Protein Family Models

Date:

2024-08-14

This is a small domain that is found C terminal to Pfam:PF00501. It has a central beta sheet core that is flanked by alpha helices. (from Pfam)

Date:

2024-11-05

This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included. [1]. 9351246. The Arabidopsis MALE STERILITY 2 protein shares similarity with reductases in elongation/condensation complexes. Aarts MG, Hodge R, Kalantidis K, Florack D, Wilson ZA, Mulligan BJ, Stiekema WJ, Scott R, Pereira A;. Plant J 1997;12:615-623. (from Pfam)

Date:

2024-10-16

This family of proteins utilise NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions. [1]. 9174344. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM;. Biochemistry 1997;36:6294-6304. (from Pfam)

Date:

2024-10-16

A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. (from Pfam)

Date:

2024-08-14

This domain is found in many multi-domain enzymes which synthesise peptide antibiotics. This domain catalyses a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (Pfam:PF00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site [1]. [1]. 9712910. Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain. Stachelhaus T, Mootz HD, Bergendahl V, Marahiel MA;. J Biol Chem 1998;273:22773-22781. (from Pfam)

Date:

2024-10-16

The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyses the oxidation and isomerisation of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones. [1]. 1562516. Structure and tissue-specific expression of 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase genes in human and rat classical and peripheral steroidogenic tissues. Labrie F, Simard J, Luu-The V, Pelletier G, Belanger A, Lachance Y, Zhao HF, Labrie C, Breton N, de Launoit Y, et al. J Steroid Biochem Mol Biol 1992;41:421-435. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14