SUPERFAMILY 1.75 HMM library and genome assignments server

Gurmarin-like superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Small proteins [ 56992] (90)
Fold:   Knottins (small inhibitors, toxins, lectins) [ 57015] (19)
Superfamily:   Gurmarin-like [ 57048] (2)
Families:   Gurmarin, a sweet taste-suppressing polypeptide [ 57049]
  Antifungal peptide [ 57052] (2)

Superfamily statistics
Genomes (21) Uniprot 2014_06 PDB chains (SCOP 1.75)
Domains 29 41 3
Proteins 29 40 3

Functional annotation
General category Other
Detailed category Unknown function

Function annotation of SCOP domain superfamilies

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Cellular componentSecreted4.827e-11Moderately InformativeDirect
DomainKnottin0Highly InformativeDirect
Post-translational modificationAntimicrobial0InformativeDirect
Post-translational modificationDisulfide bond0Least InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR009101 SSF57048 Protein matches

Gurmarin is a sweet taste-suppressing polypeptide from the Indian-originated tree Gymnema sylvestre. Gurmarin acts to selectively inhibit the neural response to sweet stimuli in rats. The crystal structure of Gumarin reveals a disulphide-bound fold containing an antiparallel beta-hairpin [PubMed10491100]. The aromatic residues that form a hydrophobic cluster in gurmarin are thought to be a possible functional site for the interaction of gurmarin with the taste receptors [PubMed11697741].

Gurmarin is structurally related to the antifungal peptide PAFP-S from the seeds of the pokeweed Phytolacca americana, and to the antifungal peptide Alo3 from the insect Acrocinus longimanus. PAFP-S exhibits a broad spectrum of antifungal activity, including inhibition of saprophytic fungi and some plant pathogens. The amphiphilic surfaces of PAFP-S is thought to be the main functional site for interacts with biomembranes [PubMed11551192]. Insect peptides are key elements of innate immunity against bacteria and fungi. Alo-1, Alo-2 and Alo-3 show high sequence identity, and are active against Candida species [PubMed14661954].

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 3 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 Gurmarin-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 3 hidden Markov models representing the Gurmarin-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 · UniProtKB KeyWords (KW) · Internal database links ]