ID   SYV_SPHEL               Reviewed;         811 AA.
AC   Q7X2N3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004};
OS   Sphingomonas elodea.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=179878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31461 / PS-60;
RX   PubMed=14767675; DOI=10.1007/s10295-004-0118-9;
RA   Harding N.E., Patel Y.N., Coleman R.J.;
RT   "Organization of genes required for gellan polysaccharide biosynthesis in
RT   Sphingomonas elodea ATCC 31461.";
RL   J. Ind. Microbiol. Biotechnol. 31:70-82(2004).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
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:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; AY220100; AAP46185.1; -; Genomic_DNA.
DR   STRING; 1081640.AGFU01000061_gene244; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07962; Anticodon_Ia_Val; 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; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..811
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224559"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           542..546
FT                   /note="'KMSKS' region"
FT   BINDING         545
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   811 AA;  90775 MW;  D5E32C2901DC2F4A CRC64;
     MTELPKTFDP AEIESRWYAH WEDEGLFRPE RTGAEPWTIV NPPPNVTGSL HIGHALDNTL
     QDILVRHARL KGKDARWVVG TDHAGIATQM VVERQLNAAG SKRTDFTREA FVDKVWEWKA
     ESGGQITRQL RRLGCSMDWA NERFTMDEGF SKAVLKVFVE LYRQGLVYRD KRLVNWDPGL
     GTAISDLEVE TKEVRGNFWH LRYPLADGSG YIQVATTRPE TMLADMAVAV HPEDERYKAL
     IGKQVRLPIT DRLIPIVGDE HADPELGSGA VKITPGHDFN DFEVGVRAGI KAGEMLNMLD
     AKAAICQTQD GLVPAELIGL DRFEARKVIV ARLKDEGFLV PWTDKEGAEH DAEPRTIQTP
     YGDRSGQVIE PWLTDQWYVD AATLAKPAIE AVRSGATKIV PKSWEKTYFN WMENIQPWCV
     SRQLWWGHRI PAWFDAEGKP YVAETEEEAQ AEAGEGVALT RDPDVLDTWF SSALWPFATL
     GWPENSDPTL GGRYSNDVLI SGFDILFFWD ARMMMQGLHF MKEVPFKTLY LHGLVRAADG
     QKMSKSKGNT VDPLGMIDKY GADALRFFMA AMESQGRDIK MDEKRLEGYR NFATKLWNAA
     RFCQANGIAA SKSLEAPTAE LAVNRWIIAE TIATVXALDL ALADLRFDEA ANCIYQFVWS
     RFCDWYLELI KPVLQGEGVA AAQAEETRAV AGWALDQILV MLHPFMPFIT EELWSKMGPR
     EHDLIVAKWP MADARALDPS AAQEIDWLIR LVSEIRAART ELNVPPGARL PLHVRDASAE
     TAXRLIGQEA ALARLGRVDQ AQGDAPAGGG A