nucleoredoxin-like protein 2 [Rattus norvegicus]
thioredoxin family protein( domain architecture ID 10121823)
thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif; similar to human nucleoredoxin-like protein 2 that may be involved in the maintenance of both the function and the viability of sensory neurons, including photoreceptors and olfactory neurons
List of domain hits
Name | Accession | Description | Interval | E-value | |||
TryX_like_family | cd02964 | Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ... |
10-144 | 6.58e-59 | |||
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: 178.96 E-value: 6.58e-59
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Name | Accession | Description | Interval | E-value | |||
TryX_like_family | cd02964 | Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ... |
10-144 | 6.58e-59 | |||
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: 178.96 E-value: 6.58e-59
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Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
26-124 | 3.02e-36 | |||
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: 120.49 E-value: 3.02e-36
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TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
22-125 | 1.48e-10 | |||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 55.85 E-value: 1.48e-10
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Name | Accession | Description | Interval | E-value | |||
TryX_like_family | cd02964 | Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ... |
10-144 | 6.58e-59 | |||
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: 178.96 E-value: 6.58e-59
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Thioredoxin_8 | pfam13905 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
26-124 | 3.02e-36 | |||
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: 120.49 E-value: 3.02e-36
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TryX_like_RdCVF | cd03008 | Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is ... |
19-144 | 8.40e-32 | |||
Tryparedoxin (TryX)-like family, Rod-derived cone viability factor (RdCVF) subfamily; RdCVF is a thioredoxin (TRX)-like protein specifically expressed in photoreceptors. RdCVF was isolated and identified as a factor that supports cone survival in retinal cultures. Cone photoreceptor loss is responsible for the visual handicap resulting from the inherited disease, retinitis pigmentosa. RdCVF shows 33% similarity to TRX but does not exhibit any detectable thiol oxidoreductase activity. Pssm-ID: 239306 Cd Length: 146 Bit Score: 110.68 E-value: 8.40e-32
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TryX_like_TryX_NRX | cd03009 | Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ... |
23-137 | 3.77e-29 | |||
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: 103.52 E-value: 3.77e-29
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TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
22-125 | 1.48e-10 | |||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 55.85 E-value: 1.48e-10
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TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
22-125 | 4.50e-08 | |||
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: 48.77 E-value: 4.50e-08
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Bcp | COG1225 | Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
22-125 | 5.19e-08 | |||
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 48.71 E-value: 5.19e-08
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Blast search parameters | ||||
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