ID   SYV_HAEPA               Reviewed;         378 AA.
AC   P36432;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
DE   Flags: Fragment;
GN   Name=valS;
OS   Haemophilus parainfluenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7514149; DOI=10.1016/0378-1119(94)90348-4;
RA   Kulakauskas S., Barsomian J.M., Lubys A., Roberts R.J., Wilson G.G.;
RT   "Organization and sequence of the HpaII restriction-modification system and
RT   adjacent genes.";
RL   Gene 142:9-15(1994).
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 (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000305}.
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DR   EMBL; L17342; AAA20479.1; -; Genomic_DNA.
DR   AlphaFoldDB; P36432; -.
DR   SMR; P36432; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           <1..378
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106226"
FT   COILED          307..377
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   378 AA;  42780 MW;  AFB54C7CB558C3D3 CRC64;
     DGISLEDLLE KRTGNMMQPQ LAEKIAKATR KEFVDGIAAH GTDALRFTLA ALASNGRDIN
     WDMKRLEGYR NFCNKLWNAS RFVLTNDKLD LSQGEIEFSV ADRWIQSEFN RTVESFRSAL
     SQYRFDLCAN AIYEFTWNQF CDWYLELTKP VFANGNAAQI RAASQTLVHV LEKLLRLAHP
     LIPFITEEIW QKVKGFVGIT ADSIMLQPFP QVEENGFDPE AEAEIEWLKE VIVAVRNIRA
     ESNIAPSKGL DLLFRNLSAE NAKILEKQTA LLKAMAKLDN VQVLAANETH ASVAKLVGNA
     ELLVPMAGFI NKEAELARLT KEIEKYQNEV KRIENKLSNE AFVAKAPKAV ITKEREKQAE
     YQSGLEKIQE QYKAIEAL