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 | |
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| 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 |
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