6F5Z

Complex between the Haloferax volcanii Trm112 methyltransferase activator and the Hvo_0019 putative methyltransferase


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF08241e6f5zA1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF08241ECOD (1.6)
BPF08241e6f5zB1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF08241ECOD (1.6)
CPF03966e6f5zC1 A: few secondary structure elementsX: Trm112p-like (From Topology)H: Trm112p-like (From Topology)T: Trm112p-likeF: PF03966ECOD (1.6)
DPF03966e6f5zD1 A: few secondary structure elementsX: Trm112p-like (From Topology)H: Trm112p-like (From Topology)T: Trm112p-likeF: PF03966ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF08241Methyltransferase domain (Methyltransf_11)Methyltransferase domainMembers of this family are SAM dependent methyltransferases.Domain
C, D
PF03966Trm112p-like protein (Trm112p)Trm112p-like proteinThe function of this family is uncertain. The bacterial members are about 60-70 amino acids in length and the eukaryotic examples are about 120 amino acids in length. The C terminus contains the strongest conservation. Trm112p is required for tRNA ...The function of this family is uncertain. The bacterial members are about 60-70 amino acids in length and the eukaryotic examples are about 120 amino acids in length. The C terminus contains the strongest conservation. Trm112p is required for tRNA methylation in S. cerevisiae and is found in complexes with 2 tRNA methylases (TRM9 and TRM11) also with putative methyltransferase YDR140W [1]. The zinc-finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast [2]. The crystal structure of Ynr046w has been determined to 1.7 A resolution. It comprises a zinc-binding domain built from both the N- and C-terminal sequences and an inserted domain, absent from bacterial and archaeal orthologs of the protein, composed of three alpha-helices [2].
Domain

InterPro: Protein Family Classification InterPro Database Homepage