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Conserved domains on  [gi|757598043|ref|WP_042845694|]
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MULTISPECIES: glutaredoxin family protein [Providencia]

Protein Classification

glutaredoxin family protein( domain architecture ID 10002164)

glutaredoxin (GRX) family protein similar to GRX, a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035
PubMed:  14713336|15706083|15558583|12074972|30367780

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
8-83 1.29e-21

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 79.86  E-value: 1.29e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757598043  8 QILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEHIFYGtFSSQKpnILAALK 83
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDeDPEAREELRERSGRRTVPVIFIGGEHLGG-FDEGE--LDALLA 74
 
Name Accession Description Interval E-value
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
8-83 1.29e-21

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 79.86  E-value: 1.29e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757598043  8 QILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEHIFYGtFSSQKpnILAALK 83
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDeDPEAREELRERSGRRTVPVIFIGGEHLGG-FDEGE--LDALLA 74
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 9-82 1.24e-15

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: 64.94  E-value: 1.24e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEHIFYGtFSSQKpnILAAL 82
Cdd:cd02976   2 VTVYTKPDCPYCKATKRFLDERGIPFEEVDVDeDPEALEELKKLNGYRSVPVVVIGDEHLSG-FRPDK--LRALL 73
Glutaredoxin pfam00462
Glutaredoxin;
9-66 2.01e-14

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 61.37  E-value: 2.01e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIII-GEHI 66
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDeDPEIREELKELSGWPTVPQVFIdGEHI 60
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 9-75 2.90e-12

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: 56.23  E-value: 2.90e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEHIFYGtFSSQK 75
Cdd:TIGR02196  2 VKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEkDAAAREELLKVYGQRGVPVIVIGHKIVVG-FDPEK 68
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 9-64 9.16e-12

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: 54.77  E-value: 9.16e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKART-GVRVAPIIIIGE 64
Cdd:NF041212  1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVSkDPEALEEMLRLTgGERIVPVIVEGG 58
PRK10638 PRK10638
glutaredoxin 3; Provisional
 9-66 1.60e-04

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 36.72  E-value: 1.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIII-GEHI 66
Cdd:PRK10638  4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDgDAAKREEMIKRSGRTTVPQIFIdAQHI 63
 
Name Accession Description Interval E-value
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
8-83 1.29e-21

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 79.86  E-value: 1.29e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757598043  8 QILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEHIFYGtFSSQKpnILAALK 83
Cdd:COG0695   1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDeDPEAREELRERSGRRTVPVIFIGGEHLGG-FDEGE--LDALLA 74
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 9-82 1.24e-15

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: 64.94  E-value: 1.24e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEHIFYGtFSSQKpnILAAL 82
Cdd:cd02976   2 VTVYTKPDCPYCKATKRFLDERGIPFEEVDVDeDPEALEELKKLNGYRSVPVVVIGDEHLSG-FRPDK--LRALL 73
Glutaredoxin pfam00462
Glutaredoxin;
9-66 2.01e-14

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 61.37  E-value: 2.01e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIII-GEHI 66
Cdd:pfam00462  1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDeDPEIREELKELSGWPTVPQVFIdGEHI 60
GlrX_YruB TIGR02196
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ...
 9-75 2.90e-12

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: 56.23  E-value: 2.90e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEHIFYGtFSSQK 75
Cdd:TIGR02196  2 VKVYTTPWCPPCVKAKEYLTSKGVAFEEIDVEkDAAAREELLKVYGQRGVPVIVIGHKIVVG-FDPEK 68
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 9-66 4.87e-12

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: 55.55  E-value: 4.87e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIII-GEHI 66
Cdd:cd02066   2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDILeDGELREELKELSGWPTVPQIFInGEFI 61
Uxx_star NF041212
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ...
 9-64 9.16e-12

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: 54.77  E-value: 9.16e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKART-GVRVAPIIIIGE 64
Cdd:NF041212  1 VVIYTKPGCPYCAAAKEDLARRGIPFEEIDVSkDPEALEEMLRLTgGERIVPVIVEGG 58
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 9-66 6.50e-09

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 47.58  E-value: 6.50e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVA-PIIIIGE-HI 66
Cdd:cd03418   2 VEIYTKPNCPYCVRAKALLDKKGVDYEEIDVDgDPALREEMINRSGGRRTvPQIFIGDvHI 62
GRX_bact TIGR02181
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 9-65 1.82e-08

Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]


