| Tag | Content |
|---|
| CPLM ID | CPLM-024111 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Valine--tRNA ligase |
Protein Synonyms/Alias | Protein G7a; Valyl-tRNA synthetase; ValRS |
Gene Name | Vars |
Gene Synonyms/Alias | Bat6; G7a; Vars2 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1241 | VQEADEAKLQQTEAE | acetylation | [1] |
|
Reference | [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3. Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C. PLoS One. 2012;7(12):e50545. [ PMID: 23236377] |
Functional Description | |
Sequence Annotation | DOMAIN 89 219 GST C-terminal.
MOTIF 343 353 "HIGH" region.
MOTIF 861 865 "KMSKS" region.
BINDING 864 864 ATP (By similarity).
MOD_RES 2 2 N-acetylserine (By similarity).
MOD_RES 644 644 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1263 AA |
Protein Sequence | MSILYVSPHP DAFPSLRALI AARYGEAGDG PGWGGPHPRI CLQPPPSSRT PFPPPRLPAL 60
EQGPGGLWVW GAPAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG 120
LRGPGQDPQA ALGALGKALN PLEDWLRLHT YLAGDAPTLA DLAAVTALLL PFRYVLDPSA 180
RRIWGNVTRW FNTCVRQPEF RAVLGEVALY SGARSVTQQP GSEVIAPQKT PAQLKKEAKK 240
REKLEKFQQK QKTQQQPPHG EKKPKPEKKE KRDPGVITYD LPTPPGEKKD VSGAMPDSYS 300
PQYVEAAWYP WWERQGFFKP EYGRPSVSAP NPRGVFMMCI PPPNVTGSLH LGHALTNAIQ 360
DSLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLWKERG LNRHQLGREA FLEEVWKWKA 420
EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SATVTEAFVR LHEEGVIYRS TRLVNWSCTL 480
NSAISDIEVD KKELTGRTLL PVPGYKEKVE FGVLVSFAYK VQGSDSDEEV VVATTRIETM 540
LGDVAVAVHP KDPRYQHLKG KCVVHPFLSR SLPIVFDDFV DMEFGTGAVK ITPAHDQNDY 600
EVGQRHRLEA ISIMDSKGAL INVPPPFLGL PRFEARKAVL AALKERGLFR GVKDNPMVVP 660
LCNRSKDVVE PLLRPQWYVR CGEMAQAASA AVTRGDLRIL PEAHQRTWHS WMDNIRDWCI 720
SRQLWWGHRI PAYFITVHDP AVPPGEDPDG RYWVSGRTEA EAREKAAREF GVSPDKISLQ 780
QDEDVLDTWF SSGLFPFSIF GWPNQSEDLS VFYPGTLLET GHDILFFWVA RMVMLGLKLT 840
GKLPFREVYL HAIVRDAHGR KMSKSLGNVI DPLDVIHGVS LQGLYDQLLN SNLDPSEVEK 900
AKEGQKADFP AGIPECGTDA LRFGLCAYTS QGRDINLDVN RILGYRHFCN KLWNATKFAL 960
RGLGKGFVPS ATSKPEGHES LVDRWIRSRL TEAVRLSNEG FQAYDFPAIT TAQYSFWLYE 1020
LCDVYLECLK PVLNGVDQVA AECARQTLYT CLDVGLRLLS PFMPFVTEEL FQRLPRRTPK 1080
APASLCVTPY PEPSECSWKD PEAEAALELA LSITRAVRSL RADYNLTRTR PDCFLEVADE 1140
ATGALASAVS GYVQALASAG VVAVLALGAP APQGCAVAVA SDRCSIHLQL QGLVDPAREL 1200
GKLQAKRSEA QRQAQRLQER RAASSYSAKV PLEVQEADEA KLQQTEAELR KVDEAIALFQ 1260
KML 1263 |
Gene Ontology | GO:0005739; C:mitochondrion; IDA:MGI. GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004832; F:valine-tRNA ligase activity; IEA:EC. GO:0006450; P:regulation of translational fidelity; IEA:GOC. GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |