ID   SYV_METJA               Reviewed;         878 AA.
AC   Q58413;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=MJ1007;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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   -!- 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; L77117; AAB99009.1; -; Genomic_DNA.
DR   PIR; F64425; F64425.
DR   RefSeq; WP_010870520.1; NC_000909.1.
DR   AlphaFoldDB; Q58413; -.
DR   SMR; Q58413; -.
DR   STRING; 243232.MJ_1007; -.
DR   PRIDE; Q58413; -.
DR   EnsemblBacteria; AAB99009; AAB99009; MJ_1007.
DR   GeneID; 1451904; -.
DR   KEGG; mja:MJ_1007; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   InParanoid; Q58413; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; Q58413; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
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..878
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106249"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           527..531
FT                   /note="'KMSKS' region"
FT   BINDING         530
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   878 AA;  102572 MW;  4D78BCA0D1F2022E CRC64;
     MEMPKDYNIE IEKQIQKKWE ESKIYKFDEE SNKPPYIIDT PPPYPTGRLH LGHALNWTYM
     DIIARYKRMK GFNVLFPQGW DCHGLPTEVK VEEIHGITKS DVDRHKFREL CIELTKENIE
     KMRRQIKSLG ISIDWDKEYI TMTPEYIKKS QTAFVRMYKD GLIYRGKFPV NWCPRCQTAI
     AFAEVEYKER ESKLNYIKFP AADGEGHLLI ATTRPELMAA CVAILVHPED ERYKHLIGKE
     FIVPLFGHKV KLLADEDVEK EFGTGAVMVC TFGDKTDVLW VNRHKLEIKK AIDEKGELTE
     IAGKYKGLKT EEAREKIIED LKKEGYLVKQ EPIKQNVGVC WRCKTPIEII VTEQWFVNVR
     KLIPKVREVA DEIKWIPEHM KIRLLNWIED MDWDWVISRQ RIFATPIPVW YCPKCGNVVV
     AKEEDLPIDP TKTGYVCDKC GNKDLIPETD VLDTWMDSSI TPMVITKWLD DDKFFEKHYP
     VQLRPQGHDI IRTWAFYTIV KSVALTGKKP WDEIVINGMV FGEDGHKMSK SRGNVVEPDE
     IIAKYGADAL RLWASNSVVG DDVQFLWKEV DYGYRFLRKS WNACRFAKMH ISDDIIDELK
     KPMEISNPID LWILSKLQRL IERVDKDLEN YRFNTIVEIY KFVWHEFCDN YIEMVKYRLY
     GDDEEAKKEA RWTLYYVIDK VVRLLCPFAP HFSDYIAEIY KIDNLHFSFP EVDNRFINEE
     AEKFGEIAKN TVISIRRFKA NSGMALNAPL KYVEIYTEDE ETYLALNKTA EDIKGTLKIE
     ELKIIKGKPA LESKIVEIIP DKSKIGPEFK KNAKAVMDLI KNADEETLEK IINEGLETEY
     GVIRKEHIKD VKRALFCEGE EVDSVDIEGV LAMAIIRK