| Description | Nuclear protein AMMECR1, presently a protein of unknown function, is encoded by one of the genes affected by an X-linked deletion that causes the association of Alport syndrome, midface hypoplasia, intellectual disability and elliptocytosis in humans [ ].This entry represents the C-terminal region of AMMECR1 (approximately from residue 122 to 333), which is well conserved. Homologues appear in species ranging from bacteria and archaea to eukaryotes, including Protein PH0010 from Pyrococcus horikoshii [ ]. The high level of conservation of the AMMECR1 domain points to a basic cellular function, potentially in either the transcription, replication, repair or translation machinery [, ]. The AMMECR1 domain, which contains a 6-amino-acid motif (LRGCIG) that might be functionally important since it is strikingly conserved throughout evolution []. The AMMECR1 domain consists of two distinct subdomains of different sizes. The large subdomain, which contains both the N- and C-terminal regions, consists of five α-helices and five β-strands. These five β-strands form an antiparallel β-sheet. The small subdomain consists of four α-helices and three β-strands, and these β-strands also form an antiparallel β-sheet. The conserved 'LRGCIG' motif is located at β(2) and its N-terminal loop, and most of the side chains of these residues point toward the interface of the two subdomains. The two subdomains are connected by only two loops, and the interaction between the two subdomains is not strong. Thus, these subdomains may move dynamically when the substrate enters the cleft. The size of the cleft suggests that the substrate is large, e.g., the substrate may be a nucleic acid or protein. However, the inner side of the cleft is not filled with positively charged residues, and therefore it is unlikely that negatively charged nucleic acids such as DNA or RNA interact at this site []. | Name | AMMECR1 domain |
| Short Name | AMMECR1_domain | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
