SMART: Pfam domain OAS1

The domain within your query sequence starts at position 169 and ends at position 353; the E-value for the OAS1_C domain shown below is 4.6e-81.

YLYNKIYAQLIHECTTLKKEGEFSICFTDLHQSFLEDRAPKLKNLIRLVKHWYQLCKEKL
GKPLPPQYALELLTVYAWESGSRDCEFNTAQGFRTVLELVTKYKWLRIYWTVYYDFRKTK
VSEYLHKMLQKVRPVILDPADPTRNVAGTNLLGWGLLAKEAAIWLQSSCFRNCDTCLVGP
WGVPM

OAS1_C

PFAM accession number:	PF10421
Interpro abstract (IPR018952):	This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between residues 320 and 344 at the extreme C-terminal end [ (PUBMED:14636576) ]. Oligoadenylate synthetases are antiviral enzymes that counteract viral attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesise 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication [ (PUBMED:1651324) ]. This domain is often associated with IPR002934 .

PFAM accession number:

PF10421

Interpro abstract (IPR018952):

This is the largely alpha-helical, C-terminal half of 2'-5'-oligoadenylate synthetase 1, being described as domain 2 of the enzyme and homologous to a tandem ubiquitin repeat. It carries the region of enzymic activity between residues 320 and 344 at the extreme C-terminal end [ (PUBMED:14636576) ]. Oligoadenylate synthetases are antiviral enzymes that counteract viral attack by degrading viral RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesise 2'.5'-oligoadenylates, which activate latent ribonuclease, resulting in degradation of viral RNA and inhibition of virus replication [ (PUBMED:1651324) ]. This domain is often associated with IPR002934 .

This is a PFAM domain. For full annotation and more information, please see the PFAM entry OAS1_C