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Conserved domains on  [gi|1447667943|gb|AXN06353|]
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glutathione peroxidase [Vibrio anguillarum]

Protein Classification

glutathione peroxidase( domain architecture ID 10786285)

glutathione peroxidase is a hybrid protein containing peroxiredoxin (PRX) and glutaredoxin (GRX) domains, similar to Marichromatium gracile glutathione amide-dependent peroxidase that catalyzes the oxidation of glutathione amide (GASH) to produce glutathione amide disulfide (GASSAG)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
5-163 3.55e-108

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440442  Cd Length: 160  Bit Score: 308.56  E-value: 3.55e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   5 KEGQAVPQVTFPTRQGDAWVNLTTDQLFKGKTVIVFSLPGAFTPTCSSSHLPRYNELYPVFKEHGVDDILCVSVNDTFVM 84
Cdd:COG0678     3 KVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943  85 NAWKADQEAEN-ITFIPDGNGEFTDGMGMLVDKSQIGFGKRSWRYSMLVKDGIIEKMFIEadEPGDPFKVSDADTMLKYI 163
Cdd:COG0678    83 NAWGKAQGAEGkITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVE--PAPGPFEVSDAETLLAQL 160
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
164-242 4.35e-47

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: 150.76  E-value: 4.35e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 164 APNYKTQESVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGRTTVPQVFVGGKHIGGSEELEAYLG 242
Cdd:TIGR02190   1 APQARKPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAYLA 79
 
Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
5-163 3.55e-108

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 308.56  E-value: 3.55e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   5 KEGQAVPQVTFPTRQGDAWVNLTTDQLFKGKTVIVFSLPGAFTPTCSSSHLPRYNELYPVFKEHGVDDILCVSVNDTFVM 84
Cdd:COG0678     3 KVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943  85 NAWKADQEAEN-ITFIPDGNGEFTDGMGMLVDKSQIGFGKRSWRYSMLVKDGIIEKMFIEadEPGDPFKVSDADTMLKYI 163
Cdd:COG0678    83 NAWGKAQGAEGkITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVE--PAPGPFEVSDAETLLAQL 160
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
6-161 5.29e-74

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 221.67  E-value: 5.29e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   6 EGQAVPQVTFPTRQGDAWVNLTTDQLFKGKTVIVFSLPGAFTPTCSSSHLPRYNELYPVFKEHGVDDILCVSVNDTFVMN 85
Cdd:cd03013     1 VGDKLPNVTLFEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447667943  86 AWKADQEAEN-ITFIPDGNGEFTDGMGMLVDKSQIGFGKRSWRYSMLVKDGIIEKMFIEadEPGDPFKVSDADTMLK 161
Cdd:cd03013    81 AWGKALGAKDkIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVE--EDPGDVEVSSAENVLK 155
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
164-242 4.35e-47

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: 150.76  E-value: 4.35e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 164 APNYKTQESVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGRTTVPQVFVGGKHIGGSEELEAYLG 242
Cdd:TIGR02190   1 APQARKPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAYLA 79
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
171-241 3.94e-41

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: 135.34  E-value: 3.94e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447667943 171 ESVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGRTTVPQVFVGGKHIGGSEELEAYL 241
Cdd:cd03029     1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAVTGAMTVPQVFIDGELIGGSDDLEKYF 71
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
5-160 1.76e-34

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 120.55  E-value: 1.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   5 KEGQAVPQVTFPTRQGDAwvNLTTDQLFKGKTVIVFSLPGAFTPTCSSSHlPRYNELYPVFKEHGVDDILCVSVNDTF-V 83
Cdd:pfam08534   1 KAGDKAPDFTLPDAATDG--NTVSLSDFKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943  84 MNAWKadQEAENITFIPDGNGEFTD--GMGMLVDKSQigfGKRSWRYSMLVKDGIIEKMFIEADepgDPFKVSDADTML 160
Cdd:pfam08534  78 KRFWG--KEGLPFPFLSDGNAAFTKalGLPIEEDASA---GLRSPRYAVIDEDGKVVYLFVGPE---PGVDVSDAEAVL 148
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
173-242 1.61e-24