Pssm-ID: 274017 [Multi-domain]  Cd Length: 79  Bit Score: 46.87  E-value: 1.82e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIIIGEH 65
Cdd:TIGR02181  1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVDgDPALRDEMMQRSGRRTVPQIFIGDV 58
GRX_hybridPRX5 cd03029
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ...
 7-66 4.48e-06

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: 40.58  E-value: 4.48e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757598043  7 EQILIYTTPTCPDCQQLKDWLAKEQLSFEERDLTDPKIMAEAKARTGVRVAPIIII-GEHI 66
Cdd:cd03029   1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAVTGAMTVPQVFIdGELI 61
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 9-63 6.71e-06

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: 39.99  E-value: 6.71e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757598043  9 ILIYTTPTCPDCQQLKDWLA-----KEQLSFEERDLTDPKIMAEAKARTGVRVAPIIIIG 63
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAelallNKGVKFEAVDVDEDPALEKELKRYGVGGVPTLVVF 60
GRX_DEP cd03027
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ...
 8-64 8.08e-06

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: 39.70  E-value: 8.08e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 757598043  8 QILIYTTPTCPDCQQLKDWLAKEQLSFEERDLTD-PKIMAEAKARTGVRVAPIIIIGE 64
Cdd:cd03027   2 RVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIfPERKAELEERTGSSVVPQIFFNE 59
GlrX_NrdH TIGR02194
Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox ...
 9-82 5.13e-05

Glutaredoxin-like protein NrdH; NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. Unlike other the glutaredoxins to which it is most closely related, NrdH aparrently does not interact with glutathione/glutathione reductase, but rather with thioredoxin reductase to catalyze the reduction of ribonucleotide reductase.


Pssm-ID: 131249  Cd Length: 72  Bit Score: 37.78  E-value: 5.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLTDPKIMAEAKARTGVRVAPIIIIGEHIfygTFSSQKPNILAAL 82
Cdd:TIGR02194  1 ITVYSKNNCVQCKMTKKALEEHGIAFEEINIDEQPEAIDYVKAQGFRQVPVIVADGDL---SWSGFRPDKLKAL 71
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 8-39 7.23e-05

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: 38.38  E-value: 7.23e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 757598043   8 QILIYTTPTCPDCQQLKDWLAKEQLSFEERDL 39
Cdd:cd03032    1 MIKLYTSPSCSSCRKAKQWLEEHQIPFEERNL 32
PRK10638 PRK10638
glutaredoxin 3; Provisional
 9-66 1.60e-04

glutaredoxin 3; Provisional


Pssm-ID: 182607 [Multi-domain]  Cd Length: 83  Bit Score: 36.72  E-value: 1.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757598043  9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLT-DPKIMAEAKARTGVRVAPIIII-GEHI 66
Cdd:PRK10638  4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPIDgDAAKREEMIKRSGRTTVPQIFIdAQHI 63
spxA PRK13344
transcriptional regulator Spx; Reviewed
 9-47 3.21e-04

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 36.87  E-value: 3.21e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLTDPKIMAE 47
Cdd:PRK13344   2 IKIYTISSCTSCKKAKTWLNAHQLSYKEQNLGKEPLTKE 40
spxA PRK01655
transcriptional regulator Spx; Reviewed
 9-42 6.25e-04

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 35.82  E-value: 6.25e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDL-TDP 42
Cdd:PRK01655   2 VTLFTSPSCTSCRKAKAWLEEHDIPFTERNIfSSP 36
PRK12559 PRK12559
transcriptional regulator Spx; Provisional
 9-39 7.19e-03

transcriptional regulator Spx; Provisional


Pssm-ID: 79035  Cd Length: 131  Bit Score: 33.15  E-value: 7.19e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 757598043   9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDL 39
Cdd:PRK12559   2 VVLYTTASCASCRKAKAWLEENQIDYTEKNI 32
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 9-60 7.90e-03

transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins within the larger set covered by pfam03960. That larger family includes a glutaredoxin-dependent arsenate reductase (TIGR00014). Characterized members of this family include Spx and MgsR from Bacillus subtili. Spx is a global regulator for response to thiol-specific oxidative stress. It interacts with RNA polymerase. MgsR (modulator of the general stress response, also called YqgZ) provides a second level of regulation for more than a third of the proteins in the B. subtilis general stress regulon controlled by Sigma-B. [Regulatory functions, DNA interactions]


Pssm-ID: 273720  Cd Length: 117  Bit Score: 32.79  E-value: 7.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 757598043    9 ILIYTTPTCPDCQQLKDWLAKEQLSFEERDLTDPKIMAEA----KARTGVRVAPII 60
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREElldiLSLLEDGIDPLL 56
 
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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