ID   SYV_EHRCJ               Reviewed;         802 AA.
AC   Q3YT16;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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}; OrderedLocusNames=Ecaj_0088;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(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; CP000107; AAZ68139.1; -; Genomic_DNA.
DR   RefSeq; WP_011304217.1; NC_007354.1.
DR   AlphaFoldDB; Q3YT16; -.
DR   SMR; Q3YT16; -.
DR   STRING; 269484.Ecaj_0088; -.
DR   EnsemblBacteria; AAZ68139; AAZ68139; Ecaj_0088.
DR   KEGG; ecn:Ecaj_0088; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000435; 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; Reference proteome.
FT   CHAIN           1..802
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224608"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           524..528
FT                   /note="'KMSKS' region"
FT   BINDING         527
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   802 AA;  93049 MW;  4B1A79DFF931A674 CRC64;
     MQSIFNNKYQ FKNIETKYNT LWDTTKLYKW KNSGTNQFVI DTPPPTISGQ LHIGHVFSYC
     HTDFIARYQR MLGKDVFYPI GFDDNGLPTE RLVEKTKKIR ATDISRKEFK TICTQVSHEF
     RIQFKQLFQS IGISYDWDLE YHTISKDIQK ISQTSFINLY NKGKLYRKLQ PIFWDCIDKT
     AIARAEVEEN ELSSFMNTIA FSTEAGKAIN IATTRPELMP ACVAVFFNPS DIRYQDLLGQ
     NAIVPIFGNK VKILSDDQVK IDKGTGLVMC CTFGDEMDVY WWNKHNLDTK IIISKSGTID
     HLNTLQGQDV CKQLHGLSIT EARALIIEIL ERNNLLIQKQ EITHNVKCAE RSGAPIEILL
     SHQWFIKVVD IKHELLKQVQ KINWHPQSMR KQIEIWIEGL NWDWCISRQR YFGVPFPVWY
     SKDGKIILPD INKLPIDPTN DLPEGYQDTE IEVETDVMDT WATSSLSTQF HNISATPADL
     RAQSHEIIRS WAFYTILQAY YHNNDIPWKN IMISGWCLAE DKTKMSKSKG NVLTPNKLLD
     EYGADVVRYW TANSKLGADT TFSNEILKLG KRFTTKLWNA SKFVSMFIDQ YSEPDLQYIT
     ETMDKWILSK LYKVIVKATE SFNSFEYCIA LDCIESFFWK DFCDNYLELS KKRAYGELIS
     KQEHLSAVNT LSFVLRELLK MLAPFMPYVT EEIYRTLYSS NNSIHSHNTW PAADVNLYNE
     SDELLGETFI EILNQVRKVK ASAQLSVKYK INKLIINKHF PVSLENDLKA VCNADCIVYD
     NRQNDNKEQL LVSVEFENVQ IT