ID   SYV_BIFLD               Reviewed;         911 AA.
AC   B3DU23;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=BLD_1197;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(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   -!- SUBUNIT: Monomer. {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; CP000605; ACD98642.1; -; Genomic_DNA.
DR   RefSeq; WP_010081039.1; NC_010816.1.
DR   AlphaFoldDB; B3DU23; -.
DR   SMR; B3DU23; -.
DR   EnsemblBacteria; ACD98642; ACD98642; BLD_1197.
DR   KEGG; blj:BLD_1197; -.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000002419; 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   Gene3D; 3.90.740.10; -; 1.
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; 2.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 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..911
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000189251"
FT   REGION          882..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT   MOTIF           599..603
FT                   /note="'KMSKS' region"
FT   BINDING         602
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   911 AA;  102143 MW;  23FC52758E68BF03 CRC64;
     MTEGKSIINA NLTPLPDKVG VDGLEDKWRA VWDEDGTYKF RNTRDRKAVY SIDTPPPTVS
     GSLHVGHVFS YTHTDVIARY KRMRGYDVFY PMGWDDNGLP TERRVQNYYG VRVDVSLPYD
     PDFKPPFEGT DGKKIDAKDQ VPISRKNFIE LCERLTAQDE KLFEALWRKL GLSIDWSQTY
     HTIGQHPQRV AQKAFLRNLA RGEAYQQDAP GLWDVTFQTA VAQAELESRE YPGFYHKVAF
     RFEDGTPIYI ETTRPELLAA CTSLIANPND ERYKQYFGQY VYSPLFKVKV PILAHPAAEM
     DKGAGIAMCC TFGDVTDVEW WRDLKLPTRP IIQRNGRIVM DTPDWIEDPA GREVFAETAG
     KTTFSARKII VDKLRESGDL DGEPTPTKRM TNFYEKGDKP LEIVTSRQWY LKNGGTDAKL
     NAELIERGKE LEFHPDFMRV RYENWVHGLN GDWLISRQRF FGVPFPLWYP VNASGEPDYD
     HPITPSEDRL PIDPTIDVPE GYDESQRDVP GGFTAEKDIM DTWATSSLTP QIVTHWAEPD
     EASKALFAST FPMDLRPQGQ DIIRTWLFST VDRAHLENKC LPWAHATLSG WILDPDHKKM
     SKSKGNVVVP NEPIEKFGAD AVRYWAAAAR LGLDATYDIG QMKIGRRLAI KLLNATKFAL
     AIGREDENHH VGAAAEAAWN PADVTEPLDR AAMAKLALVV RQATEALESY EHSKALEVIE
     SYFWQFCDDY IELVKNRAYG TPDEHGNVPS EKAVKSARTA LGLGLDAFAR LLAPYLPYAT
     EEVWSWMHAG SGSVHRTAWP VVDPYVEAAT GASPELLTWA GKAVEQLRKI KSEAKVSMKT
     PILSVALSAA SEGVEAIHAA LGDIAQAGRV VGKFDLVAKH AEESAAEDAP ETEVAVEASE
     LGEPPAKKPK H