TlpA disulfide reductase family protein [Blautia sp. AF32-4BH]
TlpA disulfide reductase family protein( domain architecture ID 10121831)
TlpA disulfide reductase family protein such as Bradyrhizobium japonicum thiol:disulfide interchange protein TlpA, an unusual thioredoxin which has been implicated in the biogenesis of cytochrome aa3 and also characterized as a reductant for the copper metallochaperone ScoI
List of domain hits
Name | Accession | Description | Interval | E-value | |||
TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
168-287 | 4.00e-25 | |||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. : Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 97.31 E-value: 4.00e-25
|
|||||||
Name | Accession | Description | Interval | E-value | |||
TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
168-287 | 4.00e-25 | |||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 97.31 E-value: 4.00e-25
|
|||||||
TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
168-314 | 1.60e-24 | |||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 96.30 E-value: 1.60e-24
|
|||||||
AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
168-287 | 8.11e-14 | |||
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: 66.86 E-value: 8.11e-14
|
|||||||
PRK03147 | PRK03147 | thiol-disulfide oxidoreductase ResA; |
168-287 | 4.20e-10 | |||
thiol-disulfide oxidoreductase ResA; Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 57.71 E-value: 4.20e-10
|
|||||||
Name | Accession | Description | Interval | E-value | |||
TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
168-287 | 4.00e-25 | |||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 97.31 E-value: 4.00e-25
|
|||||||
TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
168-314 | 1.60e-24 | |||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 96.30 E-value: 1.60e-24
|
|||||||
Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
168-308 | 4.58e-24 | |||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 94.93 E-value: 4.58e-24
|
|||||||
AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
168-287 | 8.11e-14 | |||
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: 66.86 E-value: 8.11e-14
|
|||||||
Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
186-286 | 1.36e-12 | |||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 464033 [Multi-domain] Cd Length: 95 Bit Score: 62.71 E-value: 1.36e-12
|
|||||||
Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
168-287 | 1.36e-12 | |||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 64.31 E-value: 1.36e-12
|
|||||||
PRK03147 | PRK03147 | thiol-disulfide oxidoreductase ResA; |
168-287 | 4.20e-10 | |||
thiol-disulfide oxidoreductase ResA; Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 57.71 E-value: 4.20e-10
|
|||||||
TlpA_like_DsbE | cd03010 | TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ... |
168-287 | 3.02e-09 | |||
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c. Pssm-ID: 239308 [Multi-domain] Cd Length: 127 Bit Score: 54.12 E-value: 3.02e-09
|
|||||||
PRX_like1 | cd02969 | Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
168-297 | 1.40e-04 | |||
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs 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. Pssm-ID: 239267 [Multi-domain] Cd Length: 171 Bit Score: 41.84 E-value: 1.40e-04
|
|||||||
TryX_like_TryX_NRX | cd03009 | Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ... |
174-289 | 4.80e-04 | |||
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors. Pssm-ID: 239307 [Multi-domain] Cd Length: 131 Bit Score: 39.58 E-value: 4.80e-04
|
|||||||
PRX_like2 | cd02970 | Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ... |
171-287 | 5.48e-04 | |||
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins. Pssm-ID: 239268 [Multi-domain] Cd Length: 149 Bit Score: 39.65 E-value: 5.48e-04
|
|||||||
TlpA_like_ScsD_MtbDsbE | cd03011 | TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ... |
168-285 | 3.41e-03 | |||
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c. Pssm-ID: 239309 [Multi-domain] Cd Length: 123 Bit Score: 36.89 E-value: 3.41e-03
|
|||||||
Blast search parameters | ||||
|