SYV_COREF
ID SYV_COREF Reviewed; 903 AA.
AC Q8FN65;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=CE2282;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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_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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC19092.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC19092.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_035108985.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FN65; -.
DR SMR; Q8FN65; -.
DR STRING; 196164.23494124; -.
DR PRIDE; Q8FN65; -.
DR EnsemblBacteria; BAC19092; BAC19092; BAC19092.
DR KEGG; cef:CE2282; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001409; 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 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; 2.
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..903
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224466"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 836..902
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 61..71
FT /note="'HIGH' region"
FT MOTIF 552..556
FT /note="'KMSKS' region"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 903 AA; 101684 MW; 938988EEFF709B40 CRC64;
MVCVTDQNNE NPSQNRADKL PKSWDPKAVE ADLYQGWVDA GYFTADPASE KPGYSIVLPP
PNVTGQLHMG HALDHTLMDA LARRKRMQGF EVLWLPGMDH AGIATQTKVE EMLKETEGKS
RYDYSREEFI EKVWEWKKEY GGKIGEQMRA IGDSVDWSRE RFTLDEGLSR AVQTIFKKLY
DSGMIYQANR LVNWSPVLET AVSDIEVVYK DVEGELVSIR YGSLNDDEPH VVVATTRVET
MLGDVAVAVH PDDERYRHLV GTTLPHPFRD DLTLKVVADD YVDPEFGSGA VKITPAHDPN
DYALGLRHHL DMPTIMDKTG RIADTGTQFD GMTREEARVK VREALAEQGR IVKEVRPYVH
SVGHSERSGE AIEPRLSLQW WVKVEELAKM SGDAVRAGDT TIHPKSLEPR YFDWVDDMHD
WCISRQLWWG HRIPIWYGPD GDVICVGPDE QAPEGYTQDP DVLDTWFSSA LWPFSTMGWP
DKTPELDKFY PTSVLVTAYD ILFFWVARMM MFGTFAAKET PELLGEGTDG RPQVPFTDLF
LHGLVRDEHG RKMSKSLGNG IDPMDWVDNY GADALRFTLA RGANPGVDLP VGEDSAQSSR
NFATKLFNAT RFALMNGAVS EGLPERAELT DADRWILDRL EEVRGHVDDY LDNYQFAKAN
EELYHFAWNE FCDWYLEIAK VQIPREGVTE RGRNTQQVLG HVLDALLRLL HPAMPFVTEV
LWKALTDGES IVTSSWPTPA DTNGGAAVDA DAARRIADVE KLVTEIRRFR SDQGVKPSQK
VPARLDFAAC DLTELEGAVR ALVRIEEPAE DFEESASLEI RLSTATITVE LDTSGTVDVA
AERKRLEKDL ATANKELETT GKKLGNEAFL AKAPDAVVEK IRGRQQVARE EVERITKRLE
ELG
