Protein Family Models

HD domains are metal dependent phosphohydrolases [1,2]. This entry covers the HD-GYP domain [2]. [1]. 9868367. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Aravind L, Koonin EV;. Trends Biochem Sci 1998;23:469-472. [2]. 34928179. Sequence Conservation, Domain Architectures, and Phylogenetic Distribution of the HD-GYP Type c-di-GMP Phosphodiesterases. Galperin MY, Chou SH;. J Bacteriol. 2021; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

HD domains are metal dependent phosphohydrolases. [1]. 9868367. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Aravind L, Koonin EV;. Trends Biochem Sci 1998;23:469-472. (from Pfam)

Date:

2024-10-16

HD-GYP domain-containing protein functions as a cyclic nucleotide phosphodiesterase, such as Borreliella burgdorferi cyclic di-GMP phosphodiesterase PdeB that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP

Date:

2024-07-10

This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. For proteins scoring above the trusted cutoff, confidence is high both that the domain is present and that the HMM produces an essentially correct alignment. Protein regions scoring between the trusted and noise cutoffs include correctly aligned domains, homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits indications of homology.

Date:

2024-01-02