SUPERFAMILY 1.73 HMM library and genome assignments server


Nudix superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a+b) [ 53931] (334)
  Mainly antiparallel beta sheets (segregated alpha and beta regions)
Fold:   Nudix [ 55810]
  beta(2)-alpha-beta(3)-alpha; 3 layers: alpha/beta/alpha; mixed sheet
contains beta-grasp motif
Superfamily:   Nudix [ 55811] (7)
Families:   MutT-like [ 55812] (16)
  MutY C-terminal domain-like [ 103211] (2)
  NADH pyrophosphatase [ 103214]
  duplication: consists of two structurally similar domains separated by a rubredoxin-like zinc finger; the N-terminal domain has a rudiment Nudix fold, the C-terminal, probably catalytic, domain has the canonical fold
  IPP isomerase-like [ 64369] (3)
  GDP-mannose mannosyl hydrolase NudD [ 111132]
  BT0354 N-terminal domain-like [ 143772] (2)
  accosiated with the C-terminal "winged helix" domain (scop_sf 46785)
  mRNA decapping enzyme-like [ 143777]
  part of Pfam 00293


Superfamily statistics
Genomes (1,325) UniProt 15.0 PDB chains (SCOP 1.73)
Domains 14,804 13,989 44
Proteins 14,639 13,819 43


Functional annotation
General category Information
Detailed category DNA replication/repair

Function annotation of SCOP domain superfamilies
InterPro annotation
Cross references IPR015797 SSF55811 Protein matches
Abstract MutT is a small bacterial protein (~12-15Kd) involved in the GO system [PubMed1328155] responsible for removing an oxidatively damaged form of guanine (8-hydroxy- guanine or 7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with near equal efficiency, leading to A-T to G-C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate, with the concomitant release of pyrophosphate. A short conserved N-terminal region of mutT (designated the MutT domain) is also found in a variety of other prokaryotic, viral and eukaryotic proteins [PubMed8233837, PubMed8170394, PubMed8226881, PubMed10373642].

The generic name `NUDIX hydrolases' (NUcleoside DIphosphate linked to some other moiety X) has been coined for this domain family [PubMed8810257]. The family can be divided into a number of subgroups, of which MutT anti- mutagenic activity represents only one type; most of the rest hydrolyse diverse nucleoside diphosphate derivatives (including ADP-ribose, GDP- mannose, TDP-glucose, NADH, UDP-sugars, dNTP and NTP).


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

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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 31 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 Nudix 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 31 hidden Markov models representing the Nudix 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 · Internal database links ]