ID   SYV_LISMO               Reviewed;         883 AA.
AC   Q8Y6X9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=lmo1552;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591979; CAC99630.1; -; Genomic_DNA.
DR   PIR; AH1268; AH1268.
DR   RefSeq; NP_465077.1; NC_003210.1.
DR   RefSeq; WP_010989740.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y6X9; -.
DR   SMR; Q8Y6X9; -.
DR   STRING; 169963.lmo1552; -.
DR   PaxDb; Q8Y6X9; -.
DR   EnsemblBacteria; CAC99630; CAC99630; CAC99630.
DR   GeneID; 986904; -.
DR   KEGG; lmo:lmo1552; -.
DR   PATRIC; fig|169963.11.peg.1593; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_9; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; Q8Y6X9; -.
DR   BioCyc; LMON169963:LMO1552-MON; -.
DR   Proteomes; UP000000817; 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; -; 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; Reference proteome.
FT   CHAIN           1..883
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224500"
FT   COILED          811..847
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           527..531
FT                   /note="'KMSKS' region"
FT   BINDING         530
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   883 AA;  102093 MW;  B72EE805D2F3B270 CRC64;
     MTTEHNEINM PTKYEPSNVE AGKYKWWLEK EFFKAEGNTD KEPYSIVIPP PNVTGKLHLG
     HAWDTTLQDI ITRMKRMQGF DTLYLPGMDH AGIATQAKVE AKLKESNISR YDLGRENFVD
     KTWEWKEEYA EFIREQWEKL GLGLDYSRER FTLDDGLSDA VKKVFVTLYN KGLIYRGQYI
     INWDPEAKTA LSDIEVIHKD IEGSFYHLKY PLTDGSGYLE VATTRPETIP GDTAVAVHPK
     DERYQHLIGK TIMLPILNRE IPIVADEYVE REFGSGAVKI TPAHDPNDFE VGNRHNLPRI
     IVMHEDGTMN ENAGKYDGLD RFVARKEIIQ DFKDLGLFIK QEPHLHSVGH SERTGAVVEP
     YLSLQWFVKM EPLAAEALEL QKTENKVNFV PARFEKTYET WMDNIHDWCI SRQLWWGHRI
     PAWYHKETGE IYVGEKEPEN LSEWEQDEDV LDTWFSSALW PFSTMGWPDT ESPDFQHFFP
     TNTLVTGYDI IFFWVSRMIF QSVEFTGERP FKDTLIHGLV RDSEGRKMSK SLGNGVDPIE
     VIDKYGADSL RYTLATGSSP GQDLKFSYEK VESTWNFINK IWNASRFVLM NLDGMKYNEI
     DLSNVTEVSD KWILTRLNET IQAVTSLGEK YEFGEVGRTL YNFIWDDFCD WYIEIAKIPL
     YGEDEVAKQT TRSVLAYTLN ATMRLLHPFM PFVTEEIWQN LPHEGESITI AEWPKVNEQQ
     IDTKSSTAMA TLVEVIRAVR NIRSEVNTPL SKPIVLEIKP KDTTYKEILE QNISYIERFC
     NPEQVTISFD VEASKTAMTA VVSGAEIFIP LEALIDLNVE IARLEKELEK WNKEVARVQG
     KLNNERFISK APESVVAEER LKEKDYLDKK ASVLERIETL KEV