ID   SYV_ORITB               Reviewed;         854 AA.
AC   A5CCE0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=OTBS_0273;
OS   Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=357244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boryong;
RX   PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA   Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA   Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA   Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT   "The Orientia tsutsugamushi genome reveals massive proliferation of
RT   conjugative type IV secretion system and host-cell interaction genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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; AM494475; CAM79339.1; -; Genomic_DNA.
DR   RefSeq; WP_011944374.1; NC_009488.1.
DR   AlphaFoldDB; A5CCE0; -.
DR   SMR; A5CCE0; -.
DR   EnsemblBacteria; CAM79339; CAM79339; OTBS_0273.
DR   KEGG; ots:OTBS_0273; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000001565; 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..854
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000022181"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           551..555
FT                   /note="'KMSKS' region"
FT   BINDING         554
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   854 AA;  98045 MW;  DB6B8160A138F849 CRC64;
     MAELSANYNY LENEPKWQDD WQKKNIYQWN STLPKDKTFI VDPPPPTVSG DLHIGHAMSF
     IQLDCIVRYQ RMLGKNIFFP IGFDDNGLPT ERFVEKIKNV RASNIARPDF IKMCQEVVIA
     KEGEFCKFLN AIGLSVDWSL KYQTISSLSC KISQMSFLDL VNKNQVYRNH QPVLWDCIDQ
     TALSQADVED KERITSMYYI AFAVMNSELK VQIATTRPEM LPACCAIFFN PNDIRYQHLH
     NQFAITPLFK SVVPILAEET VDINKGSGLV MCCTFGDTKD VAWWRKHNLP TRIIIDYYGK
     VKPLDFTVSS QNQEKFTEYY NQITGLKIAQ ARNKVVELLH HNQLIIKQEQ ISQTVKQAER
     SGAILEIIMA PQWFIKVVEH KDALLQKSQE LEWYPKSMKI KLDNWINSLA WDWCISRQRY
     FGIPFPVWYS KREGEEGKII FADISQLPVD PLYDLPAGYS KDEVIPDSDV MDTWATSSLS
     PQLSSHGISS NLTIDSTRHN QLFPADLRSQ AHEIIRTWTF YTIVKSYLHQ NSLPWSKIMI
     SGWCLADDRK KMSKSKGNII LPTELIKRYG ADAVRYWALT SQLGHDCVVS EQVIGIGKKL
     VNKLWNAARF ILQHITGKLT AEFLISAKHC VEKKVISCTT DLWMLSKLQD TVNNTSNLLN
     NYEYASARLY VEEFFLKDFC DNYLELVKSR IYDHSSEYQK SAIYSVFWGL KTILELFAPF
     VPFITEELYA AIYQSNNLCN GSIHSSNKWP LAQNFYNDEL ILTTGNLAIN ILTLVRKSKS
     ARKLSVKAPI SLLQVKYDSD SYQQLPSDLV DDLKLVTNSN EFSIVTNFTT IDDLITGDGI
     TVNIVYPGSM KHEC