Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lysine--tRNA ligase |
Protein Synonyms/Alias | LysRS |
Gene Name | lysS |
Gene Synonyms/Alias | asuD, herC; OrderedLocusNames=b2890, JW2858 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 133 | GKLFKTKTGELSIHC | T | HTP | [1] | 2 | ******MSEQHAQGA | S | HTP | [1] | |
Reference | [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M Mol. Cell Proteomics 2008, Feb;7(2):299-307. [ PMID:17938405] |
Functional Description From UniProt | |
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| 3D-structure; Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Directproteinsequencing; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome |
Protein Sequence | MSEQHAQGAD AVVDLNNELK TRREKLANLR EQGIAFPNDF RRDHTSDQLH AEFDGKENEE 60 LEALNIEVAV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDDLPEGVYN EQFKKWDLGD 120 ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES 180 RNTFKVRSQI LSGIRQFMVN RGFMEVETPM MQVIPGGAAA RPFITHHNAL DLDMYLRIAP 240 ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT 300 LAQDILGKTE VTYGDVTLDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS AKAIAESIGI 360 HVEKSWGLGR IVTEIFEEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG 420 REIGNGFSEL NDAEDQAQRF LDQVAAKDAG DDEAMFYDED YVTALEHGLP PTAGLGIGID 480 RMVMLFTNSH TIRDVILFPA MRPVK 505 |
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