endoplasmic reticulum resident protein 29 isoform 2 precursor [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
Thioredoxin_like super family | cl00388 | Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ... |
33-50 | 1.72e-03 | ||
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others. The actual alignment was detected with superfamily member pfam07912: Pssm-ID: 469754 Cd Length: 126 Bit Score: 33.28 E-value: 1.72e-03
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Name | Accession | Description | Interval | E-value | ||
ERp29_N | pfam07912 | ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ... |
33-50 | 1.72e-03 | ||
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organized into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI). However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that ERp29's function is similar to the chaperone function of PDI. The N-terminal domain is exclusively responsible for the homodimerization of the protein, without covalent linkages or additional contacts with other domains. Pssm-ID: 400320 Cd Length: 126 Bit Score: 33.28 E-value: 1.72e-03
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Name | Accession | Description | Interval | E-value | ||
ERp29_N | pfam07912 | ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ... |
33-50 | 1.72e-03 | ||
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organized into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI). However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that ERp29's function is similar to the chaperone function of PDI. The N-terminal domain is exclusively responsible for the homodimerization of the protein, without covalent linkages or additional contacts with other domains. Pssm-ID: 400320 Cd Length: 126 Bit Score: 33.28 E-value: 1.72e-03
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Blast search parameters | ||||
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