ID SYV_STRP3 Reviewed; 882 AA. AC P0DG64; Q79XX8; Q8K6M9; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 1. DT 25-MAY-2022, entry version 53. 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=SpyM3_1273; OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=198466; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-595 / MGAS315; RX PubMed=12122206; DOI=10.1073/pnas.152298499; RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D., RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S., RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.; RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage- RT encoded toxins, the high-virulence phenotype, and clone emergence."; RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002). 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; AE014074; AAM79880.1; -; Genomic_DNA. DR RefSeq; WP_011054774.1; NC_004070.1. DR AlphaFoldDB; P0DG64; -. DR SMR; P0DG64; -. DR EnsemblBacteria; AAM79880; AAM79880; SpyM3_1273. DR KEGG; spg:SpyM3_1273; -. DR HOGENOM; CLU_001493_0_2_9; -. DR OMA; FATKLWN; -. DR Proteomes; UP000000564; 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; -; 3. 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. FT CHAIN 1..882 FT /note="Valine--tRNA ligase" FT /id="PRO_0000224579" FT COILED 808..882 FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004" FT MOTIF 45..55 FT /note="'HIGH' region" FT MOTIF 519..523 FT /note="'KMSKS' region" FT BINDING 522 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004" SQ SEQUENCE 882 AA; 100802 MW; 3DF3C1AFCAB07EA9 CRC64; MTELSPKYNP AEVEAGRYQK WLDADVFKPS GDQKAKPYSI VIPPPNVTGK LHLGHAWDTT LQDIIIRQKR MQGFDTLWLP GMDHAGIATQ AKVEERLRGQ GITRYDLGRE KFLDKVWEWK DEYATTIKEQ WGKMGLSVDY SRERFTLDEG LSKAVRKVFV DLYKKGWIYR GEFIINWDPA ARTALSDIEV IHKDVEGAFY HMNYMLEDGS RALQVATTRP ETMFGDVAVA VNPEDPRYKD LIGKHVILPI VNKLIPIVGD EHADPEFGTG VVKITPAHDP NDFEVGQRHN LPQVNVMNDD GTMNELAGDF AGMDRFEARQ ATVAKLEELG ALVNIEKRVH SVGHSERSGA VVEPRLSTQW FVKMDELAKQ AMDNQETDDR VDFYPPRFND TFLQWMENVH DWVISRQLWW GHQIPAWYNA EGEIYVGEEA PEGDGWTQDE DVLDTWFSSA LWPFSTMGWP DTDVEDFKRY FPTSTLVTGY DIIFFWVSRM IFQTLEFTGR QPFQNVLIHG LIRDEEGRKM SKSLGNGIDP MDVIEKYGAD SLRWFLSNGS APGQDVRFSY EKMDASWNFI NKIWNISRYI LMNNEGLTLE EAESNVAKVA ASEAGNVTDQ WILHNLNETI AKVTENFDKF EFGVAGHILY NFIWEEFANW YVELTKEVLY SDNEAEKVIT RSVLLYTLDK ILRLLHPIMP FVTEEIYAQY AQGSIVTAAY PTVTPAFENE AAHKGVESLK DLIRAVRNAR AEVNVAPSKP ITILVKTADS ELEDFFTSNV NYIKRFTNPE KLEISSAIAA PELAMTSIIT GAEIYLPLAD LLNVEEELAR LDKELAKWQK ELDMVGKKLG NERFVANAKP EVVQKEKDKQ ADYQAKYDAT QERIAEMQKL VK //