover, chaperones];
5-103 2.89e-06

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


Pssm-ID: 223355  Cd Length: 105  Bit Score: 41.12  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615   5 FVQSKVKPSKVTMFEKSS-----CPFCVRAKGILTKYKFKEghLEIIDI-SKLDFMSSLQQYfmqtTGESTVPRIYIGEK 78
Cdd:COG0278    7 RIQKQIKENPVVLFMKGTpefpqCGFSAQAVQILSACGVVD--FAYVDVlQDPEIRQGLKEY----SNWPTFPQLYVNGE 80
                         90       100
                 ....*....|....*....|....*
gi 148223615  79 CIGGCSDLVPLENSGELEKALESMG 103
Cdd:COG0278   81 FVGGCDIVREMYQSGELQTLLKEAG 105
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
14-82 8.52e-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  Cd Length: 74  Bit Score: 39.28  E-value: 8.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148223615   14 KVTMFEKSSCPFCVRAKGILTKY--KFKEghleiIDISKldfMSSLQQYFMQTTGESTVPRIYIGEKCIGG 82
Cdd:TIGR02196   1 KVKVYTTPWCPPCVKAKEYLTSKgvAFEE-----IDVEK---DAAAREELLKVYGQRGVPVIVIGHKIVVG 63
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
14-99 8.61e-04

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


Pssm-ID: 239274  Cd Length: 73  Bit Score: 33.74  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  14 KVTMFEKSSCPFCVRAKGILTKYKFKeghLEIIDISK----LDFMSSLqqyfmqtTGESTVPRIYIGEKCIGGcsdlvpl 89
Cdd:cd02976    1 EVTVYTKPDCPYCKATKRFLDERGIP---FEEVDVDEdpeaLEELKKL-------NGYRSVPVVVIGDEHLSG------- 63
                         90
                 ....*....|
gi 148223615  90 ENSGELEKAL 99
Cdd:cd02976   64 FRPDKLRALL 73
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
69-100 9.41e-03

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: 32.21  E-value: 9.41e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 148223615  69 TVPRIYIGEKCIGGCSDLVPLENSGELEKALE 100
Cdd:cd03031   60 SLPRVFVDGRYLGGAEEVLRLNESGELRKLLK 91
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
14-95 2.02e-03

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 34.62  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223615  14 KVTMFEKSSCPFCVRAKGIL--TKYKFKEGHLEiIDISKLDFMSSLQQYFMQTTGE-STVPRIYIGEKCIGGCSDLvpLE 90
Cdd:PRK12759   3 EVRIYTKTNCPFCDLAKSWFgaNDIPFTQISLD-DDVKRAEFYAEVNKNILLVEEHiRTVPQIFVGDVHIGGYDNL--MA 79

                 ....*
gi 148223615  91 NSGEL 95
Cdd:PRK12759  80 RAGEV 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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