ID   SYV_SOLUE               Reviewed;         855 AA.
AC   Q01PF1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Acid_7561;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC   Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000473; ABJ88469.1; -; Genomic_DNA.
DR   RefSeq; WP_011689184.1; NC_008536.1.
DR   AlphaFoldDB; Q01PF1; -.
DR   SMR; Q01PF1; -.
DR   STRING; 234267.Acid_7561; -.
DR   EnsemblBacteria; ABJ88469; ABJ88469; Acid_7561.
DR   KEGG; sus:Acid_7561; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_0; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
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; -; 3.
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.
FT   CHAIN           1..855
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000022173"
FT   COILED          797..827
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           524..528
FT                   /note="'KMSKS' region"
FT   BINDING         527
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   855 AA;  97358 MW;  879F83E8708F8334 CRC64;
     MQIEKVYEPQ RFEPHWAQWW IDSNIFRANP ESPGRVFSLV IPPPNVTGVL HIGHMLEHTE
     IDVSTRWHRM LGDNTLWLPG TDHAGIATQM VVARQLKEEG INYRDLGREK FEERVWQWKA
     QSGDTIKRQM VRLGASCDWS RERFTLDPGL SRAVREVFVS LYERGLLYRG EYMTNWCPSC
     NTAISDLEVA HADVAGHLWH IRYPVNGMPG RFVTVATTRP ETMLGDTAIA VNAKDPRYQD
     LHGKTVQLPL MDREIPIILD DLADPQFGTG VVKVTPAHDP NDFEAGKRHN LAKIQVIDNN
     ARMTAAAGPY AGLDRFDARK RVVSALEEIG ALVKVEDYPL SLGKCDRCKT PVEPLISTQW
     FVKTKPLAEK AIAVVESGEI GFVPQNWTKT YYEWMYNIRD WCVSRQLWWG HRIPAWHCGE
     CKEIIVAREA PKACPRCASE NLTQDTDVLD TWFSSGLWPF STLGWPDQTA DLAKYYPTTL
     LITGFDILFF WVARMVMFGL EFMGEVPFKQ VYIHGLVRDA DRQKMSKTKG NVIDPLVVTE
     KYGTDAVRMA LLQGAAPGTD IVLTEERMES SRAFANKIWN AARFLFMNAD QSAAAPAEPT
     IEDRWIVSRL NAAAETANRA IEQYRYHELA QELWKFFWHE FCDWYLELKK VSATGWGNAV
     AAFETALRLL HPAMPFLTEE LWQRLERKEG DPKSIALAQY PQYRAELADS EAEKEVAIIQ
     EIVTLARTLR TESKLDPKQQ LKGALYCRTA SLAIAQRHAD AIQKIARTTL EFKAEAPPKA
     DVIRSTVEFD LVLDVPKVEE DPARKQKERE QLEKNIANSK RQLGDEVFLS KAPAKVVDSI
     RAKLVDYEAQ LAKML