(data stored in ACNUC30630 zone)

SWISSPROT: 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   11-DEC-2019, entry version 94.
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; 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}.
DR   EMBL; BX251410; CAD66960.1; -; Genomic_DNA.
DR   RefSeq; WP_011096240.1; NC_004551.1.
DR   EnsemblBacteria; CAD66960; CAD66960; TW286.
DR   KEGG; tws:TW286; -.
DR   HOGENOM; HOG000020095; -.
DR   KO; K01873; -.
DR   OMA; RQWYIRN; -.
DR   BioCyc; GCF_000196075:G1EE9-309-MONOMER; -.
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; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
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   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;
DR   PRODOM; Q83I17.
DR   SWISS-2DPAGE; Q83I17.
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                   /note="ATP"
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
//

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