HMM Summary Page: TIGR01575

AccessionTIGR01575
NamerimI
Functionribosomal-protein-alanine acetyltransferase
Gene SymbolrimI
Trusted Cutoff86.40
Domain Trusted Cutoff86.40
Noise Cutoff82.65
Domain Noise Cutoff82.65
Isology Typeequivalog
EC Number2.3.1.128
HMM Length132
Mainrole CategoryProtein synthesis
Subrole CategoryRibosomal proteins: synthesis and modification
Gene Ontology TermGO:0006464: protein modification process biological_process
GO:0008999: ribosomal-protein-alanine N-acetyltransferase activity molecular_function
GO:0042254: ribosome biogenesis biological_process
AuthorDurkin S
Entry DateJul 3 2002 2:45PM
Last ModifiedFeb 14 2011 3:27PM
CommentMembers of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli [1]. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database.
ReferencesRN [1] RM PMID: 2828880 RT Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. RA Yoshikawa A, Isono S, Sheback A, Isono K RL Mol Gen Genet 1987 Oct;209(3):481-8 RN [2] RM PMID: 6806564 RT Purification and characterization of 30S ribosomal proteins from Bacillus subtilis: correlation to Escherichia coli 30S proteins. RA Higo K, Otaka E, Osawa S RL Mol Gen Genet 1982;185(2):239-44