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 92.57  E-value: 1.61e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHIGG--SEELEAYLG 242
Cdd:COG0695     2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREeLRERSGRRTVPVIFIGGEHLGGfdEGELDALLA 74
Glutaredoxin pfam00462
Glutaredoxin;
173-231 9.51e-22

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 84.86  E-value: 9.51e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHI 231
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREeLKELSGWPTVPQVFIDGEHI 60
PRK10638 PRK10638
glutaredoxin 3; Provisional
172-239 4.97e-15

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 67.92  E-value: 4.97e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 172 SVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHIGGSEELEA 239
Cdd:PRK10638    3 NVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREeMIKRSGRTTVPQIFIDAQHIGGCDDLYA 71
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
173-229 5.53e-08

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 48.61  E-value: 5.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS--LRAITGRTTVPQVFVGGK 229
Cdd:NF041212    1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVSKDPEALEemLRLTGGERIVPVIVEGGE 59
PRK13189 PRK13189
peroxiredoxin; Provisional
7-113 7.81e-07

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 48.44  E-value: 7.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   7 GQAVPQVTFPTRQGDawVNLTTDqlFKGKTVIVFSLPGAFTPTCSSSHLPrYNELYPVFKEHGVDDIlCVSVNDTFVMNA 86
Cdd:PRK13189   12 GDKFPEFEVKTTHGP--IKLPDD--YKGKWFVLFSHPADFTPVCTTEFVA-FQKRYDEFRELNTELI-GLSIDQVFSHIK 85
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1447667943  87 W------KADQEaenITF--IPDGNGEFTDGMGML 113
Cdd:PRK13189   86 WvewikeKLGVE---IEFpiIADDRGEIAKKLGMI 117
 
Name Accession Description Interval E-value
AHP1 COG0678
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
5-163 3.55e-108

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440442  Cd Length: 160  Bit Score: 308.56  E-value: 3.55e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   5 KEGQAVPQVTFPTRQGDAWVNLTTDQLFKGKTVIVFSLPGAFTPTCSSSHLPRYNELYPVFKEHGVDDILCVSVNDTFVM 84
Cdd:COG0678     3 KVGDKLPDVTFKTRTADGPEDVTTDDLFAGKKVVLFAVPGAFTPTCSSAHLPGFVELADAFKAKGVDEIACVSVNDAFVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943  85 NAWKADQEAEN-ITFIPDGNGEFTDGMGMLVDKSQIGFGKRSWRYSMLVKDGIIEKMFIEadEPGDPFKVSDADTMLKYI 163
Cdd:COG0678    83 NAWGKAQGAEGkITMLADGNGEFTKALGLEVDKSALGFGKRSQRYAMLVEDGVVKKLNVE--PAPGPFEVSDAETLLAQL 160
PRX5_like cd03013
Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, ...
6-161 5.29e-74

Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.


Pssm-ID: 239311 [Multi-domain]  Cd Length: 155  Bit Score: 221.67  E-value: 5.29e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   6 EGQAVPQVTFPTRQGDAWVNLTTDQLFKGKTVIVFSLPGAFTPTCSSSHLPRYNELYPVFKEHGVDDILCVSVNDTFVMN 85
Cdd:cd03013     1 VGDKLPNVTLFEYVPGPPNPVNLSELFKGKKVVIFGVPGAFTPTCSAQHLPGYVENADELKAKGVDEVICVSVNDPFVMK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447667943  86 AWKADQEAEN-ITFIPDGNGEFTDGMGMLVDKSQIGFGKRSWRYSMLVKDGIIEKMFIEadEPGDPFKVSDADTMLK 161
Cdd:cd03013    81 AWGKALGAKDkIRFLADGNGEFTKALGLTLDLSAAGGGIRSKRYALIVDDGKVKYLFVE--EDPGDVEVSSAENVLK 155
GlrX-dom TIGR02190
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ...
164-242 4.35e-47

