ID   SYV_PHOLL               Reviewed;         965 AA.
AC   Q7MZ25;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=plu4483;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571874; CAE16855.1; -; Genomic_DNA.
DR   RefSeq; WP_011148564.1; NC_005126.1.
DR   AlphaFoldDB; Q7MZ25; -.
DR   SMR; Q7MZ25; -.
DR   STRING; 243265.plu4483; -.
DR   EnsemblBacteria; CAE16855; CAE16855; plu4483.
DR   GeneID; 24169181; -.
DR   KEGG; plu:plu4483; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; PLUM243265:PLU_RS22125-MON; -.
DR   Proteomes; UP000002514; 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; -; 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..965
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224528"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          893..960
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           568..572
FT                   /note="'KMSKS' region"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         571
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   965 AA;  109990 MW;  257E93DDB1F3643B CRC64;
     MEKTPATQTQ AEPSLDKTYN PKEIEQPLYN HWEKSGYFKP NGDTSRESFC IVIPPPNVTG
     SLHMGHAFQQ TIMDTMIRYQ RMQGKNTLWQ SGTDHAGIAT QMVVERKIAA EEGKTRHDYG
     REAFIDKIWQ WKAESGGTIT NQMRRLGNSV DWERERFTMD EGLSNAVKEA FVRLYQENLI
     YRGKRLVNWD PKLHTAISDL EVENREVKGS MWHLRYPLAD GVTTAEGKDY LIVATTRPET
     MLGDTGVAVN PEDPRYKDLI GKEIILPLIN RRIPIIGDEH ADMEKGTGCV KITPAHDFND
     YEVGKRHALP MINIMTFDGN IRHKAEVFDT HGEISDSYSS DIPAEYQGIE RFAARKTIVA
     EFERLGLLVE IKAHDLTVPY GDRGGVVIEP MLTDQWYVRT APLAKVAIEA VENGDIQFVP
     KQYENMYYSW MRDIQDWCIS RQLWWGHRIP AWYDTNGNVY VGRSEEEVRR ENNLGTDISL
     NQDEDVLDTW FSSGLWTFST LGWPEQTDAL KTFHPTDVLV SGFDIIFFWI ARMIMMTMHF
     IKDENGKPQV PFKTVYMTGL IRDEEGQKMS KSKGNVIDPL DMVDGISLEE LLEKRTGNMM
     QPQLAEKIRK RTEKQFPAGI ETHGTDALRF TLAALASTGR DINWDMKRLQ GYRNFCNKLW
     NASRFVLMNT EGQDCGQHGG EMALSLADRW ILAEFNQTVK AYREALDTYR FDMAANILYE
     FTWNQFCDWY LELSKPAINK GSEAEVRGAR HTLIEVLEGL LRLAHPIIPF ITETIWQRVK
     IVKGIEADTI MLQPFPEFAQ EKTDELALTD LEWIKEAIIA VRNIRAEMNI APGKPLEVLL
     RNADAGAQRR VAENLNFIQA MGRLSSVTLL STDEEAPISV TKLINGAEVL IPMAGLVDKE
     AELSRLNKEI EKLDKEIGAI EGKLSNEGFV SRAPEAVVTK ERERLANCNT SKEKLLAQKE
     TIAAL