Tag | Content |
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CPLM ID | CPLM-011200 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Valine--tRNA ligase |
Protein Synonyms/Alias | Valyl-tRNA synthetase; ValRS |
Gene Name | Vars |
Gene Synonyms/Alias | Vars2 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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398 | VVEKKLWKERGLNRH | acetylation | [1] | 432 | DRIYHQLKKLGSSLD | acetylation | [1] | 645 | KAVLAALKEQGLFRG | acetylation | [1] | 975 | FVPSPTSKPEGHESL | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | |
Sequence Annotation | DOMAIN 89 219 GST C-terminal. MOTIF 344 354 "HIGH" region. MOTIF 862 866 "KMSKS" region. BINDING 865 865 ATP (By similarity). MOD_RES 2 2 N-acetylserine (By similarity). MOD_RES 645 645 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 | 1264 AA |
Protein Sequence | MSILYVSPHP DAFPSLRALI AARYGEAGDG PGWGGPHPRI CLQPPPSSRT PFPPPRLPAL 60 EQGPGGLWVW GAPAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELTPA ACGATLPALG 120 LRGPGQDPQA ALGALGKALN PLEEWLRLHT YLAGDAPTLA DLAAVTALLL PFRYVLDPSA 180 RRIWGNVTRW FNTCVRQPEF RAVLGEVVLY SGARSVTQQP GSEITAPQKT AAQLKKEAKK 240 REKLEKFQQK QKTQQQQPAH GEKKPKPEKK EKRDPGVITY DLPTPPGEKK DVSGTMPDSY 300 SPQYVEAAWY PWWERQGFFK PEYGRPSVSA PNPRGVFMMC IPPPNVTGSL HLGHALTNAI 360 QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWKER GLNRHQLGRE AFLQEVWKWK 420 AEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSATVTEAFV RLHEEGVIYR STRLVNWSCT 480 LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET 540 MLGDVAVAVH PKDPRYQHLK GKSVVHPFLS RSLPIVFDDF VDMEFGTGAV KITPAHDQND 600 YEVGQRHRLE AISIMDSKGA LVNVPPPFLG LPRFEARKAV LAALKEQGLF RGIKDNPMVV 660 PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH SWMDNIRDWC 720 ISRQLWWGHR IPAYFITVHD PAVPPGEDPD GRYWVSGRTE AEAREKAARE FGVSPDKISL 780 QQDEDVLDTW FSSGLFPFSI FGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL 840 TEKLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIHGV SLQGLHDQLL NSNLDPSEVE 900 KAKEGQRADF PAGIPECGTD ALRFGLCAYT SQGRDINLDV NRILGYRHFC NKLWNATKFA 960 LRGLGKGFVP SPTSKPEGHE SLVDRWIRSR LAEAVRLSNE GFQAYDFPAV TTAQYSFWLY 1020 ELCDVYLECL KPVLNGVDQV AADCARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRTP 1080 NAPASLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRT RPDCFLEVAD 1140 EATGALASAV SAYVQTLASA GVVAVLALGA PAPQGCAVAV ASDRCSIHLQ LQGLVDPARE 1200 LGKLQAKRSE AQRQAQRLQE RRAASGYSAK VPLEVQEADE VKLQQTEAEL RKVDEAIALF 1260 QKML 1264 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:Compara. GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004832; F:valine-tRNA ligase activity; IDA:RGD. GO:0006450; P:regulation of translational fidelity; IEA:GOC. GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |