ID   SYV_FRATT               Reviewed;         919 AA.
AC   Q5NHZ4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-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=FTT_0299;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(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; AJ749949; CAG44932.1; -; Genomic_DNA.
DR   RefSeq; WP_003021639.1; NZ_CP010290.1.
DR   RefSeq; YP_169348.1; NC_006570.2.
DR   AlphaFoldDB; Q5NHZ4; -.
DR   SMR; Q5NHZ4; -.
DR   IntAct; Q5NHZ4; 6.
DR   STRING; 177416.FTT_0299; -.
DR   DNASU; 3191933; -.
DR   EnsemblBacteria; CAG44932; CAG44932; FTT_0299.
DR   KEGG; ftu:FTT_0299; -.
DR   eggNOG; COG0525; Bacteria.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000001174; 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..919
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224479"
FT   COILED          849..919
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           528..532
FT                   /note="'KMSKS' region"
FT   BINDING         531
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   919 AA;  104790 MW;  365042C72423CA40 CRC64;
     MTQEINKNYN PKEIEQANYQ NWEASGKFAC GNTDSKDTYT IMLPPPNVTG TLHMGHGFQM
     SLMDILIRYN RMSGKDTLWQ PGTDHAGIAT QMVVERQLNA QGISRHDLGR ENFVSKVWEW
     KELSGGTITS QMRRIGASPD WDRERFTMDK GLSDAVKKCF IKLYEDGLAY RGERLVNWDP
     KLKTAVSDLE VAQVDKQGSL WHFIYPVADS DEKIIIATTR PETMLGDMAV AVHPEDERYT
     HLVGKMINLP LTDRQIPIIA DDYVEKDFGT GCVKITPAHD FNDYEMGKRH NLPMLNILTD
     DATLNTNVPS KYQGLDRFEA RKQVVADMEA LGLLDKIEPH ALKVPTGDRT GEILEPYLTK
     QWFVKADVLA KPAIEAVEKG DVRFVPDNWK NTYFAWMRDI QDWCVSRQLW WGHRIPAWYD
     EAGNAYVGED EADVRAKYNL ADDIAIKQDE DVFDTWFSSA LWPFSTLGWP EQTPELAKYY
     PTSVLVTGFD IIFFWVARMM MFGMYFMNDV PFRDIYITGL IRDSEGQKMS KSKGNVLDPV
     DLIDGISLDE LLKKRTTGLM QPQMKAKIEK ATKKEFPEGI SAYGADAVRF TYAALASTSR
     DISFDTARVE GYRNFCNKLW NASRFVMMNL DDYKVCDNYE LGVADKWIWS VLNTATADVH
     RHLANYRFDL VTNTIYDLVW NNYCDWYVEF AKVALKDDSL SEQQKNGVKY TLTKVLENIL
     ALAHPLIPFI TESIYQQLKA HLNDAKDTIM DVSYPVATQA LEAPEAEKAI VWLQNVVTTL
     RNMRSEVGIK PSLEISLIVK DVADKDREYL AQTEGFIKAL ARINNIEFND NPPTSLSQIV
     EGLELNIPLA GLVDIEAEKA RLDKELDKLK DEVDRVQKKL SNERFVSNAP EAVVAAEQEK
     LAKYQELYAK TLEKKEALG