ID   SYV_AZOSB               Reviewed;         998 AA.
AC   A1K9L8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=azo2907;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(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; AM406670; CAL95523.1; -; Genomic_DNA.
DR   RefSeq; WP_011766633.1; NC_008702.1.
DR   AlphaFoldDB; A1K9L8; -.
DR   SMR; A1K9L8; -.
DR   STRING; 62928.azo2907; -.
DR   EnsemblBacteria; CAL95523; CAL95523; azo2907.
DR   KEGG; azo:azo2907; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_4; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002588; 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..998
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000022163"
FT   COILED          455..486
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   COILED          929..989
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           597..601
FT                   /note="'KMSKS' region"
FT   BINDING         600
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   998 AA;  112276 MW;  E094580C3CFAB664 CRC64;
     MELAKSFEPA AIEARRYPEW ESRGYFDAGL DTSNPNAFCI LLPPPNVTGT LHMGHGFNQT
     IMDALTRYHR MRGDNTLWQP GTDHAGIATQ IVVERQLDAQ GVSRHDLGRE KFLEKVWEWK
     EYSGGTITRQ MRRLGTSPDW KRERFTMDEG LSKTVTETFV RLYNEGLIYR GKRLVNWDPK
     LGTAVSDLEV VSEEEDGKLY HILYPFSDGP VGDLRGLTVA TTRPETLLGD VAVMVHPEDE
     RYAHLIGKTV ALPLTGRHIP IIADDYVDRE FGTGCVKVTP AHDFNDYAVG QRHQLDMIVV
     LKLDGSVPAV AERYTTDGQP REGVAMPAGV AGLDRVPARD KVVAELEALG LMLEIKAHKL
     QVPRGDRTNV VIEPMLTDQW FVAMSKPGAD GKSITAKALE VVASGEIKFY PENWVNTYNQ
     WLNNIQDWCI SRQLWWGHRI PAWYDDEGRI YVAANEEAAL HAWKADLEAE IARLQGEVQS
     RQSQGQTAEQ YPDLAERLSV LHARYEEGTL RQEEDVLDTW YSSALWPFST LDWTPEWPQK
     SNPALDLYLP STVLVTGFDI IFFWVARMVM MTKHITGKIP FKHVYVHGLI RDAEGQKMSK
     SKGNVLDPID LIDGIGIDEL VQKRTFGLMN PKQAQSIEKK TRKEFPEGIP AFGTDALRFT
     FASLASPGRD IKFDLARCEG YRNFCNKLWN ATRFVLMNCE GQDCGMDPHE PGTCVPGGYL
     DFSFADRWIV SRLQRTEAEV AAQFEAYRFD LVARAVYEFV WDEYCDWYLE LAKVQIQTGT
     PEQQRATRRT LLRVLETVLR LAHPLIPFIT EELWETVAPL AGRKDADSIM LARYPQADMG
     RIDEASEAQV AELKALIYAC RNLRGEMNIS PAQRLPLVAA GNAELLGRYA PYLAGLAKLS
     EVEIVAEIGA DELAPVAVAG ETRLMLKVEI DIAAERERLT KEIARLEGEV AKAEGKLGNA
     SFVDRAPAAV VQQERDRLAG FKATLEQLRP QLAKLAGR