Protein Family Models

This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling [1]. This family includes: AP endonuclease proteins EC:4.2.99.18 e.g Swiss:P27695, DNase I proteins EC:3.1.21.1 e.g. Swiss:P24855, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56 Swiss:O43426, Sphingomyelinase EC:3.1.4.12 Swiss:P11889 and Nocturnin Swiss:O35710. [1]. 10838565. Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases. Dlakic M;. Trends Biochem Sci 2000;25:272-273. [2]. 7885481. Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Mol CD, Kuo CF, Thayer MM, Cunningham RP, Tainer JA;. Nature 1995;374:381-386. [3]. 1748997. DNase I-induced DNA conformation. 2 A structure of a DNase I-octamer complex. Lahm A, Suck D;. J Mol Biol 1991;222:645-667. (from Pfam)

Date:

2024-10-16

The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies [1]. [1]. 15611647. Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. Mans BJ, Anantharaman V, Aravind L, Koonin EV;. Cell Cycle. 2004;3:1612-1637. (from Pfam)

Date:

2024-10-16

Date:

2020-10-26

This homology domain, GlyGly-CTERM, shares a species distribution with rhombosortase (TIGR03902), a subfamily of rhomboid-like intramembrane serine proteases. It is recognized, and cleaved, by rhombosortase. Shewanella species have the largest number of target proteins per genome, up to thirteen. The domain occurs at the extreme carboxyl-terminus of a diverse set of proteins, most of which are enzymes with conventional signal sequences and with hydrolytic activities: nucleases, proteases, agarases, etc. The agarase AgaA from Vibro sp. strain JT0107 is secreted into the medium, while the same protein heterologously expressed in E. coli is retained in the cell fraction. VesB, from Vibrio cholerae, was shown to be processed by rhombosortase so as to expose the second Gly of the motif, and then to be linked to a glycerophosphoethanolamine, prior to type II secretion. Note that both the processing, and the chemical structure of the domain (motif, hydrophobic predicted transmembrane helix, cluster of basic residues), closely parallels those of the LPXTG/sortase system, the PGF-CTERM/archaseosortase system, and the PEP-CTERM/exosortase(EpsH) system.

Date:

2023-07-12