MULTISPECIES: thiol:disulfide interchange protein [Myxococcus]
Protein Classification
TlpA family protein disulfide reductase( domain architecture ID 10001660)
TlpA family protein disulfide reductase 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, and similar to ResA and DsbE, which are essential proteins in cytochrome c maturation
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
36-171 | 2.97e-53 | |||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 166.02 E-value: 2.97e-53
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| Name | Accession | Description | Interval | E-value | ||||
| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
36-171 | 2.97e-53 | ||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 166.02 E-value: 2.97e-53
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| TlpA_like_DsbE | cd03010 | TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ... |
39-165 | 9.48e-49 | ||||
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: 154.27 E-value: 9.48e-49
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| dsbE | TIGR00385 | periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ... |
10-168 | 9.60e-39 | ||||
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization] Pssm-ID: 129481 [Multi-domain] Cd Length: 173 Bit Score: 130.28 E-value: 9.60e-39
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| PRK15412 | PRK15412 | thiol:disulfide interchange protein DsbE; Provisional |
10-171 | 1.11e-29 | ||||
thiol:disulfide interchange protein DsbE; Provisional Pssm-ID: 185310 [Multi-domain] Cd Length: 185 Bit Score: 107.77 E-value: 1.11e-29
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| AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
38-152 | 1.53e-26 | ||||
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: 97.68 E-value: 1.53e-26
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| Name | Accession | Description | Interval | E-value | ||||
| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
36-171 | 2.97e-53 | ||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 166.02 E-value: 2.97e-53
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| TlpA_like_DsbE | cd03010 | TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ... |
39-165 | 9.48e-49 | ||||
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: 154.27 E-value: 9.48e-49
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| TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
43-157 | 2.13e-46 | ||||
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: 148.15 E-value: 2.13e-46
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| Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
41-161 | 5.88e-41 | ||||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 134.61 E-value: 5.88e-41
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| dsbE | TIGR00385 | periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ... |
10-168 | 9.60e-39 | ||||
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization] Pssm-ID: 129481 [Multi-domain] Cd Length: 173 Bit Score: 130.28 E-value: 9.60e-39
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| PRK15412 | PRK15412 | thiol:disulfide interchange protein DsbE; Provisional |
10-171 | 1.11e-29 | ||||
thiol:disulfide interchange protein DsbE; Provisional Pssm-ID: 185310 [Multi-domain] Cd Length: 185 Bit Score: 107.77 E-value: 1.11e-29
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| PRK03147 | PRK03147 | thiol-disulfide oxidoreductase ResA; |
12-157 | 5.24e-28 | ||||
thiol-disulfide oxidoreductase ResA; Pssm-ID: 179545 [Multi-domain] Cd Length: 173 Bit Score: 102.77 E-value: 5.24e-28
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| AhpC-TSA | pfam00578 | AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
38-152 | 1.53e-26 | ||||
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: 97.68 E-value: 1.53e-26
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| TlpA_like_ScsD_MtbDsbE | cd03011 | TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ... |
42-150 | 1.74e-22 | ||||
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: 86.97 E-value: 1.74e-22
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| Redoxin | pfam08534 | Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. |
36-165 | 2.54e-22 | ||||
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins. Pssm-ID: 400717 [Multi-domain] Cd Length: 148 Bit Score: 87.43 E-value: 2.54e-22
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| CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
62-171 | 4.61e-17 | ||||
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442352 [Multi-domain] Cd Length: 105 Bit Score: 72.54 E-value: 4.61e-17
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| TlpA_like_DipZ_like | cd03012 | TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ... |
42-157 | 1.57e-15 | ||||
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3. Pssm-ID: 239310 [Multi-domain] Cd Length: 126 Bit Score: 69.26 E-value: 1.57e-15
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| thioredoxin | TIGR01068 | thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ... |
63-124 | 1.23e-13 | ||||
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport] Pssm-ID: 200072 [Multi-domain] Cd Length: 101 Bit Score: 63.46 E-value: 1.23e-13
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| TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
60-169 | 2.96e-13 | ||||
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins. Pssm-ID: 239245 [Multi-domain] Cd Length: 93 Bit Score: 62.19 E-value: 2.96e-13
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| PRX_like1 | cd02969 | Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ... |
38-160 | 6.89e-13 | ||||
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: 63.41 E-value: 6.89e-13
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| PRX_BCP | cd03017 | Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ... |
39-157 | 1.01e-11 | ||||
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: 59.48 E-value: 1.01e-11
