YgfZ/GcvT domain-containing protein with similarity to Escherichia coli tRNA-modifying protein YgfZ and GcvT family member, mitochondrial putative transferase CAF17
folate-binding protein YgfZ; YgfZ is a protein from Escherichia coli, homologous to the ...
218-285
1.84e-27
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. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274518 [Multi-domain] Cd Length: 67 Bit Score: 102.62 E-value: 1.84e-27
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, ...
59-163
7.72e-05
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 catalyzes the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.
Pssm-ID: 460255 Cd Length: 254 Bit Score: 43.73 E-value: 7.72e-05
folate-binding protein YgfZ; YgfZ is a protein from Escherichia coli, homologous to the ...
218-285
1.84e-27
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. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274518 [Multi-domain] Cd Length: 67 Bit Score: 102.62 E-value: 1.84e-27
Glycine cleavage system protein T (aminomethyltransferase) [Amino acid transport and ...
59-327
1.06e-05
Glycine cleavage system protein T (aminomethyltransferase) [Amino acid transport and metabolism]; Glycine cleavage system protein T (aminomethyltransferase) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440173 [Multi-domain] Cd Length: 372 Bit Score: 47.00 E-value: 1.06e-05
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, ...
59-163
7.72e-05
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 catalyzes the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.
Pssm-ID: 460255 Cd Length: 254 Bit Score: 43.73 E-value: 7.72e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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