EC Number   |
General Information |
Reference |
|---|
   3.4.21.B56 | more |
C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin |
731822 |
| 3.4.21.B56 | more |
the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138). The hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and oligonucleotide binding-fold domains, molecular modeling of hexameric oligonucleotide binding domains of enzyme 1510-C, domain structure, overview. Conserved residues at the domain surface may play key roles in maintaining protein-protein interactions of enzyme and substrate |
731379 |
| 3.4.21.B56 | more |
the N-terminal region of PH1510p is a serine protease with a catalytic Ser-Lys dyad, Ser97 and Lys138 |
731295 |
| 3.4.21.B56 | physiological function |
the enzyme may be involved in the quality control of membrane proteins, e.g. stomatin, prohibitin, flotillin, and HflK/C domain proteins found in the lipid raft microdomains of various cellular membranes |
731822 |