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: 150.76  E-value: 4.35e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 164 APNYKTQESVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGRTTVPQVFVGGKHIGGSEELEAYLG 242
Cdd:TIGR02190   1 APQARKPESVVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAVTGATTVPQVFIGGKLIGGSDELEAYLA 79
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
171-241 3.94e-41

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: 135.34  E-value: 3.94e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447667943 171 ESVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGRTTVPQVFVGGKHIGGSEELEAYL 241
Cdd:cd03029     1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAVTGAMTVPQVFIDGELIGGSDDLEKYF 71
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
10-160 1.72e-34

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They 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 TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 120.35  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943  10 VPQVTFPTRQGDaWVNLTTdqlFKGKTVIVFSLPGAFTPTCSSShLPRYNELYPVFKEHGVDdILCVSVNDTFVMNAWKA 89
Cdd:cd02971     2 APDFTLPATDGG-EVSLSD---FKGKWVVLFFYPKDFTPVCTTE-LCAFRDLAEEFAKGGAE-VLGVSVDSPFSHKAWAE 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447667943  90 DQEAENITFIPDGNGEFTDGMGMLVDKSqiGFGKRSWRYSMLV-KDGIIEKMFIEADEpgdpfKVSDADTML 160
Cdd:cd02971    76 KEGGLNFPLLSDPDGEFAKAYGVLIEKS--AGGGLAARATFIIdPDGKIRYVEVEPLP-----TGRNAEELL 140
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
5-160 1.76e-34

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 120.55  E-value: 1.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   5 KEGQAVPQVTFPTRQGDAwvNLTTDQLFKGKTVIVFSLPGAFTPTCSSSHlPRYNELYPVFKEHGVDDILCVSVNDTF-V 83
Cdd:pfam08534   1 KAGDKAPDFTLPDAATDG--NTVSLSDFKGKKVVLNFWPGAFCPTCSAEH-PYLEKLNELYKEKGVDVVAVNSDNDAFfV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943  84 MNAWKadQEAENITFIPDGNGEFTD--GMGMLVDKSQigfGKRSWRYSMLVKDGIIEKMFIEADepgDPFKVSDADTML 160
Cdd:pfam08534  78 KRFWG--KEGLPFPFLSDGNAAFTKalGLPIEEDASA---GLRSPRYAVIDEDGKVVYLFVGPE---PGVDVSDAEAVL 148
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
173-242 1.61e-24

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 92.57  E-value: 1.61e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHIGG--SEELEAYLG 242
Cdd:COG0695     2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAREeLRERSGRRTVPVIFIGGEHLGGfdEGELDALLA 74
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
173-240 2.19e-23

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: 89.45  E-value: 2.19e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHIGGSEELEAY 240
Cdd:cd02066     2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDILEDGELREeLKELSGWPTVPQIFINGEFIGGYDDLKAL 70
Glutaredoxin pfam00462
Glutaredoxin;
173-231 9.51e-22

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 84.86  E-value: 9.51e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHI 231
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREeLKELSGWPTVPQVFIDGEHI 60
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
173-239 6.01e-21

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: 83.41  E-value: 6.01e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDAttvSLRA--IT---GRTTVPQVFVGGKHIGGSEELEA 239
Cdd:cd03418     2 VEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDP---ALREemINrsgGRRTVPQIFIGDVHIGGCDDLYA 70
GRX_GRXh_1_2_like cd03419
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ...
173-240 1.02e-20

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: 82.97  E-value: 1.02e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS----LRAITGRTTVPQVFVGGKHIGGSEELEAY 240
Cdd:cd03419     2 VVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEiqdyLQELTGQRTVPNVFIGGKFIGGCDDLMAL 73
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
173-239 1.74e-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 [Multi-domain]  Cd Length: 79  Bit Score: 82.31  E-value: 1.74e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDAttvSLRAI----TGRTTVPQVFVGGKHIGGSEELEA 239
Cdd:TIGR02181   1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDGDP---ALRDEmmqrSGRRTVPQIFIGDVHVGGCDDLYA 68
GRX_euk TIGR02180
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ...
173-240 2.56e-18

