Protein Family Models

This family appears to have methyltransferase activity. (from Pfam)

Date:

2024-08-14

This family appears to be a methyltransferase domain. (from Pfam)

Date:

2024-08-14

This family appears to be a methyltransferase domain. (from Pfam)

Date:

2024-08-14

Members of this family are SAM dependent methyltransferases. (from Pfam)

Date:

2024-08-14

Members of this family are SAM dependent methyltransferases. (from Pfam)

Date:

2024-08-14

This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalysed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganisms the reaction is catalysed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells [1]. [1]. 11479715. The methionine biosynthetic pathway from homoserine in Pseudomonas putida involves the metW, metX, metZ, metH and metE gene products. Alaminos M, Ramos JL;. Arch Microbiol 2001;176:151-154. (from Pfam)

Date:

2024-10-16

This domain is found in ribosomal RNA small subunit methyltransferase C (eg Swiss:P44453) as well as other methyltransferases (eg Swiss:Q53742). (from Pfam)

Date:

2024-08-14

This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyse the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid. [1]. 8917504. A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis. Yuan Y, Barry CE 3rd;. Proc Natl Acad Sci U S A 1996;93:12828-12833. [2]. 7592990. The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2. George KM, Yuan Y, Sherman DR, Barry CE 3d;. J Biol Chem 1995;270:27292-27298. [3]. 10882107. A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis. Glickman MS, Cox JS, Jacobs WR Jr;. Mol Cell. 2000;5:717-727. (from Pfam)

Date:

2024-10-16

This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesised that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping [2]. [1]. 10983982. RNA methylation under heat shock control. Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U;. Mol Cell 2000;6:349-360. [2]. 8385698. Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and lambda 2 protein of reovirus. Koonin EV;. J Gen Virol 1993;74:733-740. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14