Protein Family Models

Pair of presumed choline-binding repeats often found adjacent to Pfam:PF01473. (from Pfam)

Date:

2024-08-14

This family of uncharacterised archaeal proteins are related to Transglutaminase-like domains. This family has previously been called DUF553 and UPF0252. (from Pfam)

Date:

2024-08-14

This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterised transglutaminase, the human blood clotting factor XIIIa' [1]. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase [2], it is proposed that many, if not all, microbial homologues of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease. [3] [1]. 7913750. Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC;. Proc Natl Acad Sci USA 1994;91:7296-7300. [2]. 9791169. Molecular analysis of Methanobacterium phage psiM2. Pfister P, Wasserfallen A, Stettler R, Leisinger T;. Mol Microbiol 1998;30:233-244. [3]. 10452618. A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases [In Process Citation]. Makarova KS, Aravind L, Koonin EV;. Protein Sci 1999;8:1714-1719. (from Pfam)

Date:

2024-10-16

These repeats are characterised by conserved aromatic residues and glycines are found in multiple tandem copies in a number of proteins. The CW repeat is 20 amino acid residues long. The exact domain boundaries may not be correct. It has been suggested that these repeats in Swiss:P15057 might be responsible for the specific recognition of choline-containing cell walls [1]. Similar but longer repeats are found in the glucosyltransferases and glucan-binding proteins of oral streptococci and shown to be involved in glucan binding [2] as well as in the related dextransucrases of Leuconostoc mesenteroides. Repeats also occur in toxins of Clostridium difficile and other clostridia, though the ligands are not always known. [1]. 3422470. Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Garcia E, Garcia JL, Garcia P, Arraras A, Sanchez-Puelles JM, Lopez R;. Proc Natl Acad Sci U S A 1988;85:914-918. [2]. 14527392. Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M;. Structure (Camb) 2003;11:1239-1249. [3]. 7860591. Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene. Sanchez-Beato AR, Ronda C, Garcia JL;. J Bacteriol 1995;177:1098-1103. [4]. 1830357. A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Wren BW;. Mol Microbiol 1991;5:797-803. [5]. 2307516. Sequence analysis of the gene. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16