Protein Family Models

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

Date:

2024-08-14

The DinB family are an uncharacterised family of potential enzymes. The structure of these proteins is composed of a four helix bundle [1]. [1]. 20208147. The structure of DinB from Geobacillus stearothermophilus: a representative of a unique four-helix-bundle superfamily. Cooper DR, Grelewska K, Kim CY, Joachimiak A, Derewenda ZS;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010;66:219-224. (from Pfam)

Date:

2024-10-16

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 domain is found in eukaryotic proteins [1] required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD) [2]. The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases [3]. FGE is localised to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesised sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilised by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidised cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases [4]. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase [5,6]. [1]. 14563551. The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes. Landgrebe J, Dierks T, Schmidt B, von Figura K;. Gene 2003;316:47-56. [2]. 15146462. Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency. Cosma MP, Pepe S, Parenti G, Settembre C,. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

bifunctional 5-histidylcysteine sulfoxide synthase/4-mercaptohistidine N1-methyltransferase functions in ovothiol biosynthesis

Date:

2020-09-23

Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes the 5-histidylcysteine sulfoxide synthase domain, a homolog of the ergothioneine biosynthesis protein EgtB.

Gene:

ovoA

Date:

2019-09-10

Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain.

Date:

2021-04-27