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Aminomethyltransferase folate-binding domain
This is a family of glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyses the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase. [1]. 9047339. Cloning, and molecular characterization of the GCV1 gene encoding the glycine cleavage T-protein from Saccharomyces cerevisiae. McNeil JB, Zhang F, Taylor BV, Sinclair DA, Pearlman RE, Bognar AL;. Gene 1997;186:13-20. (from Pfam)
folate-binding protein YgfZ
YgfZ is a protein from Escherichia coli, homologous to the glycine cleavage system T protein, or aminomethyltransferase, GcvT (TIGR00528). Homologs of YgfZ other than members of the GcvT family share a well-conserved signature region that includes the motif, KGCYxGQE. Elsewhere, sequence diverge and length variation are substantial. Members of this family are mostly bacterial, largely absent from the Firmicutes and otherwise usually present. A few eukaryotic examples are found among the Apicomplexa, and a few archaeal sequences are found. Two functions implicated for this folate-binding protein are RNA modification (a function likely to be conserved) and replication initiation (a function likely to be highly variable). Many members of this family are, at the time of construction of this model, misnamed as the glycine cleavage system T protein.
YgfZ/GcvT domain-containing protein
YgfZ/GcvT domain-containing protein with similarity to Escherichia coli tRNA-modifying protein YgfZ and GcvT family member, mitochondrial putative transferase CAF17
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