SYV_TROW8
ID SYV_TROW8 Reviewed; 856 AA.
AC Q83I17;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=TW286;
OS Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=218496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW08/27;
RX PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA Relman D.A.;
RT "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT Tropheryma whipplei.";
RL Lancet 361:637-644(2003).
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_02005}.
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_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; BX251410; CAD66960.1; -; Genomic_DNA.
DR RefSeq; WP_011096240.1; NC_004551.1.
DR AlphaFoldDB; Q83I17; -.
DR SMR; Q83I17; -.
DR GeneID; 67388062; -.
DR KEGG; tws:TW286; -.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OMA; RQWYIRN; -.
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; 3.40.50.620; -; 2.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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 PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..856
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224617"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 578..582
FT /note="'KMSKS' region"
FT BINDING 581
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 856 AA; 97596 MW; 3B76B698D670FE1B CRC64;
MNIPDKPSLE GLEEKWSKLW KSSKIYNFEL EQVSAKQDVY SIDTPPPTAS GVLHIGHVFS
YTHTDIIARF QRMQGKIVFY PMGWDDNGLP TERRVQNYFS VRCDPSLPYC QNLKLAQINN
DSMARSISRR NFIELCQQLS EEDERKFEEL WNYLGLSVDW SQTYRTIDDD AIHLSQHFFL
ENVNSGAAYQ DWAPTLWDVT YRTAVAQAEI EERQITGFYY RLAFENENAT VEIETTRPEL
LAGCVALVAH PDDNRYKHLF GSHVITPVFD VKVPVLPHRA AQPDKGSGIA MVCTFGDITD
VQWWRDLNLQ SCPIIDASGR VVPDAPDPIV SERGRRAFAT LSGKTLSAAK KHTLEMLISE
KSIIGEPRKI THPVKFFEKG DKPLEILLTR QWYIRNGYSD NALTERLIEL GKQLQWYPKT
MLRRYEDWLT GLNSDWLISR QRFLGVPFPI WYQTDDRGNA KFDDPIFPDR KDLPLDPTIA
VPRGYSENQR GAPNGFVAET DVMDTWATSS LTPQLAGKYL KNPKLFEAIF PYSLRPQGQD
IIRTWLFSSI IRSEYAHATA PWKSTAISGF ILDPDRKKMS KSKGNAKTPK DILDRYGADA
VRYWAACARL GVDTALDVEN PTQIKIGRRL ALKVLNAARF VVHLHKNKET YSGQPDMKRC
YPIDFAAISN PLDLSLLKQL DQTIEQSTNA LKNFDHSKAL DTTETFFWNF CDNYVEIVKD
RAYAGDESAL TTLLVVTNIV IKLLAPFIPY ATEEAWSWFN ETSVHTQSWP ETLKLHSGDI
ELLKIACSFM SLVRGGKTEA KLSQKTEIAY LKIALPNPEI IMPIMDDLRR AGKIDKCELI
DGDAQILAIE YGEISR