Protein Family Models for Protein (Select 550733447) - Protein Family Models

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Items: 5

Select item 4118741.

Hsp70 family protein

Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region. [1]. 9476895. The Hsp70 and Hsp60 chaperone machines. Bukau B, Horwich AL;. Cell 1998;92:351-366. (from Pfam)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Molecular Function:: ATP-dependent protein folding chaperone (GO:0140662)

Date:: 2024-10-16

Family Accession:: NF012242.5
Method:: HMM

Select item 3886702.

new record, indexing in progress

Family Accession:

Select item 3468443.

new record, indexing in progress

Family Accession:

Select item 1788024.

molecular chaperone

Gene:: yegD

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Molecular Function:: ATP hydrolysis activity (GO:0016887)

Date:: 2021-08-24

Family Accession:: NF008673.0
Method:: HMM

Select item 597115.

Hsp70 family protein

uncharacterized heat shock protein 70 family protein similar to Escherichia coli YegD; may be a molecular chaperone and assist in protein folding and assembly and/or a nucleotide exchange factor which removes ADP from its Hsp70 chaperone partner