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LOCUS WP_001089225 182 aa linear BCT 10-FEB-2020 ACCESSION WP_001089225 VERSION WP_001089225.1 KEYWORDS RefSeq. SOURCE Enterobacteriaceae ORGANISM Enterobacteriaceae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales. REFERENCE 1 (residues 1 to 182) AUTHORS Ude,S., Lassak,J., Starosta,A.L., Kraxenberger,T., Wilson,D.N. and Jung,K. TITLE Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches JOURNAL Science 339 (6115), 82-85 (2013) PUBMED 23239623 REFERENCE 2 (residues 1 to 182) AUTHORS Peil,L., Starosta,A.L., Virumae,K., Atkinson,G.C., Tenson,T., Remme,J. and Wilson,D.N. TITLE Lys34 of translation elongation factor EF-P is hydroxylated by YfcM JOURNAL Nat. Chem. Biol. 8 (8), 695-697 (2012) PUBMED 22706199 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: BlastRule Evidence Accession :: NBR011092 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..182 /organism="Enterobacteriaceae" /db_xref="taxon:543" gene 1..182 /gene="epmC" Protein 1..182 /product="elongation factor P hydroxylase" /EC_number="1.14.-.-" /calculated_mol_wt=21029 Region 4..181 /region_name="EpmC" /note="Elongation factor P hydroxylase EpmC (EF-P beta-lysylation pathway) [Translation, ribosomal structure and biogenesis]; COG3101" /db_xref="CDD:442335" ORIGIN 1 mnsthhyeql ieifnscfad dfntrlikgd depiylpada evpynrivfa hgfyasaihe 61 ishwciagka rreqvdfgyw ycpdgrdaqt qsqfedvevk pqaldwlfcv aagypfnvsc 121 dnlegdfepd rvvfqrrvha qvmdyltngi perparfika lqnyyhtpel taeqfpwpea 181 ln