ID   SYV_ARCFU               Reviewed;         863 AA.
AC   O28059;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=AF_2224;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB89032.1; -; Genomic_DNA.
DR   PIR; H69527; H69527.
DR   RefSeq; WP_010879713.1; NC_000917.1.
DR   AlphaFoldDB; O28059; -.
DR   SMR; O28059; -.
DR   STRING; 224325.AF_2224; -.
DR   EnsemblBacteria; AAB89032; AAB89032; AF_2224.
DR   GeneID; 1485454; -.
DR   KEGG; afu:AF_2224; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; O28059; -.
DR   Proteomes; UP000002199; 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..863
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106248"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           517..521
FT                   /note="'KMSKS' region"
FT   BINDING         520
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   863 AA;  100444 MW;  3A6E2C1883AA3E10 CRC64;
     MEIRKDYDAH EVEEKWLKLW KDEMYYFDWN SEKPHYIIDT PPPYPTGSFH IGHALNWCII
     DFIARYKRMN GYEVMFPQGW DCHGLPTEVK VEEKYGIKKG DIPRDEFRRL CVEFTEENIA
     KMRETARRMG YSIDWSKEYI TMYPEYYSKT QLSFVRMYNK GLIYRDYHPV VFCPRCETTI
     ALAEIEYRQG KTKLNYIKFD DDVIIATTRP ELIPACVAIA VHPDDERNKH LIGKKVRVPT
     TPYEVEVIAD EEVDPEFGTG VVMICTFGDR QDVKWWKKHK LELRNIVGRD GRLNEKAGRY
     AGMTIPEARE AILEDLKKEG KLLKQVEIDH NVGTCWRCKT PVEIIPAEQW FVKVEKEKIL
     EAAKRIKWVP EHMYSRLESW VQSMEWDWVI SRQRIFATPI PAWYCKNCGE VVVAKEEWLP
     VDPTATQPPE PCPKCGSTEF RGETDVLDTW MDSSITPLMI CGWPSLKEYP THLRPQGHDI
     IRTWAFYTIL RSLALEGQIP WYEIVINGMV FGEDGRKMSK SLGNVIVPEE VVEKYGVDAL
     RQWAASGVIG DDIIFNWKDV IAASRFQQKF WSITRFTLMH ISDYTPSEED KKLLRDADRW
     ILSKLNRLVG EVRKHMDEYR FDEAIKAIRT FTWYEYADNY LEIVKNRLYS GSEEEKRAAK
     FVLSYALDVL TRLLAPITPF MAEECWSHFR EGSVHLQSYP VVEEEFLDER AEKAGEEIKE
     IVAAVRKFKH DKGLALNAPL KKLIVYSKLD GLDVRDIAGA TNSEVEIVTE MPEVRERVKE
     LKPKFAIIGP MFREKAKTLI KAVGSLSKEE KERLLKEGAI QVNLDGASVE VKAEWFEAVT
     EKSIEGREVE MLETANSVVF VEV