ID   SYV_BARHE               Reviewed;         907 AA.
AC   Q6G2V3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=BH10630;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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}.
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DR   EMBL; BX897699; CAF27854.1; -; Genomic_DNA.
DR   RefSeq; WP_011180924.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q6G2V3; -.
DR   SMR; Q6G2V3; -.
DR   STRING; 283166.BH10630; -.
DR   PaxDb; Q6G2V3; -.
DR   PRIDE; Q6G2V3; -.
DR   EnsemblBacteria; CAF27854; CAF27854; BH10630.
DR   GeneID; 64157273; -.
DR   KEGG; bhe:BH10630; -.
DR   eggNOG; COG0525; Bacteria.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000421; 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; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
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.
FT   CHAIN           1..907
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224440"
FT   COILED          838..870
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           554..558
FT                   /note="'KMSKS' region"
FT   BINDING         557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   907 AA;  103385 MW;  CA334E7F733CBCB3 CRC64;
     MLEKNYDAAS IEQRIAKKWE ARGAFKAGMG SKSAAQSFCV MLPPPNVTGS LHMGHALNTT
     IQDIVVRFQR MRGKNVLWQP GMDHAGIATQ MVVERQLAER QEPTRQEMGR EKFVERIWEW
     RYETGGVIAN QLRRLGVSCD WSRERFTMDD GLSEAVREVF VTLYKQGLIY RDKRLVNWDP
     KLLTAISDLE VEQKEVKGHL WHFRYPLEGK LFDPSDATTF ITVATTRPET MLGDTGIAVN
     PEDDRYRNLI GQNAILPLVG RRLSIVADAY ANPDEGSGAV KITPAHDFND FEVGRRNNLR
     LINIFTEKAE VFLHENEAFF EGVVLSDALK MLVKDLDQKD RFIARDQIVS LMEEKGYLVT
     VDDHPHTVPY GDRSGVPIEP FLTDQWYVNA AELAKPAIEA VHQGKTQFIP DSWQKTYFNW
     MQNIQPWCVS RQLWWGHQIP AWYGPDGRVF VEKSEEEALN SALSHYGEVV NLTRDPDVLD
     TWFSSALWPF STLGWPNKTP ELATFYPTSL SVTGFDIIFF WVARMMMMGL HFMGEVPFPT
     VYVHALVRDQ KGAKMSKSKG NIIDPLELID QYSADSLRFT LAIMAAQGRD VKLDPSRIAG
     YRNFATKLWN ATRFAQMNGV KHDPDFKPEK AKLALNRWIL TELSKTVVAV TTGIENYKFN
     ESASALYRFI WNTLCDWYLE LLKPIFQGSN EDAKNEVQAC TAWVLDEVYK LLHPFMPHMT
     EELWSLTETL GMKREDMLAL IQWPEASFSD EEAASDINWL IDAVSAIRSV RFEMNIPAAA
     LAPLVIVEGG ELTLKRVELY ESLLKKLARV ETISFSDKAP ALSAQMILGE AIFCLPLGQL
     IDLEAERARL MKDVSKIEQD IEKLSAKLSN PKFIENAKPE IVEVERNRIV ELRTAQKKIS
     LALERLV