Protein Family Models for Protein (Select 487654699) - Protein Family Models

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Links from Protein

Items: 8

Select item 4230061.

thioredoxin fold domain-containing protein

Date:: 2024-08-14

Family Accession:: NF024498.5
Method:: HMM

Select item 4205072.

disulfide isomerase DsbC N-terminal domain-containing protein

This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of the V, so are vital for dimerisation [1]. DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein-folding in bacterial periplasm. It also has chaperone activity [2]. [1]. 10700276. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P;. Nat Struct Biol. 2000;7:196-199. [2]. 16087673. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. Hiniker A, Collet JF, Bardwell JC;. J Biol Chem. 2005;280:33785-33791. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF021896.5
Method:: HMM

Select item 3986473.

new record, indexing in progress

Family Accession:

Select item 3977494.

new record, indexing in progress

Family Accession:

Select item 3561435.

new record, indexing in progress

Family Accession:

Select item 3555966.

new record, indexing in progress

Family Accession:

Select item 2156327.

bifunctional protein-disulfide isomerase/oxidoreductase DsbC

bifunctional protein-disulfide isomerase/oxidoreductase DsbC is required for disulfide bond formation in some periplasmic proteins; also acts as a disulfide isomerase