ID   SYVC_TAKRU              Reviewed;        1217 AA.
AC   P49696;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   Name=vars1; Synonyms=vars;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9254008; DOI=10.3109/10425179709034030;
RA   Lim E.H., Corrochano L.M., Elgar G., Brenner S.;
RT   "Genomic structure and sequence analysis of the valyl-tRNA synthetase gene
RT   of the Japanese pufferfish, Fugu rubripes.";
RL   DNA Seq. 7:141-151(1997).
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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X91856; CAA62967.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49696; -.
DR   SMR; P49696; -.
DR   STRING; 31033.ENSTRUP00000005137; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   eggNOG; KOG0867; Eukaryota.
DR   InParanoid; P49696; -.
DR   BRENDA; 6.1.1.9; 6209.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
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; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004046; GST_C.
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; 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; PF00043; GST_C; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1217
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106256"
FT   DOMAIN          27..155
FT                   /note="GST C-terminal"
FT   MOTIF           293..303
FT                   /note="'HIGH' region"
FT   MOTIF           809..813
FT                   /note="'KMSKS' region"
FT   BINDING         812
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1217 AA;  138218 MW;  5E08AF24B5C8A7A1 CRC64;
     MATLYVSPHL DDFRSLLALV AAEYCGNAKQ QSQVWQWLSF ADNELTPVSC AVVFPLMGMT
     GLDKKIQQNS RVELMRVLKV LDQALEPRTF LVGESITLAD MAVAMAVLLP FKYVLEPSDR
     NVLMNVTRWF TTCINQPEFL KVLGKISLCE KMVPVTAKTS TEEAAAVHPD AAALNGPPKT
     EAQLKKEAKK REKLEKFQQK KEMEAKKKMQ PVAEKKAKPE KRELGVITYD IPTPSGEKKD
     VVSPLPDSYS PQYVEAAWYP WWEKQGFFKP EFGRKSIGEQ NPRGIFMMCI PPPNVTGSLH
     LGHALTNAIQ DTLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLMREKG TSRHDLGREK
     FIEEVWKWKN EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SYAVQEAFIR MHDEGVIYRS
     KRLVNWSCSL NSAISDIEVD KNELSGRTLL PVPGYKEKVE FGVLVSFAYK VDGSDEEVVV
     ATTRIETMLG DTAVAVHPSD SRYQHLKGKT VLHPFCDRKI PVVFDDFVDM SFGTGAVKIT
     PAHDHNDYEV GVRHNLAFIN ILDENGFVIN VPPPFLGMKR FDARKAVLQA LKDRDQFKEI
     KDNPMVVPVC SRSKDIVEPL MKPQWYVSCS DMGKQAADAV REGRLKIIPD HHSQTWFNWM
     DNIRDWCISR QLWWGHRIPA YFITVSDPSV KPGEDMDGHY RVSGRTPEEA REKAAKRFNV
     SPDKIALRQD EDVLDTWFSS GINPFSILGW PNETEDLNVF YPGTLLETGH DILFFWVARM
     VMMGLKLTGK LPFKEVYHCA VVRDAHGRKM SKSLGNVIDP LDDHIGIALE GLHAQLMDTN
     LDPLEVEKPK KVQKADYPNC IPECGTDALR FALCAYTSQG RDINLDVNRI LGYRHFCNKL
     WNAVKFAMRT LGDQFVPADT SPAEREESVS DRWILSRLST AVAQCDAAFR TYDFPAITTA
     IYNFWLYELC DVYLESVKPV FIKAKEDGSC ERPAAVCRQT LYTCLEVGLR LLAPLMPFVT
     EELYQRLPRR RPQSDPPSIC VTPYPDAAEF CWQCEDVDRD IDFIMGVVRT IRSLRSDYKL
     TKTAADCYLQ CTDAATVSLV QKYSLQIQTL SYSQAIVPLM APQPAPEGCA VAIASDRCTV
     NMMLKGLIDV EKEVPKLMGK KTDLEKQIEK LSEKISKGDY KEKVPVKVQE QDTEKLRQSQ
     TELEKVKEAM DNFQKMM