Protein Domain : Non-structural protein NSP15, N-terminal domain superfamily, coronavirus IPR042515

Type  Homologous_superfamily
Description  The unique coronavirus transcription/replication machinery comprised of multiple virus-encoded non structural proteins (NSP) plays a vital role during initial and intermediate phases of the viral life cycle. NSP15 forms a hexamer made of dimers of trimers which is suggested to be a functional unit, responsible for the endoribonuclease activity. The NSP15 monomer consists of three domains: N-terminal, middle and C-terminal [ , ]. The catalytic function of NSP15 resides in the C-terminal NendoU domain. The active site carries six key residues conserved among SARS-CoV-2, SARS-CoV and MERS-CoV, suggesting that its activity is important for sustained replication in the host [, ].This superfamily represents the N-terminal oligomerization domain of NSP15, which is an uridine-specific endonuclease []. This domain stabilises the hexamer and is critical for its formation []. Structurally, this domain consists of 2 small α-helices and 3 β-strands.
Short Name  NSP15_N_CoV

0 Child Features

0 Gene Families

0 Genes

0 Ontology Annotations

0 Parent Features

0 Publications

USDA
InterMine logo
The Legume Information System (LIS) is a research project of the USDA-ARS:Corn Insects and Crop Genetics Research in Ames, IA.
LegumeMine || ArachisMine | CicerMine | GlycineMine | LensMine | LupinusMine | PhaseolusMine | VignaMine | MedicagoMine
InterMine © 2002 - 2022 Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, United Kingdom