SYV_LARHH
ID SYV_LARHH Reviewed; 937 AA.
AC C1D6J9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=LHK_01113;
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Laribacter.
OX NCBI_TaxID=557598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9;
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO74105.1; -; Genomic_DNA.
DR RefSeq; WP_012696595.1; NC_012559.1.
DR AlphaFoldDB; C1D6J9; -.
DR SMR; C1D6J9; -.
DR STRING; 557598.LHK_01113; -.
DR PRIDE; C1D6J9; -.
DR EnsemblBacteria; ACO74105; ACO74105; LHK_01113.
DR KEGG; lhk:LHK_01113; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002010; 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; Reference proteome.
FT CHAIN 1..937
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000189241"
FT COILED 874..937
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 548..552
FT /note="'KMSKS' region"
FT BINDING 551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 937 AA; 104928 MW; 3D57FE5FE96AF11D CRC64;
MELAKSFEPG NIENRWYDRW EAAGYFKPSM DTDRPSFCIQ LPPPNVTGTL HMGHAFNQTI
MDGLTRYYRM KGDNTLWVPG ADHAGIATQI VVERQLAEQG VSRHDLGRDT FIGKVWEWKE
KSGGTITSQM RRVGCSVDWD KEYFTMDDKM STAVTEVFVR LYEQGLIYRG KRLVNWDPKL
GTAVSDLEVI SEEEDGKMWH IRYPVVGSDD VVVVATTRPE TLLGDVAVAV NPDDERYRHL
VGKQLELPLT GRTIPVIADD YVDAAFGTGF VKITPAHDFN DYQVGKRHNT ALINVMSLDA
TMLAKAQVFG FDGSAQGSID LPAAYAGLST ADARKAMLAD LDAAGLLVDT KPHKLMVPRG
DRTGSVIEPL LTDQWFVAMT KVGEGDATGK SITQKAIDAV ESGEVRFVPE NWVNTYNQWM
NNIQDWCISR QLWWGHQIPA WYDEDGKAYV GRTLEEVQAK APGKTLRRDE DVLDTWFSSA
LVPFSSLGWP NETPELKAFV PSQVLVTGYE IIFFWVARMI MMTTHFLGKV PFKDVYIHGI
VRDHEGKKMS KSEGNVIDPV DLIDGIALPE LITKRTTGLR RPEKAPQIVK ATEKLFPEGI
PAYGTDALRF TMASYASLGR SVNFDFKRAE GYRNFCNKLW NATRFVMMNV EGKDCGQDES
LPLEYSFVDK WIISRLQELE AAVTEALDTY RFDMASQLIY EFVWNEYCDW YVELAKVQLA
NGNEAQQRAT RRTLVRVLEV ALRLTHPLMP FITEELWQTV APLANAKKTD SIMVAAWPVA
DMSKVDAEAC GRMTVFKELV NAIRNLRGEM NLGPSVKAPL FVEGPAAYAD FLPYARLLGR
LSDAAVVEKL PDADAPVAIA GEARLMLKVE IDKAAETARL TKEIGKAESD VEKLTAKLEK
PGYVDKAPAQ LVERDRAQLA DLTDKLAKLK AQLLKLA
