ID   SYV_METBF               Reviewed;         869 AA.
AC   Q46B32;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=Mbar_A1976;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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   -!- 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; CP000099; AAZ70910.1; -; Genomic_DNA.
DR   RefSeq; WP_011306956.1; NC_007355.1.
DR   AlphaFoldDB; Q46B32; -.
DR   SMR; Q46B32; -.
DR   STRING; 269797.Mbar_A1976; -.
DR   EnsemblBacteria; AAZ70910; AAZ70910; Mbar_A1976.
DR   GeneID; 3627951; -.
DR   KEGG; mba:Mbar_A1976; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 4914at2157; -.
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.
FT   CHAIN           1..869
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224626"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           521..525
FT                   /note="'KMSKS' region"
FT   BINDING         524
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   869 AA;  98973 MW;  7FE0C7981E66E3BD CRC64;
     MTESEIPKEY NASEVEEKWM DKWDLSMYHF NWGEDPRPQY IIDTPPPYPT GNFHIGNALN
     WCYIDFVARY KRMRGYNVMF PQGWDCHGLP TEVKVEEIHG ITKNQVPRAE FRKMCRELTA
     GNIDKMRKTM LRLGFSVDWS NEFITMDPSY FVKTQKSFVR MYNKDYIYHE EHPVNWCPRC
     ETAIAFAEVE YETRQTKLNF VHFDKVDIAT TRPELMAACV AVAVNPEDKR YSQYVGQEIT
     VPLFGQKVTL IADEDVEPEF GTGAVMICTF GDKQDVRWWV KYELPLIKAI DKQGKMTKAA
     GKYEGLSIAE CREAVVADLK AAGFLYDQKP LEQNVGLCWR CDTPIEILSE PQWFVKIDND
     AILKAADEIK WYPEYMKVRL QNWTGTMEWD WCISRQRIFA TPIPIWHCKK CGEVMVAEES
     WLPIDPNEAA PKKACACGST EFEPETDVLD TWMDSSITAL HVTGWESEHD LRLPAQIRPQ
     GHDIIRTWAF YTILRSLALE GKRPWDSIVI NGMVLGPDGH KMSKSLGNVI SPEEVTTKYS
     ADAFRQWGAV GGSTGSDVMF RWKDVVSASR FLQKMWSIYR FSMSHLKGFG QEDAEKFQKD
     SLHIIDRWLL SKLNRLVDTA TKELDDYQFD STFKAIRGFA WEVLADNYLE LVKGRLYGDD
     PEGKRAAQYV LYRTTKTLSL LLAPFIPFFA EELYSRLSDE SVHTQAWPAV DESLINEEAE
     AAGELIKEIT GEVRRYKSEL GMALNAPLKK LEIYNADIDT GDIAGAANSK VELMEGAPSF
     EYVPVEVKPN MGILGPRFRK DAGAVVKALK AESPAAIEAQ AASGKITVNV DGKPIELEPE
     AVEIRKEVIS GGREVDVLEV RGAVVVIVR