Ubergraph |

Ubergraph

Matches in Ubergraph for { <http://purl.obolibrary.org/obo/SO_0000590> ?p ?o ?g. }

Showing items 1 to 100 of ±326 with 100 items per page.

SO_0000590 BFO_0000051 BFO_0000001 @default.
SO_0000590 BFO_0000051 BFO_0000002 @default.
SO_0000590 BFO_0000051 BFO_0000004 @default.
SO_0000590 BFO_0000051 BFO_0000040 @default.
SO_0000590 BFO_0000051 CHEBI_10545 @default.
SO_0000590 BFO_0000051 CHEBI_24431 @default.
SO_0000590 BFO_0000051 CHEBI_24433 @default.
SO_0000590 BFO_0000051 CHEBI_25555 @default.
SO_0000590 BFO_0000051 CHEBI_25585 @default.
SO_0000590 BFO_0000051 CHEBI_27594 @default.
SO_0000590 BFO_0000051 CHEBI_33233 @default.
SO_0000590 BFO_0000051 CHEBI_33247 @default.
SO_0000590 BFO_0000051 CHEBI_33250 @default.
SO_0000590 BFO_0000051 CHEBI_33252 @default.
SO_0000590 BFO_0000051 CHEBI_33253 @default.
SO_0000590 BFO_0000051 CHEBI_33300 @default.
SO_0000590 BFO_0000051 CHEBI_33306 @default.
SO_0000590 BFO_0000051 CHEBI_33318 @default.
SO_0000590 BFO_0000051 CHEBI_33560 @default.
SO_0000590 BFO_0000051 CHEBI_33791 @default.
SO_0000590 BFO_0000051 CHEBI_33792 @default.
SO_0000590 BFO_0000051 CHEBI_36338 @default.
SO_0000590 BFO_0000051 CHEBI_36339 @default.
SO_0000590 BFO_0000051 CHEBI_36340 @default.
SO_0000590 BFO_0000051 CHEBI_36342 @default.
SO_0000590 BFO_0000051 CHEBI_36343 @default.
SO_0000590 BFO_0000051 CHEBI_36344 @default.
SO_0000590 BFO_0000051 CHEBI_36347 @default.
SO_0000590 BFO_0000051 CHEBI_50297 @default.
SO_0000590 BFO_0000051 CHEBI_50299 @default.
SO_0000590 BFO_0000051 CHEBI_50319 @default.
SO_0000590 BFO_0000051 CHEBI_50320 @default.
SO_0000590 BFO_0000051 COB_0000006 @default.
SO_0000590 BFO_0000051 COB_0000007 @default.
SO_0000590 BFO_0000051 COB_0000010 @default.
SO_0000590 BFO_0000051 COB_0000011 @default.
SO_0000590 BFO_0000051 COB_0000012 @default.
SO_0000590 BFO_0000051 COB_0000013 @default.
SO_0000590 BFO_0000051 COB_0000043 @default.
SO_0000590 BFO_0000051 COB_0000049 @default.
SO_0000590 COB_0000047 BFO_0000001 @default.
SO_0000590 COB_0000047 BFO_0000002 @default.
SO_0000590 COB_0000047 BFO_0000004 @default.
SO_0000590 COB_0000047 BFO_0000040 @default.
SO_0000590 COB_0000047 CHEBI_10545 @default.
SO_0000590 COB_0000047 CHEBI_24431 @default.
SO_0000590 COB_0000047 CHEBI_24433 @default.
SO_0000590 COB_0000047 CHEBI_25555 @default.
SO_0000590 COB_0000047 CHEBI_25585 @default.
SO_0000590 COB_0000047 CHEBI_27594 @default.
SO_0000590 COB_0000047 CHEBI_33233 @default.
SO_0000590 COB_0000047 CHEBI_33247 @default.
SO_0000590 COB_0000047 CHEBI_33250 @default.
SO_0000590 COB_0000047 CHEBI_33252 @default.
SO_0000590 COB_0000047 CHEBI_33253 @default.
SO_0000590 COB_0000047 CHEBI_33300 @default.
SO_0000590 COB_0000047 CHEBI_33306 @default.
SO_0000590 COB_0000047 CHEBI_33318 @default.
SO_0000590 COB_0000047 CHEBI_33560 @default.
SO_0000590 COB_0000047 CHEBI_33791 @default.
SO_0000590 COB_0000047 CHEBI_33792 @default.
SO_0000590 COB_0000047 CHEBI_36338 @default.
