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Table of Pairwise Domain-Domain Interactions for the domain:
FKBP_C

Interacting Domains ↕CD ↕ Accession (External Link)Description ↕
Rapamycin_bindpfam08771Rapamycin binding domain. This domain forms an alpha helical structure and binds to rapamycin.
TGF_beta_GSpfam08515Transforming growth factor beta type I GS-motif. This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor.
TPR_1pfam00515Tetratricopeptide repeat.
efhandpfam00036EF hand. The EF-hands can be divided into two classes: signaling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Metallophospfam00149Calcineurin-like phosphoesterase. This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.



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