ID   SYV_AQUAE               Reviewed;        1165 AA.
AC   O67411;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
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=aq_1413;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07375.1; -; Genomic_DNA.
DR   PIR; A70423; A70423.
DR   RefSeq; NP_213976.1; NC_000918.1.
DR   RefSeq; WP_010880914.1; NC_000918.1.
DR   AlphaFoldDB; O67411; -.
DR   SMR; O67411; -.
DR   STRING; 224324.aq_1413; -.
DR   PRIDE; O67411; -.
DR   EnsemblBacteria; AAC07375; AAC07375; aq_1413.
DR   KEGG; aae:aq_1413; -.
DR   PATRIC; fig|224324.8.peg.1107; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_1_0; -.
DR   InParanoid; O67411; -.
DR   OMA; HNIKSHF; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 3.
DR   Gene3D; 3.90.740.10; -; 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; 3.
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   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..1165
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106211"
FT   COILED          1001..1032
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   COILED          1097..1165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           800..804
FT                   /note="'KMSKS' region"
FT   BINDING         803
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   1165 AA;  137151 MW;  E612D4F28EF4A237 CRC64;
     MEIKEYNPRE IEEKWSRYWI EKALYHVEKP DKRKKFSVVI PPPNVTGSLH MGHALNATLQ
     DVIVRWQRMR GRECVWVPGF DHAGIATQYV VEKQLAKEGK SRLELGREEF LKKVWEWVPK
     SRNAIRTQLT KLGVSVDWKR ERFTLDEGFS RAVRKAFRTL FEEGLIYRAE YIVNWCPNDR
     TALSDLEVEY EEEKGSLWYI KYPIVDENGK DTGEFITVAT TRPETMLGDT AVAVNPNDDR
     YKHLVGKRAR LPLVNWERKD LRGNSVSNLI PIIADERVKM DFGTGAVKIT PAHDPLDFEI
     GKTHDLPFVR VIDETGRMNE NAGDFAGMDR YEAREAIVAK LREDELLEKE EEITHSVGHC
     YRCKTVIEPM VSVQWFVKVS DPRIKDISIK VVEEGIKERE EKELFVQLAQ VEELSVVIPL
     KEEGRHKIVV VLDKTAKFLV GKREGELAYI YYPKGDERTL EFAKRLAEEF KDYEFMVAYE
     GLPKIVVMGN EQLVEPGSYL FVYDGKKLDL YKLEGEKPKF LKTLGKGEAD LEVTQKSIQI
     KPERIKKVEE REKRVKFIPE HWKKFYLDWM YNLKDWCISR QIWWGHRIPV WYCKDCGNVN
     VFTDDDFDRA HDKIIFNLIA DGKIDQEFTP EEVEKVLKSP HFVHPEMTVL DFYKKFVFHR
     YYNMDITADS LRLLFTQDMN PMAMLTPGVS TRNIYKYDSQ KKKWKMVLRC KKCGSENLEQ
     ERDVLDTWFS SALWPFGVFG WPESTEDLKN LYPTDLLVTG FDIIFFWVAR MIMMGTHFMK
     DIPFYDVYVH ALVRDKYGRK MSKTIGNVID PLDIIERYGA DALRFTLAIL TVQGRDIKLA
     EEKFEGYKHF ANKIWNAARY VLMNTPEDFI ARIPYMAPLK PEDKWIITKL NETAEEVNKA
     LENYQYSQAA HAIYEFFWSD YCDWYIEFTK ERIYKKAPED NEEEKAKVEN ERTTALYTLH
     YVLEKALRIL HPFMPYITEE LWHKLPNAEG ESISLAEFPQ KNEDEIYEED KQKVERLKEI
     ISAIRAIRSD LQIKPSEKIK ASFKTESEFS RRVIQEFKNH ILNLAKLESF EEVSQRPQNT
     VATFSKDTEI YVHIEGHVDL DKLIQSYEKK REKLLKELER VNKKLSNENF LKKAPVEVVE
     KEKQIKEELE NDLKKVEEIL KVLRS