ID   SYV_RHILO               Reviewed;         927 AA.
AC   Q98LB1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=mll1104;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {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; BA000012; BAB48552.1; -; Genomic_DNA.
DR   RefSeq; WP_010909906.1; NC_002678.2.
DR   AlphaFoldDB; Q98LB1; -.
DR   SMR; Q98LB1; -.
DR   STRING; 266835.14021941; -.
DR   EnsemblBacteria; BAB48552; BAB48552; BAB48552.
DR   KEGG; mlo:mll1104; -.
DR   PATRIC; fig|266835.9.peg.890; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000552; 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; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 2.
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; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-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   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
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; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..927
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224544"
FT   COILED          856..917
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           571..575
FT                   /note="'KMSKS' region"
FT   BINDING         574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   927 AA;  104995 MW;  0EFAE339A503A00D CRC64;
     MLEKTYDAKT VEPKIAKVWE EADAFRAGAG AEEGAEAFTI VIPPPNVTGS LHMGHALNNT
     LQDILVRFER MRGKNVLWQP GMDHAGIATQ MVVERQLMEK QIHRRDLTRE QFIEKVWEWK
     AESGGTIFNQ LKRLGASADW SRERFTMDEG LSKAVLEVFV TLYKEGLIYK DKRLVNWDPR
     LLTAISDLEV EQHEVNGNLW HFRYPLEGET FDPENPKTFI TVATTRPETM LGDTAVAVHP
     DDERYRHLVG KNVVLPIVGR KIPVVADEYS DPEKGSGAVK ITPAHDFNDF EVGKRHKLPA
     INILTVEAAI KLKDNEDFLA GLDATPERQA VWDELDGLDR FVARKKIVEL MEEGGFLEKV
     EPHRHAVPHG DRGGVPIEPF LTEQWYANAA ELAKPAIASV REGRTNFVPK NWEKTYFDWM
     ENIQPWCISR QLWWGHQIPA WYGPDGRVFV EKTEEEALSA AIEYYLALEG PWKAWVEDRL
     ENFQPGEILT RDEDVLDTWF SSALWPFSTL GWPDQTPELK TYYQTDVLVT GFDIIFFWVA
     RMMMMGLHFM DEEPFHTVYV HALVRDKNGA KMSKSKGNVI DPLDLIDEYG ADALRFTLTV
     MAAQGRDVKL DPARIAGYRN FGTKLWNATR FAEMNEVARN DDFWLNDAKL AVNRWILTEL
     TRAARQITDG ITSYRFNEAA GAAYRFVWNL FCDWYLELLK PVFMGTDEAA KAESRACVAF
     VLDEIYKLLH PMMPFMTEEL WAQTAGEGKE RESLLCHAAW PSPDFEDDEA AADINWLVDL
     VSGIRSVRSE MNVPPAAIAP LVVVGANGVT RERLVRQDSA IKRLARVGDI SLADAAPKGS
     AQIVLNEATI CLPLGSLIDL AAEAARLQKE LAKVTEEIAR LHKKLSNERF VASAPAEIVE
     AEREKLAEYR DAQDKLAVAL TRVRDAG