※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Leucine--tRNA ligase 2
Protein Synonyms/Alias
 LeuRS 2
Gene Name
 leuS2
Gene Synonyms/Alias
 leuS; OrderedLocusNames=SSO0589
Created Date
 3-June-2014
Organism
 Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
NCBI Taxa ID
 273057
Phosphorylation
Position
Peptide
Code
Type
References
365 DLKKLTEYVYRTEYN Y HTP [1]
531 KIKQYKLSPSKLTQE S HTP [1]
52 GHGRTYVTGDILARY T HTP [1]
930 DEEVKKTYNKEAMPL Y HTP [1]
704 KWLLSRIYEITSSTT Y HTP [1]
929 YDEEVKKTYNKEAMP T HTP [1]
49 WHIGHGRTYVTGDIL T HTP [1]
710 IYEITSSTTRHMEAL T HTP [1]
709 RIYEITSSTTRHMEA S HTP [1]
59 TGDILARYKRMRGYN Y HTP [1]
50 HIGHGRTYVTGDILA Y HTP [1]
707 LSRIYEITSSTTRHM T HTP [1]
363 DEDLKKLTEYVYRTE T HTP [1]
367 KKLTEYVYRTEYNKG Y HTP [1]
533 KQYKLSPSKLTQEFW S HTP [1]
6 **MNNIAYKWQTRWE Y HTP [1]
711 YEITSSTTRHMEALE T HTP [1]
708 SRIYEITSSTTRHME S HTP [1]
Reference
 [1]Change of carbon source causes dramatic effects in the phospho-proteome of the archaeon Sulfolobus solfataricus.
 Esser D,Pham TK,Reimann J,Albers SV,Siebers B,Wright PC
 J. Proteome Res. 2012, Oct, 5;11(10):4823-33. [PMID:22639831]
Functional Description From UniProt
 
Sequence Annotation From UniProt
 
Key Word From UniProt
 Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome
Protein Sequence
 MNNIAYKWQT RWEEDKIYES NPNPSKPKFF TTVAFPYPNS PWHIGHGRTY VTGDILARYK 60
 RMRGYNVLFP MAFHYTGTPI MAMADAIAKG DKELIETFKD IYEISPDVIP RMSDPLFMAN 120
 YFKEDIKASM REIGLGIDWR REFTTIDPEF SSFVTWQFHK LQSKGYIVKD THPVGWCPVH 180
 HIPVGMHDTK GDVEPEIGEF VLIYFNSEKG IFPAATLRPE TIFGATALWI NPSEMYVVAS 240
 MLGKKMILSE KAAAKLSFQI DDIEIEEKIK GSKLVGLKVE NPITGKHIAV LGADFVDVSL 300
 GTGVVMSVPA HAPFDYYYSK KTFKNNNIEI IPVITVEGLG NALAKDVVEK NNPKSDEDLK 360
 KLTEYVYRTE YNKGVLRSDL GNLIREEYRN ELKSLGGLPV PKGRELITNF LISKGLGRKI 420
 FEVMNKPVYC RCGTEIVVKI LKDQWFLDYS NKEWKELARK SLSKINVIPE ESRKDFEFTI 480
 EWLEKRACAR TRGLGTPLPW DKKWIIESLS DSTIYMAYYT ISHKIKQYKL SPSKLTQEFW 540
 DYVMLGIGNL EEISEKTGIP SNIIKEFREE FLYWYPLDIR HSGKDLIPNH LTFFIFNHAA 600
 IFQENLWPKA IAVNGLVLYE GKKMSKSLRN IIPLRKGLKM YGVDVMRIAV SSTADMGSDV 660
 NFSESLVKTV GETLRKMYEL FKSLDNYTGD ILGFPEKWLL SRIYEITSST TRHMEALELR 720
 DAVNELLFVF SSDLDEYFGM VSAEGREANN KVLREVLTIW LKLITPFAPH LAEEIWHEIL 780
 KQKTYIVNEG WPEVEGSKMD ELTLLEHEYM KRIVEDIRSI LNIFKGTPKL IKIYALNDSR 840
 YMELLRDAIV ANGQMKKFMD IHKPKSREDA RILQKIFNES LEIDDKMKKL VTNYNINEVD 900
 VLNKLSKYIR RKLNVDILIE PYDEEVKKTY NKEAMPLRPA IIIE 944
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  GO:0002161   F:aminoacyl-tRNA editing activity IEA:InterPro
  GO:0005524   F:ATP binding IEA:UniProtKB-HAMAP
  GO:0004823   F:leucine-tRNA ligase activity IEA:UniProtKB-HAMAP
  GO:0006429   P:leucyl-tRNA aminoacylation IEA:UniProtKB-HAMAP
  IPR002300   aa-tRNA-synth_Ia.
  IPR020791   Leu-tRNA-lgase_arc.
  IPR004493   Leu-tRNA-synth_Ia_arc/euk.
  IPR014729   Rossmann-like_a/b/a_fold.
  IPR009080   tRNAsynth_1a_anticodon-bd.
  IPR013155   V/L/I-tRNA-synth_anticodon-bd.
  IPR009008   Val/Leu/Ile-tRNA-synth_edit.
  PF08264   Anticodon_1.
  PF00133   tRNA-synt_1.