Protein Family Models

This entry corresponds to the N-terminal alpha helical domain of the HemK protein. HemK is a methyltransferase enzyme that carries out the methylation of the N5 nitrogen of the glutamine found in the conserved GGQ motif of class-1 release factors [3]. [1]. 15223314. Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase. Yang Z, Shipman L, Zhang M, Anton BP, Roberts RJ, Cheng X;. J Mol Biol. 2004;340:695-706. [2]. 16364916. Molecular basis for bacterial class I release factor methylation by PrmC. Graille M, Heurgue-Hamard V, Champ S, Mora L, Scrima N, Ulryck N, van Tilbeurgh H, Buckingham RH;. Mol Cell. 2005;20:917-927. [3]. 12741815. Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase. Schubert HL, Phillips JD, Hill CP;. Biochemistry. 2003;42:5592-5599. [4]. 18247349. A novel mode of dimerization via formation of a glutamate anhydride crosslink in a protein crystal structure. Agarwal R, Burley SK, Swaminathan S;. Proteins. 2008;71:1038-1041. (from Pfam)

Date:

2024-10-16

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

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

Date:

2024-08-14

This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences. [1]. 8226664. Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12. Vanet A, Plumbridge JA, Alix JH;. J Bacteriol 1993;175:7178-7188. (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

Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (Pfam:PF01420), and R [1]. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes. [1]. 9440532. A type IC restriction-modification system in Lactococcus lactis. Schouler C, Clier F, Lerayer AL, Ehrlich SD, Chopin MC;. J Bacteriol 1998;180:407-411. [2]. 9593305. Combinational variation of restriction modification specificities in Lactococcus lactis. Schouler C, Gautier M, Ehrlich SD, Chopin MC;. Mol Microbiol 1998;28:169-178. [3]. 9108149. The specificity of sty SKI, a type I restriction enzyme, implies a structure with rotational symmetry. Thorpe PH, Ternent D, Murray NE;. Nucleic Acids Res 1997;25:1694-1700. (from Pfam)

Date:

2024-10-16