SYV_SYMTH
ID SYV_SYMTH Reviewed; 911 AA.
AC Q67SJ2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=STH366;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(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; AP006840; BAD39351.1; -; Genomic_DNA.
DR RefSeq; WP_011194500.1; NC_006177.1.
DR AlphaFoldDB; Q67SJ2; -.
DR SMR; Q67SJ2; -.
DR STRING; 292459.STH366; -.
DR PRIDE; Q67SJ2; -.
DR EnsemblBacteria; BAD39351; BAD39351; STH366.
DR KEGG; sth:STH366; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000417; 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; -; 2.
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; Reference proteome.
FT CHAIN 1..911
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224584"
FT COILED 845..910
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT MOTIF 533..537
FT /note="'KMSKS' region"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 911 AA; 103067 MW; FB05FF7210EF0EB9 CRC64;
MSAEQKQGGT ELAPRYDAKL VEDEYYQYWM DGGFYRAPIV EGKQPYTIVI PPPNVTGTLH
LGHALNNTMI DILIRWKRMQ GHPTLYLPGT DHAGLATQIR VEEDLRKSGG PTRHELGREA
FVAKVWDWKE RYHATITSQL RKLGVSVDWS REAFTMDERL SRAVRAFFVQ LYKKGLIYQG
TRITHWCPKD QTALSDIEVE YEERQGHMWH FRYPLADGSG SIVIATTRPE TMLGDTAVAV
NPEDERYKHL VGKMLRHPAT GREIPIIADE YVDPAFGTGC VKITPFHDPN DFEIGLRHGL
EMPQVIGPKG EMTEAAGKYA GLDRYECRRR IVADAEAEGW LVKVEEHQHA VGCCARCGTV
IEPLISRQWY VKMKPLAEPA IRAVESGQIK IVPERFTKVY LHWMENIQDW CISRQIWWGH
RIPVWYCDDC GHLTVSETDP TRCEKCGSAN IRQDEDALDT WFSSALWPFS TLGWPDDTAD
LRYFFPTDVL VTGYDILFFW VARMIFSSLE LTGKIPFHTV VLHGLVRDAQ GRKMSKSLGN
GVDPIDVIDQ YGTDALRFML VTGSSPGNDI RFHTERVENA RNFANKLWNA SRFVLMNLAD
WQPAAEGAAL QYDVADRWIR HRFNEAARAV NELLGEYQYG EAARTIYDFI WSEFCDWYIE
LVKPRLYNPA DPTRAAAQET LARVLEGTLR LLHPFMPYIT EAIWQKLPLR SPQVETAPEI
ARAAGRDALP PSISVTAYPT PVEGWADAEA NERMALIIDT IRALRSIRAE FRLGEHTRID
AVVMATSDQA LAILNEGRAF IENLGKTGQL TIQPVAEAKP KNAAAAVVTG AEIYVPLGGL
IDLPKEIERL TKELTTTGDE LAKLEKKLSN EGFLTKAKPE VVEKTREEAA ALAEKRQALE
NRLAMLRSMQ G
