6ZXW

Structure of Archaeoglobus fulgidus Trm11-Trm112 m2G10 tRNA methyltransferase complex bound to sinefungin


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth G]F_UNCLASSIFIEDe6zxwG1 A: a+b two layersX: Alpha-beta plaitsH: Ferredoxin-like domain in ThiI (From Topology)T: Ferredoxin-like domain in ThiIF: F_UNCLASSIFIEDECOD (1.6)
A [auth G]F_UNCLASSIFIEDe6zxwG2 A: a+b two layersX: THUMP domain-like (From Topology)H: THUMP domain-like (From Topology)T: THUMP domain-likeF: F_UNCLASSIFIEDECOD (1.6)
A [auth G]PF01170e6zxwG3 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF01170ECOD (1.6)
B [auth H]PF03966e6zxwH1 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 [auth G]PF01170Putative RNA methylase family UPF0020 (UPF0020)Putative RNA methylase family UPF0020This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains [1].Domain
A [auth G]PF02926THUMP domain (THUMP)THUMP domainThe THUMP domain is named after after thiouridine synthases, methylases and PSUSs [1]. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-bi ...The THUMP domain is named after after thiouridine synthases, methylases and PSUSs [1]. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains [2]. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets [1].
Domain
B [auth H]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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth G]tRNA (Guanine(10)-N2)-dimethyltransferase
B [auth H]Uncharacterized protein- - -