ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) and similar proteins
RB1CC1, also termed FAK family kinase-interacting protein of 200 kDa (FIP200), is the mammalian counterpart of the yeast Atg17 gene and functions as a component of the ULK1/Atg13/RB1CC1/Atg101 complex essential for induction of autophagy. RB1CC1 is a key signaling node to regulate cellular proliferation and differentiation. As a DNA-binding transcription factor, RB1CC1 has been implicated in the regulation of retinoblastoma 1 (RB1) expression. RB1CC1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, as well as a nuclear localization signal (KPRK), a leucine zipper motif and a coiled-coil structure.
Feature 1: key conserved lysine K27, 1 residue position
Conserved feature residue pattern:[KR]
Evidence:
Comment:K27 (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 K6 is a conserved Phe, the residue corresponding to K48 is a Gly, and the residue corresponding to K63 is an Asp/Glu; 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.",