SYV_DEHM1
ID SYV_DEHM1 Reviewed; 880 AA.
AC Q3Z9C5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=DET0430;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(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; CP000027; AAW40282.1; -; Genomic_DNA.
DR RefSeq; WP_010936207.1; NC_002936.3.
DR AlphaFoldDB; Q3Z9C5; -.
DR SMR; Q3Z9C5; -.
DR STRING; 243164.DET0430; -.
DR PRIDE; Q3Z9C5; -.
DR EnsemblBacteria; AAW40282; AAW40282; DET0430.
DR KEGG; det:DET0430; -.
DR PATRIC; fig|243164.10.peg.408; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008289; 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 Gene3D; 3.90.740.10; -; 1.
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; Reference proteome.
FT CHAIN 1..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224471"
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; 99965 MW; 91B19D29BDDE3605 CRC64;
MAQCSGLPEM AKAYEAAEVE KKWYQYWMEK GYFKPNPDSD KKPFVIIMPP PNVTGELHLG
HALTATLEDI MIRWHRMLGE PALWLPGADH AGIAAQVVVE RMLAKQGKTR QELGRELFLE
KMWEWVNPCR ERIRHQHMRL GASCDWDRET FTLDPGPVKA VREIFTNLYQ KGLIYRGERI
INWCPRCATA VSDLEVDHKD LAGHIWHLRY PLEDGSGFVT VATTRPETML GDTAVAVHPD
DARYTGMVGK NVLLPIMNRR IPVIADEAVD MAFGTGAVKV TPAHDPNDFE MGLRHSLPMI
TIQNRDTTMN ENAGPCSGMT AKACREYVVS ELKSLGLLLK IEDYTHSVGH CQRCSAVIEP
MVSKQWFVKM EPLAKPALEA VNSGRIQILP ERFTKVYQNW MENIRDWCIS RQLWWGHRIP
VWYCPCGEMI VSKEDPTACP KCGSTKLEQD PDVLDTWFSS GLWPHSTLGW PDQTEDLKRF
YPGSVLETAY DIIFFWVARM IVMGIEDMKE VPFRTVYLHG LIRDDKGEKM SKTKGNVIDP
LKVIDQYGTD ALRFAVTFGT SPGNDSKLGQ TKLEAARNFV NKLWNASRFV IMNLGEEKEL
LPEAGLPLED RWILSRMNRV TADVIRLMEE FQFGEAQRVL QDFVWGEFCD WYIELAKVRL
RDEASVSPRP VLVKVLSTIL RLLHPYMPFI TEELWSYLRP YLPKSLGETD IIVAPFPQAD
ETCFDEQAES IMGSLVEVVR SLRNLRAEHN VEISRYIQAN IYAGDMAEVL SNYLGAVETL
SRSRPVNILP GHYSGASTAT EVVLVLNGIE VVVPMSTMVD LEAEAKRVEA EIAELETQIE
RLSARLSDTQ FLAKAPQAVV DKERTKLEGY IEKVSRLKAV
