ID   SYV_TRIVA               Reviewed;         489 AA.
AC   P46216;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
DE   Flags: Fragment;
GN   Name=VALS;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30001 / NIH-C1;
RX   PubMed=7708661; DOI=10.1073/pnas.92.7.2441;
RA   Brown J.R., Doolittle W.F.;
RT   "Root of the universal tree of life based on ancient aminoacyl-tRNA
RT   synthetase gene duplications.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995).
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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; L37098; AAC41565.1; -; Genomic_DNA.
DR   AlphaFoldDB; P46216; -.
DR   SMR; P46216; -.
DR   STRING; 5722.XP_001321729.1; -.
DR   PRIDE; P46216; -.
DR   eggNOG; KOG0432; Eukaryota.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 2.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF50677; SSF50677; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           <1..>489
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106257"
FT   MOTIF           482..486
FT                   /note="'KMSKS' region"
FT   BINDING         485
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         489
SQ   SEQUENCE   489 AA;  56217 MW;  B21C02F404EB35D3 CRC64;
     DHAGIATQFR VEKKIYDEKK LHRGEYSREY FLEEAHKWVE SKSGTILSQL RDMGSSLAWK
     DTYYTLDEKL SESVIAAFIK LFDEGLIYRS ERLVNWDCAL KTAISDAEVE YITLTKRTKL
     NVPNHKYPQY PFGVMAHFYY EICDKDGKKT GEKVEIATTR LETMLGDTAV AINPKDARYN
     HLHGMYVWHP IREVPIPIIQ DEILVDMNFG TGVVKVTPGH DPNDYEVYKR HPEIGLISIL
     TPDGAIAPGY GQFSGMMRFD ARVEMVKWMK EHGLYKEEKD HEMRLGITQR GHDIVEQVIT
     PQWFVNTTDM AARAIKAVDD GELKIVPDEF VVDWKKWHEN IRPWCISRQL MWGLRIPAYR
     VQIDGKWAEG NGEWVAAASQ EEAIAKGAKA NNVVPSRVTV EQDPDVLDTW FSSALLPFSG
     VGWPSNEERL NRYFPNSILE TGWDILTFWV SRMVMMSLTL TNKVPFHTIL LHPLVRDAQG
     RKMSKSFGN