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Items: 7

1.

CheR methyltransferase, all-alpha domain

CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase. [1]. 9115443. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Djordjevic S, Stock AM;. Structure 1997;5:545-558. (from Pfam)

Date:
2024-10-16
Family Accession:
NF015650.5
Method:
HMM
2.

CheR family methyltransferase

CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM. [1]. 9115443. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Djordjevic S, Stock AM;. Structure 1997;5:545-558. (from Pfam)

Date:
2024-10-16
Family Accession:
NF013867.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
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6.
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Family Accession:
7.

CheR family methyltransferase

CheR family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as chemotaxis protein methyltransferase that methylates membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP

Date:
2024-08-27
Family Accession:
11442594
Method:
Sparcle
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