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FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All alpha proteins [ 46456] (284)
Fold:   Four-helical up-and-down bundle [ 47161] (28)
Superfamily:   FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) [ 47212]
Families:   FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) [ 47213]


Superfamily statistics
Genomes (458) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 617 1,911 3
Proteins 615 1,906 3


Functional annotation
General category General
Detailed category Small molecule binding

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Protein-serine/threonine kinases0.00000007787Moderately InformativeDirect

Document: EC annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Transferring phosphorus-containing groups0Least InformativeDirect
Enzyme Commission (EC)Protein-serine/threonine kinases0Moderately InformativeDirect
Enzyme Commission (EC)Non-specific serine/threonine protein kinase0InformativeDirect

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR009076 SSF47212 Protein matches
Abstract

Rapamycin and FK506 are potent immunosuppressive agents that bind to the FK506-binding protein (FKBP12), inhibiting its peptidyl-prolyl isomerase activity. The rapamycin-FKBP12 complex can then bind to and inhibit the FKBP12-rapamycin-associated protein (FRAP) in humans and RAFT1 in rats, causing cell-cycle arrest [PubMed10089303]. The FK506-FKBP12 complex cannot bind FRAP, but can bind to and inhibit calcineurin. Rapamycin is able to bind to two proteins, FKBP12 and FRAP, by simultaneously occupying two hydrophobic binding pockets, thereby linking these two proteins together to form a dimer [PubMed8662507]. The structure of the FKBP12-rapamycin-binding domain of FRAP consists of a core bundle of four helices arranged up-and-down in a left-handed twist.

FRAP has been shown to interact in vitro with CLIP-170, a protein involved in microtubule organisation and function [PubMed12231510]. FRAP is thought to act as a kinase to phosphorylate CLIP-170, thereby regulating its binding to microtubules. FRAP is also thought to cooperate with p85/p110 phosphatidylinositol 3-kinase (PI3K) to induce the activation of the serine/threonine kinase p70 S6 kinase (p70S6K), which in turn phosphorylates the 40S ribosomal protein S6, thereby altering the translation of ribosomal proteins and translation elongation factors [PubMed11684675].


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 1 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 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) 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 1 hidden Markov models representing the FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) 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) · Enzyme Commission (EC) · Internal database links ]