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 16-OCT-2013, entry version 17. DE RecName: Full=Valine--tRNA ligase; DE EC=6.1.1.9; DE AltName: Full=Valyl-tRNA synthetase; DE Short=ValRS; GN Name=valS; 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., RA Mammarella N.D., Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., RA Campbell D.S., Smith T.M., McCormick J.K., Leung D.Y.M., RA Schlievert P.M., Musser J.M.; RT "Genome sequence of a serotype M3 strain of group A Streptococcus: RT phage-encoded toxins, the high-virulence phenotype, and clone RT emergence."; RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002). CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As CC ValRS can inadvertently accommodate and process structurally CC similar amino acids such as threonine, to avoid such errors, it CC has a "posttransfer" editing activity that hydrolyzes mischarged CC Thr-tRNA(Val) in a tRNA-dependent manner (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate CC + L-valyl-tRNA(Val). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- DOMAIN: ValRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated threonine is CC translocated from the active site to the editing site (By CC similarity). CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for CC aminoacylation activity (By similarity). CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. ValS type 1 subfamily. 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; NP_665077.1; NC_004070.1. DR ProteinModelPortal; P0DG64; -. DR EnsemblBacteria; AAM79880; AAM79880; SpyM3_1273. DR GeneID; 1009588; -. DR KEGG; spg:SpyM3_1273; -. DR HOGENOM; HOG000020093; -. DR KO; K01873; -. DR OMA; MAGFINK; -. DR BioCyc; SPYO198466:GJDL-1335-MONOMER; -. 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-HAMAP. DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC. DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. 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; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR010978; tRNA-bd_arm. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd. DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR002303; Valyl-tRNA_ligase. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 2. 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; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis. FT CHAIN 1 882 Valine--tRNA ligase. FT /FTId=PRO_0000224579. FT COILED 808 882 Potential. FT MOTIF 45 55 "HIGH" region. FT MOTIF 519 523 "KMSKS" region. FT BINDING 522 522 ATP (By similarity). 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 //