Tag | Content |
---|
CPLM ID | CPLM-002641 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phenylalanine--tRNA ligase alpha subunit |
Protein Synonyms/Alias | Phenylalanyl-tRNA synthetase alpha subunit; PheRS |
Gene Name | pheS |
Gene Synonyms/Alias | b1714; JW5277 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
---|
34 | VRVEYLGKKGHLTLQ | acetylation | [1] | 64 | GAVINEAKEQVQQAL | acetylation | [1] | 75 | QQALNARKAELESAA | acetylation | [1] | 179 | GVQIRTMKAQQPPIR | acetylation | [1] | 262 | AEVDVMGKNGKWLEV | acetylation | [1] | 265 | DVMGKNGKWLEVLGC | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | |
Sequence Annotation | METAL 252 252 Magnesium (By similarity). |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 327 AA |
Protein Sequence | MSHLAELVAS AKAAISQASD VAALDNVRVE YLGKKGHLTL QMTTLRELPP EERPAAGAVI 60 NEAKEQVQQA LNARKAELES AALNARLAAE TIDVSLPGRR IENGGLHPVT RTIDRIESFF 120 GELGFTVATG PEIEDDYHNF DALNIPGHHP ARADHDTFWF DTTRLLRTQT SGVQIRTMKA 180 QQPPIRIIAP GRVYRNDYDQ THTPMFHQME GLIVDTNISF TNLKGTLHDF LRNFFEEDLQ 240 IRFRPSYFPF TEPSAEVDVM GKNGKWLEVL GCGMVHPNVL RNVGIDPEVY SGFAFGMGME 300 RLTMLRYGVT DLRSFFENDL RFLKQFK 327 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |