SYV_STRP6
ID SYV_STRP6 Reviewed; 882 AA.
AC Q5XAW8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=M6_Spy1310;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(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; CP000003; AAT87445.1; -; Genomic_DNA.
DR RefSeq; WP_011184776.1; NC_006086.1.
DR AlphaFoldDB; Q5XAW8; -.
DR SMR; Q5XAW8; -.
DR EnsemblBacteria; AAT87445; AAT87445; M6_Spy1310.
DR KEGG; spa:M6_Spy1310; -.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001167; 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 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; 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..882
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224580"
FT COILED 808..877
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 /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 882 AA; 100976 MW; 5AE1E86DC005AB23 CRC64;
MTELSPKYNP AEVEAGRYQK WLDADVFKPS GDQKAKPYSI VIPPPNVTGK LHLGHAWDTT
LQDIIIRQKR MQGFDTLWLP GMDHAGIATQ AKVEERLREQ GISRYDLGRD KFLDKVWEWK
DEYATTIKEQ WGKMGLSVDY SRERFTLDEG LSKAVRKVFV DLYKKGWIYR GEFIINWDPA
ARTALSDIEV VHKDVEGAFY HMNYMLEDGS RALQVATTRP ETMFGDVAVA VNPEDPRYKD
LIGKHVLLPI VNKLIPIVGD EHADPEFGTG VVKITPAHDP NDFEVGQRHN LPQVNVMNDD
GTMNELAGDF AGMDRFEARQ ATVAKLEELG ALVNIEKRVH SVGHSERSGA VVEPRLSTQW
FVKMDELAKQ AMDNQETDDR VDFYPPRFND TFLQWMENVH DWVISRQLWW GHQIPAWYNA
EGEIYVGEEA PEGDGWTQDE DVLDTWFSSA LWPFSTMGWP DTDSEDFKRY FPTSTLVTGY
DIIFFWVSRM IFQSLEFTER QPFQNVLIHG LIRDEEGRKM SKSLGNGIDP MDVIEKYGAD
SLRWFLSNGS APGQDVRFSY EKMDASWNFI NKIWNISRYI LMNNEGLTLE EAESNVAKVA
ASEAGNVTDQ WILHNLNETI AKVTENFDKF EFGVAGHILY NFIWEEFANW YVELTKEVLY
SDNEAEKVIT RSVLLYTLDK ILRLLHPIMP FVTEEIYAQY AQGSIVTAAY PTVTPAFENE
AAHKGVESLK DFIRAVRNAR AEVNVAPSKP ITILVKTADS ELEDFFNSNI NYIKRFTNPE
KLEISSAIAA PELAMTSIIT GAEIYLPLAD LLNVEEELAR LDKELAKWQK ELDMVGKKLG
NERFVANAKP EVVQKEKDKQ ADYQAKYDAT QERIVEMHKL VK