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 [Multi-domain]  Cd Length: 83  Bit Score: 76.51  E-value: 2.56e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLID---HGLQYEEVVLGKDATTVS--LRAITGRTTVPQVFVGGKHIGGSEELEAY 240
Cdd:TIGR02180   1 VVVFSKSYCPYCKKAKEILAKlnvKPYEVVELDQLSNGSEIQdyLEEITGQRTVPNIFINGKFIGGCSDLLAL 73
PRK10638 PRK10638
glutaredoxin 3; Provisional
172-239 4.97e-15

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 67.92  E-value: 4.97e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 172 SVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHIGGSEELEA 239
Cdd:PRK10638    3 NVEIYTKATCPFCHRAKALLNSKGVSFQEIPIDGDAAKREeMIKRSGRTTVPQIFIDAQHIGGCDDLYA 71
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
173-241 9.00e-14

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: 64.17  E-value: 9.00e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHIGGS--EELEAYL 241
Cdd:cd02976     2 VTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEALEeLKKLNGYRSVPVVVIGDEHLSGFrpDKLRALL 73
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
7-140 5.68e-13

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 63.78  E-value: 5.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   7 GQAVPQVTFPTRQGdAWVNLTTdqlFKGKTVIVFSLPGAFTPTCsSSHLPRYNELYPVFKEHGVdDILCVSVNDTFVMNA 86
Cdd:pfam00578   2 GDKAPDFELPDGDG-GTVSLSD---YRGKWVVLFFYPADWTPVC-TTELPALADLYEEFKKLGV-EVLGVSVDSPESHKA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1447667943  87 WKADQEAeNITFIPDGNGEFTDGMGMLVDKSQIGfgkrsWRYSMLV-KDGIIEKM 140
Cdd:pfam00578  76 FAEKYGL-PFPLLSDPDGEVARAYGVLNEEEGGA-----LRATFVIdPDGKVRYI 124
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
173-238 3.24e-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 [Multi-domain]  Cd Length: 73  Bit Score: 60.12  E-value: 3.24e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDAT-TVSLRAITGRTTVPQVFVGGKHIGGSEELE 238
Cdd:cd03027     3 VTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPErKAELEERTGSSVVPQIFFNEKLVGGLTDLK 69
grxA PRK11200
glutaredoxin 1; Provisional
173-240 2.60e-11

glutaredoxin 1; Provisional


Pssm-ID: 183036 [Multi-domain]  Cd Length: 85  Bit Score: 58.12  E-value: 2.60e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447667943 173 VTVFTKPGCPFCTKAKQL---LIDH--GLQYEEV-VLGKDATTVSLRAITGRT--TVPQVFVGGKHIGGSEELEAY 240
Cdd:PRK11200    3 VVIFGRPGCPYCVRAKELaekLSEErdDFDYRYVdIHAEGISKADLEKTVGKPveTVPQIFVDQKHIGGCTDFEAY 78
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
173-242 8.01e-11

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: 56.62  E-value: 8.01e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRTTVPQVFVGGKHIGG--SEELEAYLG 242
Cdd:TIGR02196   2 VKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEKDAAAREeLLKVYGQRGVPVIVIGHKIVVGfdPEKLDQLLN 74
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
7-113 8.06e-10

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 56.62  E-value: 8.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   7 GQAVPQVTFPTRQGDAWVNLTTDQlFKGKTVIVFSLPGAFTPTCsSSHLPRYNELYPVFKEHGVdDILCVSVNDTFVMNA 86
Cdd:COG0450     6 GDKAPDFTAEATHGGEFKKISLSD-YKGKWVVLFFHPADFTFVC-PTELGAFAKRYEEFKKLGV-EVIGLSVDSVFSHKA 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1447667943  87 WKAD-QEAENITFIP-----DGNGEFTDGMGML 113
Cdd:COG0450    83 WHETiKEKGGIVKIKfpiiaDPTGKIARAYGML 115
GlrX-like_plant TIGR02189
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ...
172-239 6.57e-09