SO_0000590 COB_0000047 CHEBI_36339 @default.
SO_0000590 COB_0000047 CHEBI_36340 @default.
SO_0000590 COB_0000047 CHEBI_36342 @default.
SO_0000590 COB_0000047 CHEBI_36343 @default.
SO_0000590 COB_0000047 CHEBI_36344 @default.
SO_0000590 COB_0000047 CHEBI_36347 @default.
SO_0000590 COB_0000047 CHEBI_50297 @default.
SO_0000590 COB_0000047 CHEBI_50299 @default.
SO_0000590 COB_0000047 CHEBI_50319 @default.
SO_0000590 COB_0000047 CHEBI_50320 @default.
SO_0000590 COB_0000047 COB_0000006 @default.
SO_0000590 COB_0000047 COB_0000007 @default.
SO_0000590 COB_0000047 COB_0000010 @default.
SO_0000590 COB_0000047 COB_0000011 @default.
SO_0000590 COB_0000047 COB_0000012 @default.
SO_0000590 COB_0000047 COB_0000013 @default.
SO_0000590 COB_0000047 COB_0000043 @default.
SO_0000590 COB_0000047 COB_0000049 @default.
SO_0000590 IAO_0000115 "The signal recognition particle (SRP) is a universally conserved ribonucleoprotein. It is involved in the co-translational targeting of proteins to membranes. The eukaryotic SRP consists of a 300-nucleotide 7S RNA and six proteins: SRPs 72, 68, 54, 19, 14, and 9. Archaeal SRP consists of a 7S RNA and homologues of the eukaryotic SRP19 and SRP54 proteins. In most eubacteria, the SRP consists of a 4.5S RNA and the Ffh protein (a homologue of the eukaryotic SRP54 protein). Eukaryotic and archaeal 7S RNAs have very similar secondary structures, with eight helical elements. These fold into the Alu and S domains, separated by a long linker region. Eubacterial SRP is generally a simpler structure, with the M domain of Ffh bound to a region of the 4.5S RNA that corresponds to helix 8 of the eukaryotic and archaeal SRP S domain. Some Gram-positive bacteria (e.g. Bacillus subtilis), however, have a larger SRP RNA that also has an Alu domain. The Alu domain is thought to mediate the peptide chain elongation retardation function of the SRP. The universally conserved helix which interacts with the SRP54/Ffh M domain mediates signal sequence recognition. In eukaryotes and archaea, the SRP19-helix 6 complex is thought to be involved in SRP assembly and stabilizes helix 8 for SRP54 binding." @default.
SO_0000590 RO_0002131 BFO_0000001 @default.
SO_0000590 RO_0002131 BFO_0000002 @default.
SO_0000590 RO_0002131 BFO_0000004 @default.
SO_0000590 RO_0002131 BFO_0000040 @default.
SO_0000590 RO_0002131 CHEBI_10545 @default.
SO_0000590 RO_0002131 CHEBI_24431 @default.
SO_0000590 RO_0002131 CHEBI_24433 @default.
SO_0000590 RO_0002131 CHEBI_25555 @default.
SO_0000590 RO_0002131 CHEBI_25585 @default.
SO_0000590 RO_0002131 CHEBI_27594 @default.
SO_0000590 RO_0002131 CHEBI_33233 @default.
SO_0000590 RO_0002131 CHEBI_33247 @default.
SO_0000590 RO_0002131 CHEBI_33250 @default.
SO_0000590 RO_0002131 CHEBI_33252 @default.
SO_0000590 RO_0002131 CHEBI_33253 @default.
SO_0000590 RO_0002131 CHEBI_33300 @default.
SO_0000590 RO_0002131 CHEBI_33306 @default.
SO_0000590 RO_0002131 CHEBI_33318 @default.
SO_0000590 RO_0002131 CHEBI_33560 @default.