cd16576: RING-HC_TRIM9_like_C-I (this model, PSSM-Id:319490 is obsolete and has been replaced by 438238)
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM36, TRIM46, TRIM67, and similar proteins
Tripartite motif-containing proteins TRIM9, TRIM36, TRIM46, and TRIM67 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. TRIM36 (the human ortholog of mouse Haprin), also known as RING finger protein 98 (RNF98), or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in the carcinogenesis. TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that forms parallel microtubule bundles in the proximal axon and plays a crucial role for the establishment and maintenance of neuronal polarity. TRIM67, also known as TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H, also known as glucosidase II beta, a protein kinase C substrate.
Jiyao W et al.(2023). "The conserved domain database in 2023.",