SUPERFAMILY 1.75 HMM library and genome assignments server

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Fibre shaft of virus attachment proteins superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   Triple beta-spiral [ 51224]
Superfamily:   Fibre shaft of virus attachment proteins [ 51225] (2)
Families:   Adenovirus [ 51226]
  Reovirus attachment protein sigma 1 [ 69356]

Superfamily statistics
Genomes (6) Uniprot 2014_06 PDB chains (SCOP 1.75)
Domains 16 1,259 4
Proteins 13 748 4

Functional annotation
General category Other
Detailed category Viral proteins

Function annotation of SCOP domain superfamilies

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processHost-virus interaction0Moderately InformativeDirect
Biological processVirus entry into host cell0InformativeDirect
Cellular componentHost nucleus0InformativeDirect
Cellular componentCapsid protein0InformativeDirect
Developmental stageLate protein0Least InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR009013 SSF51225 Protein matches

The attachment proteins in adenoviruses and reoviruses display structural similarity, indicating similar cell-surface receptor binding strategies, even though these viruses differ from one another in design, capsid composition and genome composition [PubMed10553913, PubMed11782420]. The dsDNA adenoviruses are responsible for diseases such as pneumonia, cystitis, conjunctivitis and diarrhoea, all of which can be fatal to patients who are immunocompromised, while the dsRNA reoviruses are responsible for mild respiratory or gastrointestinal infections.

The attachment proteins play a pivotal role in disease patterns through their selective recognition of cell-surface receptors. The fibre protein and the sigma 1 protein act as attachment proteins in adenoviruses and reoviruses, respectively. The attachment proteins are homo-trimeric, and contain a long, thin central shaft, or tail domain, and a C-terminal head domain that plays an important role in cell attachment. The structure of the shaft or tail domain reveals a triple beta-spiral that is formed by interlocking beta-hairpin repeat units.

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 · 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 2 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 Fibre shaft of virus attachment proteins 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 2 hidden Markov models representing the Fibre shaft of virus attachment proteins 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 · UniProtKB KeyWords (KW) · Internal database links ]