ID   SYV_EHRRG               Reviewed;         812 AA.
AC   Q5FF72;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02005};
GN   OrderedLocusNames=ERGA_CDS_00680;
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
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_02005}.
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_02005};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR   EMBL; CR925677; CAI27520.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5FF72; -.
DR   SMR; Q5FF72; -.
DR   EnsemblBacteria; CAI27520; CAI27520; ERGA_CDS_00680.
DR   KEGG; erg:ERGA_CDS_00680; -.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000000533; Chromosome.
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   HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR022874; Valine-tRNA_ligase_type_2.
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..812
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224609"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           536..540
FT                   /note="'KMSKS' region"
FT   BINDING         539
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   812 AA;  94150 MW;  61D6C3E0DF4C9A5C CRC64;
     MIMQSLFSNK YKFKDTEEKL NAYWDKIKLY KWKNLQGKQF IIDTPPPTIS GQLHIGHVFS
     YCHTDFIARY QRMLGKDVLY PIGFDDNGLP TERLVEKIKK VRAADIDRKE FKALCNEVSA
     KFRMEFKILF QSLGISYDWD LEYHTISEEI QKLSQMSFIA LYNMGKIYRK LQPIFWDCAD
     RTAIARVEVE EKEMSSFMST IAFSTEAGER INIATTRPEL MPACVALFFN PLDIRYQHLQ
     GQYAIVPIFG NKVPILSDEQ VKIDKGTGLV MCCTFGDELD VYWWNKHNLN TQIIISKSGT
     LDLKHNIAET DTLSGKLHGV SIVEARKLVL ETLSKCNLLI KKEEILHNVK CAERSGMPIE
     ILLSNQWFIK VVEVKHELLE QVRKINWYPQ SMRKQIEMWI DGLNWDWCIS RQRYFGIPFP
     VWYSKRDNEE IIIPDVNELP IDPTETLPQG YSKEEVEADV DVMDTWATSS LSPQFNSIHT
     GINSIPLVPA SLRAQSHEII RSWAFYTILQ AYYHHNSIPW ENIMVSGWCL AADKSKMSKS
     KGNALIPNQL LQEYGADVIR YWAANSRLGS DTVFSDEVLQ LGKRLVTKLW NASKFVSMFV
     SQCQIPDLNY VTETMDKWVL TKLYKVIVKA TESFDVFEYC VALDYIESFF WKDFCDNYLE
     LVKKRAYGES VTSKENLSAV NTLSFVLTTL LKMLAPFMPY ITEEIYSTLY NNGSIHDHDN
     WPIVNTSLCN EMDEQLGEDF IEILNQVRKI KANAQLSVKC KIYKLIINSE NYDFPTSWEN
     DLKAVCNAEH IVRDKRTSYY DDKFLVSVQF AS