SYV_CAEEL
ID SYV_CAEEL Reviewed; 1050 AA.
AC Q9U1Q4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Valine--tRNA ligase;
DE EC=6.1.1.9;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=glp-4 {ECO:0000312|WormBase:Y87G2A.5};
GN Synonyms=vars-2 {ECO:0000312|WormBase:Y87G2A.5},
GN vrs-2 {ECO:0000312|WormBase:Y87G2A.5};
GN ORFNames=Y87G2A.5 {ECO:0000312|WormBase:Y87G2A.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAB60428.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB60428.1}
RP PROTEIN SEQUENCE OF 513-524; 646-658; 704-714 AND 760-771, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000305};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255}.
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DR EMBL; AL110500; CAB60428.1; -; Genomic_DNA.
DR RefSeq; NP_493377.1; NM_060976.4.
DR AlphaFoldDB; Q9U1Q4; -.
DR SMR; Q9U1Q4; -.
DR BioGRID; 38618; 10.
DR STRING; 6239.Y87G2A.5; -.
DR iPTMnet; Q9U1Q4; -.
DR EPD; Q9U1Q4; -.
DR PaxDb; Q9U1Q4; -.
DR PeptideAtlas; Q9U1Q4; -.
DR PRIDE; Q9U1Q4; -.
DR EnsemblMetazoa; Y87G2A.5.1; Y87G2A.5.1; WBGene00006936.
DR GeneID; 173224; -.
DR KEGG; cel:CELE_Y87G2A.5; -.
DR UCSC; Y87G2A.5; c. elegans.
DR CTD; 173224; -.
DR WormBase; Y87G2A.5; CE24685; WBGene00006936; glp-4.
DR eggNOG; KOG0432; Eukaryota.
DR GeneTree; ENSGT00940000167981; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; Q9U1Q4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 229591at2759; -.
DR PhylomeDB; Q9U1Q4; -.
DR BRENDA; 6.1.1.9; 1045.
DR PRO; PR:Q9U1Q4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006936; Expressed in larva and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..1050
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000252086"
FT REGION 37..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 127..137
FT /note="'HIGH' region"
FT /evidence="ECO:0000255"
FT MOTIF 642..646
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255"
FT COMPBIAS 37..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1050 AA; 118921 MW; F33DB53587EAC057 CRC64;
MSDPAGNRPK TEKELKKEAE KAAKLAKFEE KQKKLAEKKA AASDKPVKEA KAKKEQTVEA
AEPVDQTPTG QRKKIDGEIP AAYFPGYVES GWYSWWEKEG FFKPEYIDKL NPGSNPADSF
TVCIPPPNVT GNLHVGHALA TTVEDTITRF NRMHGKRTLF NPGCDHAGIA TQVVVEKRLK
RERGLTRHDL GRDRFNQEVW HWKNEKGDVI YDQFRKLGAS VDWDRAVFTM DPKMCRAVTE
AFIRMHESGT IYRSNRLVNW SCALRSAISD IEVDKKELTG STLIAVPGYD KKIEFGVLNS
FAYKIQGSDE EIVVSTTRIE TMLGDSGVAV HPDDQRYKHL VGKQCIHPFI PTRNLPIFAD
SFVEMEFGTG AVKITPAHDH NDYEVGIRQN LPFHNCITDD GLISQGCGEF SGMKRFDART
AVIEALKEKG LYRGKEDNPM VVPTCSRSKD VIEPILKPQW YVKCAHMAEK AVAAVANGDL
QIIPEFHKAT WNRWLESSRD WCISRQLWWG HRIPAYYISF ADGREQPLPE ENYWVSARTE
QEALAKAAQK FQVPEAEILL KWDEDVLDTW FSSGMWPFAV FGWPDATKDM DLFFPGAVLE
TGHDILFFWV ARMVFMAQEL TGKLPFKEIL LHAMIRDAHG RKMSKSLGNV IDPLDVIRGI
SLNDLQAQLL GGNLDEKEIA VAKEGQARDY PDGIPECGVD ALRFALLSYT SQGRDINLDV
LRVHGYRKFC NKLWQVVRFA LARISDKPEQ KPTFEINLKS ATPTDLWILS RLAKAVKETN
EALKAYNFTQ ATTVTYNFWL YDFCDVYVET IKPVLYGDNT TLRQVAISVL HKCIDTGLRL
ISPLMPFISE ELWQRMPRLD DSDYTSPSII VAQYPLTQKY EKYQNEKLEA AFEFAQELIG
KVRSLRADYD LKKTKITMQI LSETPEDESM LNDISAVITT LTFSEKVSIL NKCESDKIEK
GSAHIACGGR CQVYINLTGI IDVPKEIEKL GAKLQKNQIS VKKIGDIQSS ADYEQKVPVD
IRALDQEKKA TLEKEIENIT AAIAQLKALN
