SYV_METKA
ID SYV_METKA Reviewed; 914 AA.
AC Q8TVG5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=MK1424;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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 -!- 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; AE009439; AAM02637.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TVG5; -.
DR SMR; Q8TVG5; -.
DR STRING; 190192.MK1424; -.
DR PRIDE; Q8TVG5; -.
DR EnsemblBacteria; AAM02637; AAM02637; MK1424.
DR KEGG; mka:MK1424; -.
DR PATRIC; fig|190192.8.peg.1580; -.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001826; 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; 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 TIGRFAMs; TIGR00422; valS; 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; Reference proteome.
FT CHAIN 1..914
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224624"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 552..556
FT /note="'KMSKS' region"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 914 AA; 105317 MW; 3B24088E8E9DF06D CRC64;
MPGEAPVEDY DPKEIEPKWR ERWLEERKYR FEGGEDRPAF VIDTPPPYPT GELHMGHVLN
WTYMDVVARY KRMCGYDVFF PQGWDCHGLP TEVKVEEIHG ITKRDAPRRE FRKLCEELTL
ENIRKMREQL IQLGCSIDWW TDCIDYENEE LKELGSYVTM DPDYIRRSQY GFLELLEKGY
AYREEHPVNW CPRCETAIAF AEVEYVTRET YLNYIEFPVA DGDGSVTIAT TRPELLPACV
AVAVHPDDDR YSDLVGKKLV VPLHERFGDR DTPWEVPVIA DEEVDPEFGT GIVMICTFGD
KQDVAWVKRH DLPIVRAIDE QGKMTEVAGE FAGMEVEEAR AAIVEALKEE GYLVKREKIT
QNVGVCWRCK TPIEILVKEQ WFVKVRELAE DVKEAARKMV WIPEHMRKRL EDWTESMDWD
WCISRQRIFA TPIPVWYCKE CGEVIPAEKD QLPVDPTRDD PPVDECPKCG CSEFEPETDV
MDTWMDSSIT PLVITGWPDE EPDLPVDLRP QGHDIIRTWL YYTTVRALVH ADTEPFKEIL
INGMVFGEDG YKMSKSRGNV VEPTEVIEEY GADALRYWAV SSGAPGSDVQ YMTKTIKRGY
RFAKKIWNVC RLAKDHIDDA PSVEEVEGDL TPADRWILSK FHRLVDEVTE HLESGYRFND
AIKAIEEFAW EELADDYLEM AKLRLYRPEE LGEGSREAAR AVLRHVLDGL LRLLAPFMPF
VTEELYYRLF DESVHDQAWP EASEKWIDEG VEEVGEILRE IVTEVRKAKT DAGLRMGAEF
EGLTVHVQDE ELAESLEKAI PDLKSATRAK EVEVEVGEPK LERVPVKVEP RMDVIGPKYR
ELTRDIIEYV ENNPDEVASA IKEDGKAKLE IDGEKVVLDE ECVDVEWELR VKGGEGKAVE
IRPGVVVEIR GLST
