ID   SYVM_RAT                Reviewed;        1065 AA.
AC   Q6MG21;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Valine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
DE   Flags: Precursor;
GN   Name=Vars2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15060004; DOI=10.1101/gr.1987704;
RA   Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA   Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT   "The genomic sequence and comparative analysis of the rat major
RT   histocompatibility complex.";
RL   Genome Res. 14:631-639(2004).
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BX883047; CAE84026.1; -; Genomic_DNA.
DR   RefSeq; NP_998728.1; NM_213563.1.
DR   AlphaFoldDB; Q6MG21; -.
DR   SMR; Q6MG21; -.
DR   STRING; 10116.ENSRNOP00000046565; -.
DR   CarbonylDB; Q6MG21; -.
DR   PhosphoSitePlus; Q6MG21; -.
DR   PaxDb; Q6MG21; -.
DR   PRIDE; Q6MG21; -.
DR   GeneID; 309596; -.
DR   KEGG; rno:309596; -.
DR   UCSC; RGD:1303122; rat.
DR   CTD; 57176; -.
DR   RGD; 1303122; Vars2.
DR   eggNOG; KOG0432; Eukaryota.
DR   HOGENOM; CLU_001493_0_1_1; -.
DR   InParanoid; Q6MG21; -.
DR   OrthoDB; 229591at2759; -.
DR   PhylomeDB; Q6MG21; -.
DR   TreeFam; TF354250; -.
DR   PRO; PR:Q6MG21; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 2.
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; IPR009080; tRNAsynth_Ia_anticodon-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   PRINTS; PR00986; TRNASYNTHVAL.
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; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..15
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..1065
FT                   /note="Valine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000338004"
FT   REGION          27..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           146..156
FT                   /note="'HIGH' region"
FT   MOTIF           659..663
FT                   /note="'KMSKS' region"
FT   COMPBIAS        38..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         662
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1065 AA;  118894 MW;  4BF57C6962DA50CC CRC64;
     MPHLPLASFR PPLWGLRPSW GLARPRALCT QPEPHGSPVS RRNREAKQKR LREKQAALEA
     GLAEKSKTPA VPTKAWSHKE VVLYEIPTRP GEKKDVSGPL PPAYSPQYVE AAWYQWWVRE
     GFFKPEYQAR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDAFVRWH RMRGDRVLWI
     PGSDHAGIAT QAVVEKQLWR ERRVRRHELS REDFLRAVWQ WKQEKGGEIY EQLCALGASL
     DWDRECFTMD AGSSAAVTEA FVRLYDLGLL YRNRQLVNWS CTLRSAISDI EVESRPLPGR
     TVLRLPGCPI PVSFGLLVSI AFPVDGDPGT EIVVGTTRPE TLPGDVAVAV HPDDPRYTHL
     HGRQLRHPLT GQHLPLITDT TVQPHVGTGA VKVTPAHSPA DAEMGTRHGL TPLSVIAEDG
     TMTSLCGDWL QGLHRFVARE KIMCTLRERG LFRGLQEHPM VLPICSRSGD VVEYLLKSQW
     FVRCQEMGDR AAKAVESGAL ELWPSFHQKS WQHWFAHIGD WCVSRQLWWG HQIPAYRVGG
     EKAEDDREEC WVVGRSEAEA RAAAAKQTGR PEAELTLERD PDVLDTWFSS ALFPFSALGW
     PQETPDLARF YPLTLLETGS DLLTFWVGRM VMLGTQLTGQ LPFSKVLLHS MVRDRQGRKM
     SKSLGNVLDP RDIISGQELQ VLQAKLRDGN LDQGELAVAA AAQKKDFPYG IPECGTDALR
     FALCSHGILG GDLHLSVSEV LNYRHFCNKL WNALRFILRA LGDDFVPQPA EKVTPSSPMD
     AWILSRLAFA ANECERGFLS RELSLVTHTL YHFWLHNLCD VYLEAVKPVL SSAPCPPGPP
     QVLFSCADVG LRLLAPLMPF LAEELWQRLP PRQGGSMAPS ICVAPYPSGH SLVSRGQESW
     RQPELEHCFS RVQEIVQALR ALRATYQLTR ARPHVLLQSS DPGEQGLVQP FLEPLGVLSH
     CGAVGFLPPG AAAPSGWALA PLGDTIKIYM ELQGLVDPQS QLPRLAARRQ KLQKQLDDLL
     NRTVSDGPAE RQQRISSLQL ELSKLDQAAS HLQQLMEEAP DAREL