ID   SYV_METTP               Reviewed;         855 AA.
AC   A0B7C2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Mthe_0807;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK14596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B7C2; -.
DR   SMR; A0B7C2; -.
DR   STRING; 349307.Mthe_0807; -.
DR   EnsemblBacteria; ABK14596; ABK14596; Mthe_0807.
DR   KEGG; mtp:Mthe_0807; -.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000674; 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..855
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000022180"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           522..526
FT                   /note="'KMSKS' region"
FT   BINDING         525
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   855 AA;  98487 MW;  0AFEFE084F09FDCE CRC64;
     MSEISKEYNF KEVEEKWIER WDPSVYYFDW GSEKPQYIID TPPPYPTGNF HIGNALNWCY
     IDFVARYKRM RGYNVMFPQG WDCHGLPTEV KVEETYHITK NQVPREEFRR LCEEMTAQAI
     ERMRRTITRL GISTDWSNEY ITMKPEYYVK TQRSFVQMYE KGMIYREDHP VNWCPRCATA
     IAFAEVEYDT RTTTLNYMRF ESDHGCLEIA TTRPELLPAC VAVAVNPNDE RHIGFVGKSV
     KVPLFDYEVP VLSDPAVDPS FGTGVVMICT FGDKQDVRWW VEHKLPLRQA IDREGRLTEI
     AGKFGGMSIT EAKKAIVDEM LSRGIIYRQE PLEQNVGLCW RCKTPIEILS ERQWFVRIYP
     DVIIKTADEI EWVPEHMKLR LKNWTGTMEW DWCISRQRVF ATPIPAWYCK RCGEVMVAKE
     EWLPLDPTKT QPPVSCSCGS NEFEPEEDVL DTWMDSSISA LHVTGWLSRE DPRYPAQLRP
     QGHDIIRTWA FYTILRSMAL VGVKPWETIL INGMVLGEDG RKMSKSLNNF VIPEEVFEKN
     GADALRQWAA LGGSPGSDVM FQWKEIVAAS RFQQKLWSIY RFAAPFASDT DAPFTQIDRW
     LLGELGMLVS KVTDAMEAFQ FDEAFRAIRA FTWEVLADDY IEIVKSRLYG PDSDERRAAQ
     ATLYRVLDVL CRLMAPFIPF ITEEIYTSLT GKSVHTQSWP SLETYTSPEG ALIREIAAAI
     RRYKSERGMA LNAPLSGIEI YTELELETFD LRGVANAPIQ LRKGQPEIES RAVAVKPVMR
     FIGPRYKDQA GKIIKKLTSM DPADVERMLA SGRVEIEGAE ITPEMVEIVR ETLSMGEAVD
     VLRLDRATLL IRRSS