|
|
Fe,Mn superoxide dismutase (SOD), C-terminal domain superfamily
SCOP classification
Superfamily statistics
Functional annotation
| General category | Metabolism |
| Detailed category | Redox |
Document: Function annotation of SCOP domain superfamilies
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
Yeast Phenotype (YP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: YP annotation of SCOP domains
Arabidopsis Plant Ontology (AP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: AP annotation of SCOP domains
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
InterPro annotation
| Cross references | IPR001189 SSF54719 Protein matches |
| Abstract | Superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to molecular oxygen. Their function is to destroy the radicals that are normally produced within cells and are toxic to biological systems. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one [ 3315461, 3345848, 1556751]. This family includes both single metal-binding SODs and cambialistic SOD, which can bind either Mn or Fe. Fe/MnSODs are ubiquitous enzymes that are responsible for the majority of SOD activity in prokaryotes, fungi, blue-green algae and mitochondria. Fe/MnSODs are found as homodimers or homotetramers.
The structure of Fe/MnSODs can be divided into two domains, an alpha N-terminal domain and an alpha/beta C-terminal domain, connected by a loop. The structure of the N-terminal domain consists of a two helices in an antiparallel hairpin, with a left-handed twist [9537987]. The structure of the C-terminal domain is of the alpha/beta type, and consists of a three-stranded antiparallel beta-sheet in the order 213, along with four helices in the arrangement alpha/beta(2)/alpha/beta/alpha(2) [9931259].
|
InterPro database
PDBeMotif information about ligands, sequence and structure motifs
PDBeMotif resource
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Yeast Phenotype (YP) · Arabidopsis Plant Ontology (AP) · 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 51 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 Fe,Mn superoxide dismutase (SOD), C-terminal domain 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 51 hidden Markov models representing the Fe,Mn superoxide dismutase (SOD), C-terminal domain 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) · Yeast Phenotype (YP) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) · Internal database links ]
|
0
