SYV_DEHMC
ID SYV_DEHMC Reviewed; 880 AA.
AC Q3ZZG9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=cbdbA384;
OS Dehalococcoides mccartyi (strain CBDB1).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=255470;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBDB1;
RX PubMed=16116419; DOI=10.1038/nbt1131;
RA Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT "Genome sequence of the chlorinated compound-respiring bacterium
RT Dehalococcoides species strain CBDB1.";
RL Nat. Biotechnol. 23:1269-1273(2005).
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; AJ965256; CAI82595.1; -; Genomic_DNA.
DR RefSeq; WP_011308952.1; NC_007356.1.
DR AlphaFoldDB; Q3ZZG9; -.
DR SMR; Q3ZZG9; -.
DR KEGG; deh:cbdbA384; -.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
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; 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.
FT CHAIN 1..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224472"
FT COILED 815..854
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 51..61
FT /note="'HIGH' region"
FT MOTIF 529..533
FT /note="'KMSKS' region"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 880 AA; 100189 MW; E0A6F24298F69053 CRC64;
MAQCSDLPEM AKAYEAAEVE KKWYQYWMEK SYFKPNPNSD KKPFVIIMPP PNVTGELHLG
HALTATLEDI MIRWHRMQGE PTLWLPGVDH AGIAAQVVVE RELAKQGKTR QQLGRELFLE
KMWEWVNPCR EKIRHQHMRL GASCDWDRET FTLDAGPVKA VREIFTNLYE KGLIYKGERI
INWCPRCGTA VSDLEVDHKD LAGHIWHLRY PLEDGSGFVT VATTRPETMQ GDTAVAIHPD
DTRYAGMVGK NVVLPIMNRR IPVIADEAVD MAFGTGAVKV TPAHDPNDFE MGLRHNLPMI
TIQNRDTTMN ENAGPCSGMT AKACREYVVS EMKSLGLLLR IEDYIHSVGH CQRCSAVIEP
MVSKQWFVKM EPLAKPALEA VNSGRIQILP ERFNKVYQNW MENIRDWCIS RQLWWGHRIP
VWYCPCGEMI VAKVDPTVCP KCGGTELEQD PDVLDTWFSS GLWPHSTLGW PDQTEDLKRF
YPGTVMETAY DIIFFWVARM IVMGMEDMNE VPFRTVYLHG LIRDDKGEKM SKTKGNVIDP
LKVIDQYGTD ALRFAVTFGT SPGNDSKLGQ TKLEAARNFA NKLWNASRFV IMNLGEAKEL
TPEAELPLED RWIISRMNRV TADVTRLMEE FQFGEAQRVL QDFIWGEFCD WYIELAKVRL
RDEASVSPRP VLVRVLSSIL RLLHPYMPFI TEELWSYLRP YLPESLRETD IIVAPYPAAD
KTCFDEQAES VMGSLVEIVR SLRNLRAEHN VEISRYIQAN IYAGDMASVL GNYLGAVETL
SRARPVNILP GHYSGASTAT EVVLVLTGIE VVVPMSTMVD LEVEAKRVKA EISELEIQIE
RLSTRLSDEQ FLAKAPQAVV DKERIKLEGY IEKVSRLKSA
