CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008767
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cysteine--tRNA ligase 
Protein Synonyms/Alias
 Cysteinyl-tRNA synthetase; CysRS 
Gene Name
 YNL247W; N0885 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
46YNSLTRSKVEFIPQSubiquitination[1]
125YLFDNFVKENDTKFNacetylation[2]
485NSMNNFFKTIRALKNacetylation[2]
679IVKLNEEKHANELAKacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
  
Sequence Annotation
 MOTIF 65 75 "HIGH" region.
 MOTIF 427 431 "KMSKS" region.
 METAL 63 63 Zinc (By similarity).
 METAL 369 369 Zinc (By similarity).
 METAL 394 394 Zinc (By similarity).
 METAL 398 398 Zinc (By similarity).
 BINDING 430 430 ATP (By similarity).
 MOD_RES 326 326 Phosphoserine.  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 767 AA 
Protein Sequence
MNIFIKALRR YTIMSTPKIV QPKWKVPTPQ AKETVLKLYN SLTRSKVEFI PQSGNRGVTW 60
YSCGPTVYDA SHMGHARNYV SIDINRRIIQ DYFGYDVQFV QNVTDIDDKI ILRARQNYLF 120
DNFVKENDTK FNATVVDKVK TALFQYINKN FTIQGSEIKT IEEFETWLSN ADTETLKLEN 180
PKFPMHVTAV QNAIESITKG DSMDAEVAFE KVKDVTVPLL DKELGSTISN PEIFRQLPAY 240
WEQKFNDDML SLNVLPPTVT TRVSEYVPEI IDFVQKIIDN GYAYATSDGS VYFDTLKFDK 300
SPNHDYAKCQ PWNKGQLDLI NDGEGSLSNF ADNGKKSNND FALWKASKAG EPEWESPWGK 360
GRPGWHIECS VMASDILGSN IDIHSGGIDL AFPHHDNELA QSEARFDNQQ WINYFLHTGH 420
LHIEGQKMSK SLKNFITIQE ALKKFSPRQL RLAFASVQWN NQLDFKESLI HEVKSFENSM 480
NNFFKTIRAL KNDAASAGHI SKKFSPLEKE LLADFVESES KVHSAFCDNL STPVALKTLS 540
ELVTKSNTYI TTAGAALKIE PLIAICSYIT KILRIIGFPS RPDNLGWAAQ AGSNDGSLGS 600
LEDTVMPYVK CLSTFRDDVR SLAIKKAEPK EFLQLTDKIR NEDLLNLNVA LDDRNGQSAL 660
IKFLTNDEKL EIVKLNEEKH ANELAKKQKK LEQQKLREQK ENERKQKAQI KPQDMFKDVT 720
LYSAWDEQGL PTKDKDGNDI TKSMTKKLKK QWEQQKKLHE EYFGEDK 767 
Gene Ontology
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004817; F:cysteine-tRNA ligase activity; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006423; P:cysteinyl-tRNA aminoacylation; IDA:SGD. 
Interpro
 IPR015803; Cys-tRNA-ligase.
 IPR024909; Cys-tRNA/MSH_ligase.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd. 
Pfam
 PF01406; tRNA-synt_1e 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00983; TRNASYNTHCYS.