Protein Family Models

This entry represents a subclade of DUF488 domains lacking the catalytic residues common to the rhodanese-phosphatase superfamily. The C-terminal core strand is degenerate in this subclade [1]. [1]. 36968430. New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts. Burroughs AM, Aravind L;. NAR Genom Bioinform. 2023;5:lqad029. (from Pfam)

Date:

2024-10-16

This entry represents a subclade of DUF488 domains with degenerate C-terminal core strand. Sometimes it is observed adjacent to the DUF488-s subclade, suggesting it preserves a catalytic activity comparable to other active DUF488 subclades [1]. [1]. 36968430. New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts. Burroughs AM, Aravind L;. NAR Genom Bioinform. 2023;5:lqad029. (from Pfam)

Date:

2024-10-16

This entry has been described to include subclades of DUF488 domains (namely DUF488-s, for DUF488-short subclade, DUF488-l for long subclade and DUF488-u for DUF488-standalone subclade) which all which contain the ancestral core of the domain. DUF488-s commonly pairs with the DUF488-l subclade on the genome. In the case of DUF488-l and DUF488-u, the core domain is followed by a single beta-strand that stacks at the C-terminus of the core beta-sheet and a multi-helical 'cap' [1]. Unlike the DUF488-s and DUF488-l subclades, DUF488-u is not found adjacent to other DUF488 subclades on the genome [1]. [1]. 36968430. New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts. Burroughs AM, Aravind L;. NAR Genom Bioinform. 2023;5:lqad029. (from Pfam)

Date:

2024-10-16

DUF488 domain-containing protein similar to Escherichia coli protein YeaO

Date:

2024-09-19