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FMT C-terminal domain-like superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   FMT C-terminal domain-like [ 50485]
Superfamily:   FMT C-terminal domain-like [ 50486] (2)
Families:   Post formyltransferase domain [ 50487] (3)
  3-methyladenine DNA glycosylase (AAG, ANPG, MPG) [ 50490]


Superfamily statistics
Genomes (2,846) Uniprot 2017_06 genome PDB chains (SCOP 1.75)
Domains 4,883 28,867 10
Proteins 4,874 28,822 10


Functional annotation
General category Metabolism
Detailed category Other enzymes

Document:
Function annotation of SCOP domain superfamilies

Gene Ontology (high-coverage)

(show details)
GO term FDR (all) SDFO level Annotation (direct or inherited)
Biological Process (BP) cellular nitrogen compound metabolic process 0.000000008131 Least Informative Direct
Biological Process (BP) single-organism metabolic process 0.2245 Least Informative Inherited
Biological Process (BP) single-organism cellular process 0.8694 Least Informative Inherited
Biological Process (BP) organonitrogen compound metabolic process 0.219 Least Informative Inherited
Biological Process (BP) peptide metabolic process 0.0004094 Moderately Informative Direct
Molecular Function (MF) transferase activity 0.2139 Least Informative Inherited
Molecular Function (MF) transferase activity, transferring one-carbon groups 0.00000000003321 Informative Direct
Molecular Function (MF) hydroxymethyl-, formyl- and related transferase activity 0 Highly Informative Direct

Document: GO annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Transferring one-carbon groups0Least InformativeDirect
Enzyme Commission (EC)Oxidoreductases1Least InformativeInherited
Enzyme Commission (EC)With NAD(+) or NADP(+) as acceptor0.00000000113Moderately InformativeDirect
Enzyme Commission (EC)Acting on the CH-NH group of donors0.05243Moderately InformativeInherited
Enzyme Commission (EC)Hydroxymethyl-, formyl- and related transferases0InformativeDirect
Enzyme Commission (EC)Hydrolyzing N-glycosyl compounds0.2272InformativeInherited
Enzyme Commission (EC)With NAD(+) or NADP(+) as acceptor0.02932InformativeInherited
Enzyme Commission (EC)UDP-4-amino-4-deoxy-L-arabinose formyltransferase0Highly InformativeDirect
Enzyme Commission (EC)Formyltetrahydrofolate dehydrogenase0Highly InformativeDirect

Document: EC annotation of SCOP domains

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processDNA damage0Moderately InformativeDirect
Biological processLipid metabolism0.00005821Moderately InformativeDirect
Biological processLipid biosynthesis0InformativeDirect
Biological processProtein biosynthesis0InformativeDirect
Biological processDNA repair0InformativeDirect
Biological processAntibiotic resistance0InformativeDirect
Biological processLipopolysaccharide biosynthesis0Highly InformativeDirect
Biological processLipid A biosynthesis0Highly InformativeDirect
Molecular functionNAD0.000006236Moderately InformativeDirect
Post-translational modificationTransferase0Least InformativeDirect
Post-translational modificationPhosphopantetheine0.000159Highly InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR011034 SSF50486 Protein matches
Abstract

Methionyl-tRNA formyltransferase (FMT) transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. This family also includes formyltetrahydrofolate dehydrogenases, which produce formate from formyl-tetrahydrofolate. These enzymes contain an N-terminal domain in common with other formyl transferase enzymes . The C-terminal domain has an open beta-barrel fold [PubMed8887566].

The C-terminal domain of FMT structurally resembles methylpurine-DNA glycosylases (MPG). Human 3-methyladenine DNA glycosylase (AAG) catalyses the first step of base excision repair by cleaving damaged bases from DNA, excising a chemically diverse selection of substrate bases damaged by alkylation or deamination [PubMed11106395].


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Gene Ontology (high-coverage) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 6 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a FMT C-terminal domain-like domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 6 hidden Markov models representing the FMT C-terminal domain-like superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Gene Ontology (high-coverage) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) · Internal database links ]