ID   SYV_NEIMA               Reviewed;         945 AA.
AC   Q9JX22; A1INV6;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=NMA0094;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(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}.
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; AL157959; CAM07413.1; -; Genomic_DNA.
DR   PIR; E82001; E82001.
DR   RefSeq; WP_002245792.1; NC_003116.1.
DR   AlphaFoldDB; Q9JX22; -.
DR   SMR; Q9JX22; -.
DR   EnsemblBacteria; CAM07413; CAM07413; NMA0094.
DR   KEGG; nma:NMA0094; -.
DR   HOGENOM; CLU_001493_0_2_4; -.
DR   OMA; FATKLWN; -.
DR   BioCyc; NMEN122587:NMA_RS00495-MON; -.
DR   Proteomes; UP000000626; 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.
FT   CHAIN           1..945
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106234"
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;  106889 MW;  9BC88C8E7F649248 CRC64;
     MLDKYSPAEI 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 LVNVFDLEAK
     VLANAEVFNF KGEAQPSFAL PEKYAGLDRF AARKQMVADL QEQGFLVEIK AHTLMTPKGD
     RTGSVIEPML TSQWFVAMSA TPNGGEPDSE FKGLSLADKA KKAVDSGAVR FIPENWVNTY
     NQWMNNIQDW CISRQLWWGH QIPAWYDNEG NVYVARNQEE AEKQAGKTGL TREEDVLDTW
     FSSALVPFST LGWPSETDEL KAFLPSNVLV TGYEIIFFWV ARMIMMTTHF TGKVPFKDVY
     IHGIVRDHEG KKMSKSEGNV IDPVDLIDGI DLEKLLVKRT TGLRKPETAP KVEEASRKLF
     PEGIPSMGAD ALRFTMASYA SLGRSVNFDF KRAEGYRNFC NKIWNATNFV LMNTENQDCG
     YGATATEPRG YSFPDMWIVD RLNQTIEQVT QAYETYRFDL AAETLYSFMW NDYCDWYLEL
     AKVQLQTGCA SRQRATRHTL LRVLEAALRL LHPIIPFITE ELWQTVAPMC DAKTADSIML
     ARFPEADSGE IVQTAFEQMT VLQDLIGAVR NLRGEMGIQP NVKAPLFVES TDDLADYLKY
     LPMMTRLTEA QQVATLPESE DAPVAVCNGA RLMLKVEIDK ATETARLSKE AEKLQKALDK
     LNAKLSKPGY TEKAPAHLVE KDKADLAELE DKMAKVQTQL SKLKD