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: 52.07  E-value: 6.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447667943 172 SVTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGR----TTVPQVFVGGKHIGGSEELEA 239
Cdd:TIGR02189   9 AVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRlgcsPAVPAVFVGGKLVGGLENVMA 80
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
5-156 1.47e-08

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective 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. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 52.28  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   5 KEGQAVPQVTFPTRQGDAwVNLTtDQLFKGKTVIVFsLPGAFTPTCsSSHLPRYNELYPVFKEHGVdDILCVSVNDTFVM 84
Cdd:cd03018     2 EVGDKAPDFELPDQNGQE-VRLS-EFRGRKPVVLVF-FPLAFTPVC-TKELCALRDSLELFEAAGA-EVLGISVDSPFSL 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447667943  85 NAWkADQEAENITFIPDGN--GEFTDGMGMLVDKSqiGFGKRSwrySMLV-KDGIIEKMFIEAD-EPGDPFKVSDA 156
Cdd:cd03018    77 RAW-AEENGLTFPLLSDFWphGEVAKAYGVFDEDL--GVAERA---VFVIdRDGIIRYAWVSDDgEPRDLPDYDEA 146
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
173-229 5.53e-08

Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.


Pssm-ID: 469116 [Multi-domain]  Cd Length: 70  Bit Score: 48.61  E-value: 5.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS--LRAITGRTTVPQVFVGGK 229
Cdd:NF041212    1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVSKDPEALEemLRLTGGERIVPVIVEGGE 59
GRXA TIGR02183
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
173-241 3.90e-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 [Multi-domain]  Cd Length: 86  Bit Score: 46.74  E-value: 3.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447667943 173 VTVFTKPGCPFCTKAKQL-------LIDHGLQYEEVVlGKDATTVSLRAITGRT--TVPQVFVGGKHIGGSEELEAYL 241
Cdd:TIGR02183   2 VVIFGRPGCPYCVRAKQLaeklaieRADFEFRYIDIH-AEGISKADLEKTVGKPveTVPQIFVDEKHVGGCTDFEQLV 78
PRK13189 PRK13189
peroxiredoxin; Provisional
7-113 7.81e-07

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 48.44  E-value: 7.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   7 GQAVPQVTFPTRQGDawVNLTTDqlFKGKTVIVFSLPGAFTPTCSSSHLPrYNELYPVFKEHGVDDIlCVSVNDTFVMNA 86
Cdd:PRK13189   12 GDKFPEFEVKTTHGP--IKLPDD--YKGKWFVLFSHPADFTPVCTTEFVA-FQKRYDEFRELNTELI-GLSIDQVFSHIK 85
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1447667943  87 W------KADQEaenITF--IPDGNGEFTDGMGML 113
Cdd:PRK13189   86 WvewikeKLGVE---IEFpiIADDRGEIAKKLGMI 117
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
32-137 1.08e-06

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 47.50  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943  32 FKGKTVIVFSLPGAFTPTCsSSHLPRYNELYPVFKEHGVdDILCVSVNDTFVMNAWKADQEAE------NITFIPDGNGE 105
Cdd:cd03015    27 YKGKWVVLFFYPLDFTFVC-PTEIIAFSDRYEEFKKLNA-EVLGVSTDSHFSHLAWRNTPRKEgglgkiNFPLLADPKKK 104
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1447667943 106 FTDGMGMLVDKSQIgfgkrSWRYSMLV-KDGII 137
Cdd:cd03015   105 ISRDYGVLDEEEGV-----ALRGTFIIdPEGII 132
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
176-241 2.47e-06

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 44.14  E-value: 2.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447667943 176 FTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGRTTVPQVFVGGKHIGGSEELEAYL 241
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYL 67
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
8-153 3.23e-06

