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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 2018_03 genome PDB chains (SCOP 1.75)
Domains 4,883 38,165 10
Proteins 4,874 38,112 10


Functional annotation
General category Metabolism
Detailed category Other enzymes

Document:
Function annotation of SCOP domain superfamilies

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

Xenopus Anatomy (XA)

(show details)
XA termFDR (all)SDXA levelAnnotation (direct or inherited)
Xenopus ANatomical entity (XAN)trunk0Least InformativeDirect
Xenopus ANatomical entity (XAN)tissue0Least InformativeDirect
Xenopus ANatomical entity (XAN)cavitated compound organ0Least InformativeDirect
Xenopus ANatomical entity (XAN)musculoskeletal system0Moderately InformativeDirect
Xenopus DEvelopment stage (XDE)post-embryonic stage0Least InformativeDirect
Xenopus DEvelopment stage (XDE)embryonic stage0Moderately InformativeDirect
Xenopus DEvelopment stage (XDE)climax stage0Moderately InformativeDirect
Xenopus DEvelopment stage (XDE)gastrula stage0Highly InformativeDirect

Document: XA annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Oxidoreductases1Least InformativeInherited
Enzyme Commission (EC)Hydrolases1Least InformativeInherited
Enzyme Commission (EC)Transferring one-carbon groups0Moderately InformativeDirect
Enzyme Commission (EC)Acting on the CH-OH group of donors0.0000000005441Moderately InformativeDirect
Enzyme Commission (EC)Glycosylases1Moderately InformativeInherited
Enzyme Commission (EC)Hydroxymethyl-, formyl- and related transferases0InformativeDirect
Enzyme Commission (EC)With NAD(+) or NADP(+) as acceptor0.0000000000226InformativeDirect
Enzyme Commission (EC)Acting on the CH-NH group of donors0.03834InformativeInherited
Enzyme Commission (EC)Hydrolyzing N-glycosyl compounds0.2074InformativeInherited

Document: EC 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 · Enzyme Commission (EC) · Xenopus Anatomy (XA) · Enzyme Commission (EC) ]

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 · Enzyme Commission (EC) · Xenopus Anatomy (XA) · Enzyme Commission (EC) · Internal database links ]