Tag | Content |
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CPLM ID | CPLM-013654 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tyrosine--tRNA ligase, mitochondrial |
Protein Synonyms/Alias | Tyrosyl-tRNA synthetase; TyrRS |
Gene Name | Yars2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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349 | RLAAEVTKLVHGQEG | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity). |
Sequence Annotation | MOTIF 76 85 "HIGH" region. MOTIF 275 279 "KMSKS" region. BINDING 278 278 ATP (By similarity). MOD_RES 349 349 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 471 AA |
Protein Sequence | MAAPMLRHLC RVPQSGVWTR GPRAVRPGAR GMLVAPRARG LFKEFFPESG TKTELPELFD 60 RRRAGSPQTV YCGFDPTGDS LHVGHLLTLL GLFHFQRAGH NVIALVGGST ALLGDPSGRT 120 KEREALSAEC VRANARALQR GLETLAANHA RLFADGRPWG TFTVLDNAAW FQKQHLMDFL 180 ATVGGHFRMG TLLSRLSVQS RLKSPEGMSL AEFFYQVLQA YDFYYLFRHY GCRVQLGGSD 240 QLGNIMSGYE FIHKLTGEDV FGITVPLITS TTGAKLGKSA GNAVWLNREK TSPFELYQFF 300 IRQQDDSVER YLKLFTFLPL PEIDHIMQLH VKEPEKRIAQ KRLAAEVTKL VHGQEGLDSA 360 KRCTQALYHS SIEALEVMSD QELKELFKEA SFSELVLDPG TSVIDTCRKA NAIPDGPRGY 420 RMITEGGVSI NHRQVTNPES VLVIGQHILK NGLSLLKIGK RNFYIIKWLQ L 471 |
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