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 45.23  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   8 QAVPQVTFPTRQGDaWVNLTTdqlFKGKTVIVFSLPGAFTPTCsSSHLPRYNELYPVFKEHGVdDILCVSVNDTFVMNAW 87
Cdd:cd03017     1 DKAPDFTLPDQDGE-TVSLSD---LRGKPVVLYFYPKDDTPGC-TKEACDFRDLYEEFKALGA-VVIGVSPDSVESHAKF 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447667943  88 KADQEAeNITFIPDGNGEFTDGMGMLVDKSQIGFG-KRSwrySMLV-KDGIIEKMFIEADEPGDPFKV 153
Cdd:cd03017    75 AEKYGL-PFPLLSDPDGKLAKAYGVWGEKKKKYMGiERS---TFLIdPDGKIVKVWRKVKPKGHAEEV 138
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
173-211 3.57e-06

Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif.


Pssm-ID: 239330  Cd Length: 115  Bit Score: 44.93  E-value: 3.57e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS 211
Cdd:cd03032     2 IKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKE 40
PRK12759 PRK12759
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
173-242 1.74e-05

bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional


Pssm-ID: 139206 [Multi-domain]  Cd Length: 410  Bit Score: 45.02  E-value: 1.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVSLRAITGRT---------TVPQVFVGGKHIGGSEELEAYLG 242
Cdd:PRK12759    4 VRIYTKTNCPFCDLAKSWFGANDIPFTQISLDDDVKRAEFYAEVNKNillveehirTVPQIFVGDVHIGGYDNLMARAG 82
PRK13190 PRK13190
putative peroxiredoxin; Provisional
5-92 2.36e-05

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 44.07  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   5 KEGQAVPQVTFPTRQGDawVNLTTDqlfKGKTVIVFSLPGAFTPTCSSSHLpRYNELYPVFKEHGVdDILCVSVNDTFVM 84
Cdd:PRK13190    3 KLGQKAPDFTVNTTKGP--IDLSKY---KGKWVLLFSHPADFTPVCTTEFI-AFSRRYEDFKKLGV-ELVGLSVDSIYSH 75

                  ....*...
gi 1447667943  85 NAWKADQE 92
Cdd:PRK13190   76 IAWLRDIE 83
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
7-113 3.53e-05

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 43.30  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943   7 GQAVPQVTFPTRQGDawVNLTtdQLFKGKTVIVFSLPGAFTPTCsSSHLPRYNELYPVFKEHGVdDILCVSVNDTFVMNA 86
Cdd:cd03016     2 GDTAPNFEADTTHGP--IKFH--DYLGDSWGILFSHPADFTPVC-TTELGAFAKLAPEFKKRNV-KLIGLSVDSVESHIK 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1447667943  87 WKADQEA---ENITF--IPDGNGEFTDGMGML 113
Cdd:cd03016    76 WIEDIEEytgVEIPFpiIADPDREVAKLLGMI 107
GRX_PICOT_like cd03028
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ...
170-235 3.53e-05

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: 41.32  E-value: 3.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447667943 170 QESVTVFTK-----PGCPFCTKAKQLLIDHGLQYEEV-VLGKDATTVSLRAITGRTTVPQVFVGGKHIGGSE 235
Cdd:cd03028     7 ENPVVLFMKgtpeePRCGFSRKVVQILNQLGVDFGTFdILEDEEVRQGLKEYSNWPTFPQLYVNGELVGGCD 78
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
173-241 9.78e-05

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 39.48  E-value: 9.78e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLG-KDATTVSLRAITGRTTVPQVFVGGKHIGGSEELEAYL 241
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDlGEGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYL 70
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
173-219 1.28e-04

Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins including the transcriptional regulator, Spx. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX), through a single catalytic cysteine. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases. Spx is a general regulator that exerts negative and positive control over transcription initiation by binding to the C-terminal domain of the alpha subunit of RNA polymerase.


Pssm-ID: 239275  Cd Length: 105  Bit Score: 40.17  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRT 219
Cdd:cd02977     1 ITIYGNPNCSTSRKALAWLEEHGIEYEFIDYLKEPPTKEeLKELLAKL 48
PHA03050 PHA03050
glutaredoxin; Provisional
169-237 3.25e-04

glutaredoxin; Provisional


Pssm-ID: 165343 [Multi-domain]  Cd Length: 108  Bit Score: 39.23  E-value: 3.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447667943 169 TQESVTVFTKPGCPFCTKAKQLLIDHGLQ---YEEVVLGKDATTVSL----RAITGRTTVPQVFVGGKHIGGSEEL 237
Cdd:PHA03050   11 ANNKVTIFVKFTCPFCRNALDILNKFSFKrgaYEIVDIKEFKPENELrdyfEQITGGRTVPRIFFGKTSIGGYSDL 86
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
184-239 4.85e-04

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 39.14  E-value: 4.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447667943 184 CTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAITGRT----TVPQVFVGGKHIGGSEELEA 239
Cdd:cd03031    19 CNNVRAILESFRVKFDERDVSMDSGFREeLRELLGAElkavSLPRVFVDGRYLGGAEEVLR 79
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
173-232 1.00e-03

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 36.91  E-value: 1.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447667943 173 VTVFTKPGCPFCTKAKQLL-----IDHGLQYEEVVLGKDATTVSLRAITGRTTVPQVFVGGKHIG 232
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLaelalLNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIG 65
GlrX_actino TIGR02200
Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the ...
173-230 1.13e-03

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


Pssm-ID: 131255 [Multi-domain]  Cd Length: 77  Bit Score: 36.75  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447667943 173 VTVFTKPGCPFCTKAKQLLIDHGLQYEEVVLGKDATTVS-LRAIT-GRTTVPQV-FVGGKH 230
Cdd:TIGR02200   2 ITVYGTTWCGYCAQLMRTLDKLGAAYEWVDIEEDEGAADrVVSVNnGNMTVPTVkFADGSF 62
PRX_Atyp2cys cd03014
Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing ...
32-116 6.70e-03

Peroxiredoxin (PRX) family, Atypical 2-cys PRX subfamily; composed of PRXs containing peroxidatic and resolving cysteines, similar to the homodimeric thiol specific antioxidant (TSA) protein also known as TRX-dependent thiol peroxidase (Tpx). Tpx is a bacterial periplasmic peroxidase which differs from other PRXs in that it shows substrate specificity toward alkyl hydroperoxides over hydrogen peroxide. As with all other PRXs, the peroxidatic cysteine (N-terminal) of Tpx is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Tpx is able to resolve this intermediate by forming an intramolecular disulfide bond with a conserved C-terminal cysteine (the resolving cysteine), which can then be reduced by thioredoxin. This differs from the typical 2-cys PRX which resolves the oxidized cysteine by forming an intermolecular disulfide bond with the resolving cysteine from the other subunit of the homodimer. Atypical 2-cys PRX homodimers have a loop-based interface (A-type for alternate), in contrast with the B-type interface of typical 2-cys and 1-cys PRXs.


Pssm-ID: 239312 [Multi-domain]  Cd Length: 143  Bit Score: 36.02  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447667943  32 FKGKTVIVFSLPGAFTPTCSSShLPRYNELYpvfKEHGVDDILCVSVNDTFVMNAWKADQEAENITFIPD-GNGEFTDGM 110
Cdd:cd03014    24 FAGKVKVISVFPSIDTPVCATQ-TKRFNKEA---AKLDNTVVLTISADLPFAQKRWCGAEGVDNVTTLSDfRDHSFGKAY 99

                  ....*.
gi 1447667943 111 GMLVDK 116
Cdd:cd03014   100 GVLIKD 105
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
149-186 8.27e-03

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 36.14  E-value: 8.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1447667943 149 DPFKVSDADTMLKYIAPNYKTQesVTVFTKPGCPFCTK 186
Cdd:cd03020    59 IDLSALPLDDAIVYGKGNGKRV--VYVFTDPDCPYCRK 94
 
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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