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   31-JAN-2018, entry version 42.
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};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val). {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
CC       aminoacylation and one for editing. The misactivated threonine is
CC       translocated from the active site to the editing site.
CC       {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; AE014074; AAM79880.1; -; Genomic_DNA.
DR   RefSeq; WP_011054774.1; NC_004070.1.
DR   ProteinModelPortal; P0DG64; -.
DR   SMR; P0DG64; -.
DR   EnsemblBacteria; AAM79880; AAM79880; SpyM3_1273.
DR   KEGG; spg:SpyM3_1273; -.
DR   HOGENOM; HOG000020093; -.
DR   KO; K01873; -.
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-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
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   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;
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       {ECO:0000255|HAMAP-Rule:MF_02004}.
FT   MOTIF        45     55       "HIGH" region.
FT   MOTIF       519    523       "KMSKS" region.
FT   BINDING     522    522       ATP. {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
//