ID   SYV_HALS3               Reviewed;         881 AA.
AC   B0R841;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=OE_4572R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP14910.1; -; Genomic_DNA.
DR   RefSeq; WP_010903904.1; NC_010364.1.
DR   AlphaFoldDB; B0R841; -.
DR   SMR; B0R841; -.
DR   EnsemblBacteria; CAP14910; CAP14910; OE_4572R.
DR   GeneID; 5954081; -.
DR   GeneID; 62885664; -.
DR   KEGG; hsl:OE_4572R; -.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; B0R841; -.
DR   Proteomes; UP000001321; 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.
FT   CHAIN           1..881
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000189253"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           528..532
FT                   /note="'KMSKS' region"
FT   BINDING         531
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   881 AA;  99196 MW;  9C83F900A70BE192 CRC64;
     MTELPDSYDP NSIEPKWQDE WQERDVYRFD PSESDTQYVI DTPPPYPSGN LHLGHALGWS
     YIDFVARYRR LKGDAVLFPQ GWDCHGLPTE VKVEEVNDIH RTDVPSDEFR EMCIDWTEDR
     IDEMKATMQE LGFSQDWDSE YRTMDPEYWG KTQESFSEMA DAGMVYRDEH PVNWCPRCET
     AIADAEVENI DREGTLHYVT FDGVDNGDIE IATTRPELLA ACVGIVVSPD DDRYADRIGD
     TFEVPLFGQD VELLADDDVD ADFGSGAVMV CTFGDKQDVE WWMDHDLDLR TVFTEDGHLN
     EAAGEFAGLA IDDAKTQVAE ELDDQGYLND TEPTEQSVGS CWRCDTAIEI LSKEQWFVEV
     DQDRILDAAA DAEWVPEHMH DRLVEWTEGM DWDWVISRQR VFATPIPAWE CNECGHWEIA
     GREQAPVDPT EDDPAVEACP ECGGDDWAGE TDVMDTWMDS SITPLHLSGW PEGTTLDEFE
     SVDLRPQGHD IIRTWAFYTL LRTGALTDEQ PWDDVLVNGM VFGEDGNKMS KSRGNFVQPD
     EAIAEYSADA VRQALALGGR PGSDVQFQWK EVKSASRFLT KLWNITKFST GHFDEDTPAI
     QDPAYRDADR WLLSELSTVC EDVDEAMSEY RFDRALRSLR EFAWEDLADD YVELVKGRLY
     NGRPGERAAA EHTLYTAVTA VTRLLAPFSP HTTEEIWQSL PGTEGSVHAA TFPSVEYRDA
     DAELAGKRIA EVAREIRAWK SDQGMPLNAD LDRVELYFDD SDDDAARLDT YDLSETVNAP
     IRLIDGRPDV ELVPVDVDGD DSEIGPEFRS DAGTVMEAIA AADPAAIQAQ IHSGDTVTVE
     ADGESFDLDA DWLTVTEEYR ASSGEEVTVI EASFGTVIIY E