ID   SYV_LEGPH               Reviewed;         921 AA.
AC   Q5ZXL2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=lpg0719;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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; AE017354; AAU26808.1; -; Genomic_DNA.
DR   RefSeq; WP_010946456.1; NC_002942.5.
DR   RefSeq; YP_094755.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZXL2; -.
DR   SMR; Q5ZXL2; -.
DR   STRING; 272624.lpg0719; -.
DR   PaxDb; Q5ZXL2; -.
DR   PRIDE; Q5ZXL2; -.
DR   EnsemblBacteria; AAU26808; AAU26808; lpg0719.
DR   GeneID; 66489906; -.
DR   KEGG; lpn:lpg0719; -.
DR   PATRIC; fig|272624.6.peg.741; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000000609; 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   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..921
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224496"
FT   COILED          849..921
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           522..526
FT                   /note="'KMSKS' region"
FT   BINDING         525
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   921 AA;  106425 MW;  B8EAD8BC6D977E1F CRC64;
     MDKTYSPEAI EKALYKKWES HHYFQPRGEG KRFCIMLPPP NVTGSLHMGH GFQHTIMDAL
     TRYHRMLGDK TLWQPGTDHA GISTQLVVER QLEAQGVSRK DLTREQFLDK VWQWKEESGN
     TITQQMRRLG ASVDWSRERF TMDEGLSAAV QKVFVQLYEE GLIYRGTRLV NWDPKLGTAV
     SDLEVLSEEE DGFLWHIRYP VVDSEEFLIV ATTRPETLLG DCAVAIHPDD SRFRHLIGKQ
     VHLPLCDRTI PVIADDYVDK EFGSGCVKIT PAHDFNDHEV GKRHQLPQIN ILTKKGTINK
     NAPLKYQGMD RFVAREQIIK DLEKEGLLAK TEPHKLKVPR GEKSNVIIEP LLTDQWYVKT
     KPLAEPAIAA VKKGDIRFIP ETWDKTYFQW MDNIEDWCIS RQLWWGHRIP AWYDNHGNIY
     VGYSENDVRF KHKIDQSTPL KQDEDVLDTW FSSALWPFST LGWPERTPEL EQFYPTSVLV
     TGFDIIFFWV ARMIMMGLKF TGKIPFKEVF ITGLIRDSEG HKMSKSKGNV LDPLDIVDGI
     DLDSLIAKRT SNLMLNSVRD RITKATRKEF PEGISAYGTD ALRFTYCSLA STGRNVRFDL
     GRVEGYRNFC NKLWNAARYV LLNTDEEQID FGDGAFQYSP ADQWILSRLQ NTVSKVHHYF
     ETYRFDLLAN TLYEFVWHEY CDWYLELSKP ILQDDQALSA MKRGTRRTLI HVLDQILKLL
     HPLMPFITEE IWQKTTKFTS ENGISIMLST YPKVNEEFIN PAIEEELDWL KSAIQSLRTI
     RSEMSISPAK LIPLYIRNIT PELKERIAKY EKILKTLSKI DKINYLAPDE KVPVSATAVL
     GEIELLIPMA DLIDKEAELS RLNKELAKLN KDIELAQGKL NNPKFTDKAP EEIIAKEKDK
     LAQAQVAKDK LLQHKNRIES L