ID   SYV_IDILO               Reviewed;         949 AA.
AC   Q5QY15;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=IL1950;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV82782.1; -; Genomic_DNA.
DR   RefSeq; WP_011235178.1; NC_006512.1.
DR   AlphaFoldDB; Q5QY15; -.
DR   SMR; Q5QY15; -.
DR   STRING; 283942.IL1950; -.
DR   PRIDE; Q5QY15; -.
DR   EnsemblBacteria; AAV82782; AAV82782; IL1950.
DR   KEGG; ilo:IL1950; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001171; 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..949
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224488"
FT   COILED          877..949
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           553..557
FT                   /note="'KMSKS' region"
FT   BINDING         556
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   949 AA;  109230 MW;  08279CADFA62CAA7 CRC64;
     MDKTYSPAAI EQDLYQQWED KGYFKPSGKG DPYSIMIPPP NVTGSLHMGH AFQHTIMDTL
     TRYQRMDGLN TLWQVGSDHA GIATQMVVER QLAAQGQTRQ ELGRDAFIDK IWEWKEQSGG
     TITQQMRRLG DSVDWDRERF TMDEGLSDAV REVFVKLHED NLIYRGKRLV NWDPALQTAI
     SDLEVENKEQ QGYIWYLRYP LADGEKTEDG KDHLVVATTR PETMLGDVCV AVHPDDERFA
     HLVGKFLELP IVNRRIPIVA DHHVDSEFGT GCVKVTPAHD FNDYEIGKRH QTGMISIFDD
     TAHVMAKAGL YTSTGETLEE LNGFNGILPE QYAGKERFEA RKQLVAEFDE LGLLEKIEKH
     TNKIPYGDRG GVPIEPHLTD QWYVRVEPMA KQATAAVEDG RIEFVPKQYE NMYFSWMRDI
     QDWCISRQLW WGHRIPAWYD EQGNVYVGRT EEEVREKHNL GDTPLQQDED VLDTWFSSAL
     WTFSTLGWPK NTEDLKTFHP TDVLVTGFDI IFFWVARMIM MTMHFMKDEE GQPQVPFKKV
     YVTGLIRDEE GQKMSKSKGN VLDPLDMIDG ISADELVAKR TANLMQPKMR EKIEKRTRKE
     FPEGITAHGT DALRFTLTAL ASTGRDINWD MKRLEGYRNF CNKLWNASRY VLMSTEEHDC
     GLENDDMTLS LADEWIIARF NSTVKDFRQA LDTYRFDQAA AIAYEFTWNQ FCDWYLELTK
     PVLQNGTESQ QRGTRHTLVN VLEQLLRLLH PVMPYITETI WQRVKPLVGN TDDTIMLQPF
     PRVEDNVSHQ AMQDMEWLKR VILAIRNIRG EMDLSPNKPL PLLLSNADAM AKGRIQNNES
     FLSSLAKLES IEFIESDDDA PASMTALVDT LKLHIPMAGL IDKEAELQRL QKSIEKANKE
     WQRLNGKLSN DNFVSKAPEA VIAKEREKLS EAETTLKQLQ EQQDKIKAL