MULTISPECIES: arsenate reductase family protein [Staphylococcus]
arsenate reductase family protein( domain architecture ID 10122556)
arsenate reductase (ArsC) family protein similar to Bacillus subtilis uncharacterized protein YusI and Geobacillus kaustophilus ArsC3, which is involved in arsenate reduction
List of domain hits
Name | Accession | Description | Interval | E-value | |||
ArsC_like | cd03036 | Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ... |
2-112 | 1.67e-56 | |||
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine. : Pssm-ID: 239334 Cd Length: 111 Bit Score: 170.50 E-value: 1.67e-56
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Name | Accession | Description | Interval | E-value | |||
ArsC_like | cd03036 | Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ... |
2-112 | 1.67e-56 | |||
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine. Pssm-ID: 239334 Cd Length: 111 Bit Score: 170.50 E-value: 1.67e-56
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arsC_related | TIGR01617 | transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ... |
2-117 | 4.96e-54 | |||
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: 164.53 E-value: 4.96e-54
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ArsC | COG1393 | Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ... |
1-116 | 7.39e-41 | |||
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism]; Pssm-ID: 441003 Cd Length: 115 Bit Score: 131.37 E-value: 7.39e-41
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ArsC | pfam03960 | ArsC family; This family is related to glutaredoxins pfam00462. |
5-114 | 2.42e-30 | |||
ArsC family; This family is related to glutaredoxins pfam00462. Pssm-ID: 427617 Cd Length: 109 Bit Score: 104.22 E-value: 2.42e-30
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PRK10853 | PRK10853 | putative reductase; Provisional |
1-114 | 2.89e-12 | |||
putative reductase; Provisional Pssm-ID: 182780 Cd Length: 118 Bit Score: 58.52 E-value: 2.89e-12
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ArsC_rel_Se_1 | NF041106 | ArsC family (seleno)protein; Weak hits to Pfam model PF03960 and to COG1393 suggest a ... |
5-112 | 4.50e-06 | |||
ArsC family (seleno)protein; Weak hits to Pfam model PF03960 and to COG1393 suggest a relationship to glutaredoxin-like arsenate reductase protein ArsC. This family contains significant numbers of selenoproteins. Pssm-ID: 469030 Cd Length: 107 Bit Score: 42.15 E-value: 4.50e-06
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Name | Accession | Description | Interval | E-value | |||
ArsC_like | cd03036 | Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ... |
2-112 | 1.67e-56 | |||
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine. Pssm-ID: 239334 Cd Length: 111 Bit Score: 170.50 E-value: 1.67e-56
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arsC_related | TIGR01617 | transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ... |
2-117 | 4.96e-54 | |||
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: 164.53 E-value: 4.96e-54
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ArsC | COG1393 | Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ... |
1-116 | 7.39e-41 | |||
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism]; Pssm-ID: 441003 Cd Length: 115 Bit Score: 131.37 E-value: 7.39e-41
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ArsC_family | cd02977 | Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ... |
2-107 | 1.20e-39 | |||
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: 127.99 E-value: 1.20e-39
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ArsC | pfam03960 | ArsC family; This family is related to glutaredoxins pfam00462. |
5-114 | 2.42e-30 | |||
ArsC family; This family is related to glutaredoxins pfam00462. Pssm-ID: 427617 Cd Length: 109 Bit Score: 104.22 E-value: 2.42e-30
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ArsC_Yffb | cd03035 | Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ... |
2-109 | 9.13e-20 | |||
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein encoded by the yffb gene, related to the thioredoxin-fold arsenic reductases, ArsC. The structure of Yffb and the conservation of the catalytic cysteine suggest that it is likely to function as a glutathione (GSH)-dependent thiol reductase. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from GSH via glutaredoxin, through a single catalytic cysteine. Pssm-ID: 239333 Cd Length: 105 Bit Score: 77.25 E-value: 9.13e-20
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ArsC_Spx | cd03032 | Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ... |
1-110 | 4.79e-19 | |||
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: 75.74 E-value: 4.79e-19
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ArsC_ArsC | cd03034 | Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded ... |
2-106 | 7.82e-13 | |||
Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded by arsC on the R733 plasmid of Escherichia coli. E. coli ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], the first step in the detoxification of arsenic, using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX). ArsC contains a single catalytic cysteine, within a thioredoxin fold, that forms a covalent thiolate-As(V) intermediate, which is reduced by GRX through a mixed GSH-arsenate intermediate. 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. Pssm-ID: 239332 Cd Length: 112 Bit Score: 59.91 E-value: 7.82e-13
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PRK10853 | PRK10853 | putative reductase; Provisional |
1-114 | 2.89e-12 | |||
putative reductase; Provisional Pssm-ID: 182780 Cd Length: 118 Bit Score: 58.52 E-value: 2.89e-12
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PRK12559 | PRK12559 | transcriptional regulator Spx; Provisional |
1-114 | 1.57e-10 | |||
transcriptional regulator Spx; Provisional Pssm-ID: 79035 Cd Length: 131 Bit Score: 54.34 E-value: 1.57e-10
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spxA | PRK13344 | transcriptional regulator Spx; Reviewed |
1-110 | 1.14e-09 | |||
transcriptional regulator Spx; Reviewed Pssm-ID: 183988 Cd Length: 132 Bit Score: 52.27 E-value: 1.14e-09
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spxA | PRK01655 | transcriptional regulator Spx; Reviewed |
1-111 | 4.07e-09 | |||
transcriptional regulator Spx; Reviewed Pssm-ID: 179316 Cd Length: 131 Bit Score: 50.46 E-value: 4.07e-09
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ArsC_rel_Se_1 | NF041106 | ArsC family (seleno)protein; Weak hits to Pfam model PF03960 and to COG1393 suggest a ... |
5-112 | 4.50e-06 | |||
ArsC family (seleno)protein; Weak hits to Pfam model PF03960 and to COG1393 suggest a relationship to glutaredoxin-like arsenate reductase protein ArsC. This family contains significant numbers of selenoproteins. Pssm-ID: 469030 Cd Length: 107 Bit Score: 42.15 E-value: 4.50e-06
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GrxC | COG0695 | Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
1-51 | 2.61e-05 | |||
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 39.41 E-value: 2.61e-05
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NrdH | cd02976 | NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
1-51 | 2.21e-04 | |||
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein. Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 36.82 E-value: 2.21e-04
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GST_N_mPGES2 | cd03040 | GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ... |
2-32 | 5.17e-04 | |||
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated, and a C-terminal soluble domain with a GST-like structure. Pssm-ID: 239338 Cd Length: 77 Bit Score: 36.23 E-value: 5.17e-04
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Glutaredoxin | pfam00462 | Glutaredoxin; |
2-35 | 5.88e-04 | |||
Glutaredoxin; Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 35.56 E-value: 5.88e-04
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GRX_GRXb_1_3_like | cd03418 | Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
2-32 | 7.39e-03 | |||
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: 32.95 E-value: 7.39e-03
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GlrX_YruB | TIGR02196 | Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ... |
1-32 | 8.77e-03 | |||
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: 32.74 E-value: 8.77e-03
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Blast search parameters | ||||
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