SYV_BORGP
ID SYV_BORGP Reviewed; 875 AA.
AC Q660D6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, 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=BG0759;
OS Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS PBi) (Borrelia bavariensis).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(2004).
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; CP000013; AAU07585.1; -; Genomic_DNA.
DR RefSeq; WP_011194033.1; NZ_CP028872.1.
DR AlphaFoldDB; Q660D6; -.
DR SMR; Q660D6; -.
DR STRING; 290434.BG0759; -.
DR EnsemblBacteria; AAU07585; AAU07585; BG0759.
DR KEGG; bga:BG0759; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_12; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002276; 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..875
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224448"
FT COILED 803..837
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 524..528
FT /note="'KMSKS' region"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 875 AA; 101703 MW; 2FAA45A56CDCD6CD CRC64;
MNFRLLEKYD PKAFEDEIYN KWLKNNVFLP NNSLFEKFSM VAPPPNVTGV LHMGHALNFV
LQDILVRYKR MKKHNTLWLF GTDHAGIATQ TVFERNLKNI GKSKNDFERE EFVKEIFKLK
DKHRGVIVNQ IKKLGASYDH SRERFTLDES LCKAVNKVFK DLYSKGLIYR GEYLVNLDPG
SGSVVSDEEI EYKEVDGKLY FVKYFIDDSS FIEIATTRPE TMFGDTAIAV NPNDERYKSL
VGKEVTIPLT TKKIKIIADF HVDSAFGTGA LKITPAHDPN DFEISKRHNI PKVNILTQDG
KLNENVPLQY QGLSIKDARF KIEIELMEKG FLKGVKKHRQ QVGHCYRSGE VIEPYLSTQW
FVSMKPLAEK ALKALESGEL RFYPKKWENT YKYWLSNIKD WCISRQLVWG HRIPAWYNID
TSELIISDTD PSLDEKNVGK RFVQDPDVLD TWFSSWLWPF SSLGWPNITV DFENYYPTKT
LITAYDIIFF WVARMVMAGL EFTGQTPFRD VYITPLLRDK QGKKMSKSLG NGIDPLDIIH
EYGSDSLRFT LSFLSVQGQD LNIDAKDFML GAKFANKVFN ASKFILLNLE NREIFNNLKF
NDIDKWLLTS LNSTILGVES SFANYKYNEA SKFVYEFFWN DFCDWYIEIS KIDLNSENVD
IQNMAISKLL FFLKKALLIL HPFIPFVTEK IYSEFSEKGD ILALNEYPSF DISSNFKEEF
ESFKVFKTFI VAVRTLKSEF NISSSIEIDV ALKFDSDFKY EGYFKANESI SKRMINFKNI
FYNENCDGML GLAVVGFEIY ADVKLLIDKT KELIRLEKQL EKYKMLKISV SKKLENENFL
MNAPKEIIES EKLKFVEFSS LINKINSYII NLKNL
