ID   SYV_XANCP               Reviewed;         944 AA.
AC   Q8PCR7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=XCC0646;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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_02004}.
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_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008922; AAM39962.1; -; Genomic_DNA.
DR   RefSeq; NP_636038.1; NC_003902.1.
DR   RefSeq; WP_011035888.1; NC_003902.1.
DR   AlphaFoldDB; Q8PCR7; -.
DR   SMR; Q8PCR7; -.
DR   STRING; 340.xcc-b100_3709; -.
DR   EnsemblBacteria; AAM39962; AAM39962; XCC0646.
DR   KEGG; xcc:XCC0646; -.
DR   PATRIC; fig|190485.4.peg.708; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 2.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 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; 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; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
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   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
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; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..944
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224599"
FT   COILED          878..944
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           550..554
FT                   /note="'KMSKS' region"
FT   BINDING         553
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   944 AA;  106095 MW;  73EA22380436B10D CRC64;
     MTQLASSYDP SSFESRLYAQ WESAGHFKPS GSGEPYTVLL PPPNVTGTLH MGHAFQQTLM
     DALVRYHRMR GYDTLWQVGT DHAGIATEMV VSRNLALEGK GETRDTLGRE GFIAKVWEWK
     AQSGDTIERQ MRRLGTSSDW SRSTFTMDPQ PSAAVTEAFV RWYEQGLIYR GQRLVNWDPV
     LKTAISDLEV ENVEEDGFLW SIRYPLADGV TYEHVEHDAD GVETLRETRD YLVVATTRPE
     TMLGDTAVMV HPDDARYATL HAAQIVLPLT GRLVPVITDD YVDRAFGTGV VKVTPAHDFN
     DYQVGVRHDL PLINLFTVTA AINDNAPERY RGLDRYDARK LVLSELEDLG LLVETKPHKL
     QVPRGDRTGQ VIEPYLTDQW FVKMDALAKR GLELVESGQV KFVPPNWINT YRHWMENIQD
     WCISRQLWWG HRIPAWFDEA GKCYVGHDEA QVRATHGLGA EVALHQDSDV LETWFSSQLW
     PFSTLGWPDA QAMDERGFAR YLPSSVLVTG FDIIFFWVAR MIMATDSFTG QVPFRDVYIT
     GLIRDAQGQK MSKSKGNVLD PLDIIDGISI EDLVAKRTSG LMQPRMAEKI EKATRKEFPD
     GIIAHGADAL RFTIAALATH GRDIKFDLGR AEGYKNFCNK LWNATRFALM NTEGAQFSGV
     PQPQTETERW ILARLDAVAA EAQAHYANYR FDLLAQTLYE FAWNAFCDWF VELAKPALNG
     AVQDAADSTR HTLLYVLEAL LRLLHPLTPF VTEELWQQVA PRLGITGDTI SLQAFPQRGD
     VDTSGYAGAE ADIEWLKAMV SALRRVRSEL NVPPSKQVRL WLQAGSSDDR ARVARFASQL
     AFLLKLEAID WLAAGQEAPP AAAAIVGELT LLVPLEGLVD MDAERTRLDK EIKRVENEIG
     KCNGKLGNAT FVQNAPAAVV EQERARLNDW TTQLTGLREQ RAKL