SYV_STAAE
ID SYV_STAAE Reviewed; 876 AA.
AC A6QHJ8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=NWMN_1558;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
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; AP009351; BAF67830.1; -; Genomic_DNA.
DR RefSeq; WP_000425353.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QHJ8; -.
DR SMR; A6QHJ8; -.
DR EnsemblBacteria; BAF67830; BAF67830; NWMN_1558.
DR KEGG; sae:NWMN_1558; -.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000006386; 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; 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..876
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000073717"
FT COILED 805..876
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 520..524
FT /note="'KMSKS' region"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 876 AA; 101724 MW; F7629339DD15155D CRC64;
MEMKPKYDPR EVEAGRYEEW VKNGYFKPSE DKSKETYTIV IPPPNVTGKL HLGHAWDTTL
QDIITRMKRM QGYDTLYLPG MDHAGIATQA KVEAKLNEQG ITRYDLGREK FLEQAWDWKE
EYASFIRAQW AKLGLGLDYS RERFTLDEGL SKAVKKVFVD LYNKGIIYRG ERIINWDPKA
RTALSDIEVI HEDVQGAFYH FKYPYADGEG FIEIATTRPE TMLGDTAIVV NPNDERYKDV
IGKTVILPIV GRELPILADE YVDIDFGSGA MKVTPAHDPN DFEIGQRHQL ENIIVMDENG
KMNDKAGKYE GMDRFDCRKQ LVKDLKEQDL VIKIEDHVHS VGHSERSGAV VEPYLSTQWF
VRMEDLAKRS LDNQKTDDRI DFYPQRFEHT FNQWMENIRD WTISRQLWWG HQIPAWYHKE
TGEIYVGEEA PTDIENWQQD EDVLDTWFSS ALWPFSTLGW PDLESEDFKR YYPTNALVTG
YDIIFFWVAR MIFQGLEFTD RRPFNDVLLH GLVRAEDGRK MSKSLGNGVD PMDVIDEYGA
DSLRYFLATG SSPGHDLRYS TEKVESVWNF INKIWNGARF SLMNIGEDFK VEDIDLSGNL
SLADKWILTR LNETIATVTD LSDKYEFGEV GRALYNFIWD DFCDWYIEMS KIPMNSNDEE
QKQVTRSVLS YTLDNIMRML HPFMPFVTEK IWQSLPHEGD TIVKASWPEV RESLIFEESK
QTMQQLVEII KSVRQSRVEV NTPLSKEIPI LIQAKDKEIE TTLSQNKDYL IKFCNPSTLN
ISTDVEIPEK AMTSVVIAGK VVLPLEGLID MDKEISRLEK ELAKLQSELD RVDKKLSNEN
FVSKAPEKVI NEEKRKKQDY QEKYDGVKAR IEQLKA