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| TryX_like_TryX_NRX | cd03009 | Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ... |
51-151 | 2.75e-11 | ||||
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: 58.07 E-value: 2.75e-11
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| Thioredoxin | pfam00085 | Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
63-165 | 4.19e-10 | ||||
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise. Pssm-ID: 395038 [Multi-domain] Cd Length: 103 Bit Score: 54.16 E-value: 4.19e-10
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| PRX_AhpE_like | cd03018 | Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ... |
37-159 | 6.67e-10 | ||||
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: 54.97 E-value: 6.67e-10
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| Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
62-151 | 9.09e-09 | ||||
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: 50.38 E-value: 9.09e-09
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| TryX_like_family | cd02964 | Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ... |
49-149 | 1.71e-08 | ||||
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX. Pssm-ID: 239262 [Multi-domain] Cd Length: 132 Bit Score: 50.69 E-value: 1.71e-08
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| PRK10996 | PRK10996 | thioredoxin 2; Provisional |
64-100 | 2.58e-07 | ||||
thioredoxin 2; Provisional Pssm-ID: 182889 [Multi-domain] Cd Length: 139 Bit Score: 47.76 E-value: 2.58e-07
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| Thioredoxin_2 | pfam13098 | Thioredoxin-like domain; |
61-165 | 1.20e-06 | ||||
Thioredoxin-like domain; Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 45.11 E-value: 1.20e-06
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| TxlA | cd02950 | TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ... |
43-173 | 5.26e-06 | ||||
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport. Pssm-ID: 239248 [Multi-domain] Cd Length: 142 Bit Score: 44.25 E-value: 5.26e-06
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| Sco1 | COG1999 | Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
52-171 | 9.66e-06 | ||||
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441602 Cd Length: 156 Bit Score: 43.74 E-value: 9.66e-06
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| DsbD | COG4232 | Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ... |
3-149 | 4.27e-05 | ||||
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443376 [Multi-domain] Cd Length: 416 Bit Score: 42.87 E-value: 4.27e-05
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| trxA | PRK09381 | thioredoxin TrxA; |
66-164 | 5.54e-05 | ||||
thioredoxin TrxA; Pssm-ID: 181812 [Multi-domain] Cd Length: 109 Bit Score: 40.82 E-value: 5.54e-05
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| DsbDgamma | cd02953 | DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ... |
61-156 | 6.59e-05 | ||||
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes. Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 40.28 E-value: 6.59e-05
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| TRX_PICOT | cd02984 | TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ... |
57-100 | 7.23e-05 | ||||
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; 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 contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. 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. Pssm-ID: 239282 [Multi-domain] Cd Length: 97 Bit Score: 39.95 E-value: 7.23e-05
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| PRX_Typ2cys | cd03015 | Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ... |
38-152 | 8.41e-05 | ||||
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: 40.95 E-value: 8.41e-05
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| Thioredoxin_7 | pfam13899 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
50-126 | 2.69e-04 | ||||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 433567 [Multi-domain] Cd Length: 84 Bit Score: 38.11 E-value: 2.69e-04
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| PTZ00051 | PTZ00051 | thioredoxin; Provisional |
65-100 | 7.16e-04 | ||||
thioredoxin; Provisional Pssm-ID: 173347 [Multi-domain] Cd Length: 98 Bit Score: 37.16 E-value: 7.16e-04
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| ybbN | cd02956 | ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ... |
64-97 | 7.45e-04 | ||||
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria. Pssm-ID: 239254 [Multi-domain] Cd Length: 96 Bit Score: 37.25 E-value: 7.45e-04
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| TRX_superfamily | cd01659 | Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ... |
66-152 | 9.37e-04 | ||||
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: 36.52 E-value: 9.37e-04
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| PRX_like2 | cd02970 | Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ... |
40-158 | 1.15e-03 | ||||
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: 37.72 E-value: 1.15e-03
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| PDI_a_ERp38 | cd02998 | PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ... |
53-123 | 1.31e-03 | ||||
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica. Pssm-ID: 239296 [Multi-domain] Cd Length: 105 Bit Score: 36.84 E-value: 1.31e-03
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| tpx | PRK00522 | thiol peroxidase; |
20-68 | 2.75e-03 | ||||
thiol peroxidase; Pssm-ID: 179055 Cd Length: 167 Bit Score: 36.80 E-value: 2.75e-03
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| SCO1-SenC | pfam02630 | SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ... |
51-149 | 5.48e-03 | ||||
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus. Pssm-ID: 460630 Cd Length: 134 Bit Score: 35.62 E-value: 5.48e-03
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