ID   SYV_NEIMB               Reviewed;         945 AA.
AC   Q9K1H7;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=NMB0174;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF40631.1; -; Genomic_DNA.
DR   PIR; F81230; F81230.
DR   RefSeq; NP_273232.1; NC_003112.2.
DR   RefSeq; WP_002224777.1; NC_003112.2.
DR   AlphaFoldDB; Q9K1H7; -.
DR   SMR; Q9K1H7; -.
DR   STRING; 122586.NMB0174; -.
DR   PaxDb; Q9K1H7; -.
DR   EnsemblBacteria; AAF40631; AAF40631; NMB0174.
DR   KEGG; nme:NMB0174; -.
DR   PATRIC; fig|122586.8.peg.216; -.
DR   HOGENOM; CLU_001493_0_2_4; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000425; 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   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..945
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106235"
FT   COILED          879..945
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           552..556
FT                   /note="'KMSKS' region"
FT   BINDING         555
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   945 AA;  106685 MW;  B29FB68AE37DC38F CRC64;
     MLDKYNPAEI ESKHYQNWEE QGYFQPDMDL TKPSFSIQLP PPNVTGTLHM GHAFNQTIMD
     GLTRYYRMKG CNTAWIPGTD HAGIATQIVV ERQLAAQNVS RHDLGREKFL EKVWEWKEVS
     GGTITQQMRR VGCSADWTRE YFTMDDVRAE TVTEVFVRLY EQGLIYRGKR LVNWDPVLGT
     AVSDLEVESV EEQGSMWHIR YPLADNPAEA VIVATTRPET LLGDVAVAVN PEDERYTHLI
     GKELILPLTG RTIPVIADEY VEKDFGTGCV KITPAHDFND YEVGKRHDTR LINVFNLEAK
     VLANAEVFNF KGEAQLGFAL PEKYAGLDRF AARKQMVADL QEQGFLVEIK PHTLMTPKGD
     RTGSVIEPML TSQWFVAMSA TPNGGEPDSE FKGLSLADKA KKAVDSGAVR FIPENWVNTY
     NQWMNNIQDW CISRQLWWGH QIPAWYDNEG NVYVARNQEE AEKQAGKTGL TREEDVLDTW
     FSSALVPFST LGWPSETDEL KAFLPSNVLV TGYEIIFFWV ARMIMMTTHF TGKVPFKDVY
     IHGIVRDHEG KKMSKSEGNV IDPVDLIDGI GLEKLLVKRT TGLRKPETAP KVEEATKKLF
     PEGIPSMGAD ALRFTMASYA SLGRSVNFDF KRAEGYRNFC NKIWNATNFV LMNTENQDCG
     YGATAAEPRG YSFPDMWIVG RLNQTIEQVT QAYETYRFDL AAETLYSFVW NDYCDWYLEL
     AKVQLQTGCA SRQRATRHTL LRVLEAALRL LHPIIPFITE ELWQTVAPMC DAKTADSIML
     ARFPEADSGE IVQTAFEQMT VLQDLIGAVR NLRGEMGIQP NVKAPLFVES TDDLADYLKY
     LPMMTRLTEA QQVAALPESE DAPVAVCNGA RLMLKVEIDK AAETARLSKE AEKLQKALDK
     LNAKLSKPGY TEKAPAHLVE KDKADLAELE DKMAKVQNQL AKLKD