ID   SYV_NITWN               Reviewed;         952 AA.
AC   Q3SSP4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=Nwi_1436;
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX   PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA04697.1; -; Genomic_DNA.
DR   RefSeq; WP_011314705.1; NC_007406.1.
DR   AlphaFoldDB; Q3SSP4; -.
DR   SMR; Q3SSP4; -.
DR   STRING; 323098.Nwi_1436; -.
DR   EnsemblBacteria; ABA04697; ABA04697; Nwi_1436.
DR   KEGG; nwi:Nwi_1436; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002531; 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; -; 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..952
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224517"
FT   COILED          894..950
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           571..575
FT                   /note="'KMSKS' region"
FT   BINDING         574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   952 AA;  107385 MW;  94413800F10B093E CRC64;
     MIEKTYQPSD IESRMSRVWE EAGAFKAGRP ERREAEPFTI VIPPPNVTGS LHMGHALNNT
     LQDVLCRFER MRGRDVLWQP GTDHAGIATQ MVVERQLMER KEPGRREMGR ARFLERVWQW
     KAESGGVIVN QLKRLGASCD WSRERFTMDE GLSRAVAKVF VELHRAGLIY KDKRLVNWDP
     KLLTAISDLE VKQVEVKGSL WHLRYPIEGK AFDPSDPSTY IVVATTRPET MLGDTAVAVH
     PENAKLEYLI GSNVVLPLAG RIIPIVGDDY ADPEKGTGAV KITPAHDFND FEVGRRHHLP
     QISVLDREGR LTLSENEDFL RGLPSGALML AEEFDGMDRF AARKAIVARL EEFGFLDKIE
     PHTHMVPHGD RSNAVVEPYL TDQWYVDAKE LARPAMAAVR SGETAFVPKN WEKTYFEWME
     NIQPWCISRQ LWWGHQIPAW YGPDGKVFVA ETEDEAIGHA LGYYVEQGVI TAEQGAGMAR
     DPAKRDGFIT RDEDVLDTWF SSALWPFSTL GWPDETPEVR RYYPTNVLVT GFDIIFFWVA
     RMMMMGIHFM KEAPFSTVYI HALVRDEKGA KMSKSKGNVI DPLNLVDKYG ADALRFTLAA
     MAVQGRDIKL SPQRVEGYRN FATKFWNACR FAEMNDCVVP ARFDPTAATE TLNRWIVHET
     ARTACEVTEA IESSRFNDAA SAIYRFVWNV YCDWYLELAK PVILGEDSPA KSETRAMVAW
     ARDEILKLLH PFMPFITEEL WAVTAERTRL LTLTEWPNKA DQTRKRRTLI AAADPFIGSE
     PITDLLEPYF RDDAAEAEIG WVVDLVTAIR SVRAEMNIPP ATLAPLVLAG ASDESRARAQ
     RWSDVIKRMS RLADISFADQ APAGAVQLLI RGEVAALPLK GIVDVAAQRT RLGKEIAKAD
     ADIARVDLKL ADQNFIANAP GEIVEDEKEK REAAAARKAK FVEALERLKA AE