SYV_BORBU
ID SYV_BORBU Reviewed; 875 AA.
AC O51680;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=BB_0738;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; AE000783; AAC67078.1; -; Genomic_DNA.
DR PIR; A70192; A70192.
DR RefSeq; NP_212872.1; NC_001318.1.
DR RefSeq; WP_002657488.1; NC_001318.1.
DR AlphaFoldDB; O51680; -.
DR SMR; O51680; -.
DR STRING; 224326.BB_0738; -.
DR PRIDE; O51680; -.
DR EnsemblBacteria; AAC67078; AAC67078; BB_0738.
DR GeneID; 56567547; -.
DR KEGG; bbu:BB_0738; -.
DR PATRIC; fig|224326.49.peg.1129; -.
DR HOGENOM; CLU_001493_0_2_12; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001807; 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; Reference proteome.
FT CHAIN 1..875
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106215"
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; 101865 MW; D9EF63611A4BC77E CRC64;
MNCRPLEKYD PKAFEDEIYT KWLKNNVFLP DNSLFEKFSM VAPPPNVTGV LHMGHALNFV
LQDVLVRYKR MKRHNTLWLF GTDHAGIATQ AVFERHLKKI GKSKDDFERE ELVQEIFKLK
DRHRGIIVNQ INKLGASYDH SRERFTLDEN LCKAVNKVFK DLYFKGLIYR GEYLVNLDPG
SGSVVSDEEI EYKEVDGKLY FVKYFIDNSS FIEVATTRPE TMFGDTAIAV NPNDERYKSL
VGKEVTIPLT TKKIKVIADF YVDSAFGTGA LKVTPAHDPN DFEISKRHNI SKVNILTQDG
KLNKNVPLQY QGLSAKDARF KIETELMEKG FLQDVKKHKQ QVGHCYRSGE VIEPYLSTQW
FVRMKPLADK ALKALENGEL KFYPKKWENT YKYWLSNIRD WCISRQLVWG HRIPVWYNVD
TSELIVSDTD PSLDEKNMGK RFVQDPDVLD TWFSSWLWPF SSLGWPNVDV DFKNYYPTNT
LITAYDIIFF WVARMVMAGL EFTGQVPFKD VYITPLLRDK QGKKMSKSLG NGIDPLDIIN
EYGSDSLRFT LSFLSVQGQD LNIDAKDFMF GAKFANKVFN ASKFILLNLK NRKILNDLKF
NDIDKWLLTS LNSTILGVES SFANYKYNEA SKFVYEFFWN DFCDWYIEIS KIDLNNENVD
IQNMAISKLL FFLKKSLLIL HPFIPFVTEK IYSEFAEKED ILALNEYPNF DIANNFQEEF
EIFKVLKTFI IAIRTLKSEF NIPASVEIDV ALKFDADFKY EAYFKANESI VKRMINFKNI
FYNENYDGML GVAAVGFEIY ADVKSLIDKT KELIRLEKQL EKYKMLNISV SKKLENENFL
MNAPKEIVES EKLKFVEFSS LINKINNYII NLKNL
