ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins
TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes.
Feature 1: key conserved lysine K27, 1 residue position
Conserved feature residue pattern:[KR]
Evidence:
Comment:K27/R (Ub numbering) is a lysine conserved in the Ubl_ubiquitin_like family; it is one of 7 lysines involved in chain linkage in ubiquitin (K6, K11, K27, K29, K33, K48, or K63, Ub numbering), the other 6 lysines are not conserved in this family, for most the residue corresponding to K29 is a conserved Leu, and the residue corresponding to K33 a conserved Asp; may have other functions, for example in NEDD8 K27 is involved in the mechanism of protein neddylation
Jiyao W et al.(2023). "The conserved domain database in 2023.",