ID   SYVM_PIG                Reviewed;        1062 AA.
AC   Q767M3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Large white;
RX   PubMed=14673549; DOI=10.1007/s00251-003-0627-0;
RA   Shigenari A., Ando A., Renard C., Chardon P., Shiina T., Kulski J.K.,
RA   Yasue H., Inoko H.;
RT   "Nucleotide sequencing analysis of the swine 433-kb genomic segment located
RT   between the non-classical and classical SLA class I gene clusters.";
RL   Immunogenetics 55:695-705(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; AB113354; BAD08423.1; -; Genomic_DNA.
DR   EMBL; AB113355; BAD08425.1; -; Genomic_DNA.
DR   RefSeq; NP_001116686.1; NM_001123214.1.
DR   AlphaFoldDB; Q767M3; -.
DR   SMR; Q767M3; -.
DR   STRING; 9823.ENSSSCP00000030692; -.
DR   PaxDb; Q767M3; -.
DR   PeptideAtlas; Q767M3; -.
DR   PRIDE; Q767M3; -.
DR   GeneID; 100144457; -.
DR   KEGG; ssc:100144457; -.
DR   CTD; 57176; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   InParanoid; Q767M3; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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..1062
FT                   /note="Valine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000338003"
FT   REGION          1..73
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        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..56
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   1062 AA;  118288 MW;  619F230CC078EEC7 CRC64;
     MPHLPLASFR PPLRGLRPTR CFPRSHSLST QSEPHGSPIS RRNREAKQKR LREKQAALET
     GIAAKGKPPA ESTKAWTPKE IVLYEIPTEH GEKKDVSRPL PPAYSPRYVE AAWYPWWVRE
     GFFKPEYQTR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDALVRWH RMRGDRVLWV
     PGSDHAGIAT QAVVEKKLWK ERGLRRRELS REDFLREVWK WKEEKGGEIC QQLRVLGASL
     DWDRECFTMD AGSSVAVTEA FVRLYKAGLL YRSRQLVNWS CALRSAISDI EVESRPLSGR
     TELRLPGCPT PVSFGLLVSV AFPVDGEPDA EVVVGTTRPE TLPGDVAVAV HPDDARYTHL
     HGRQLHHPLT GQLLPLITDC AVQPHLGTGA VKVTPAHSPA DAELGARHGL SPLSVIAEDG
     TMTSLCGDWL QGLHRFVARE KIVSALRERG LFRGLQNHPM VLPICSRSGD VVEYLLKSQW
     FVRCQEMGEQ AAKAVVSGAL ELSPSFHQKN WQHWFSHIGD WCVSRQLWWG HRIPAYLVVE
     ERAKGNTEDC WVVGRTEAEA REVAAELTGR PGAELTLERD PDVLDTWFSS ALFPFSALGW
     PQETPDLARF YPLSLLETGS DLLLFWVGRM VMLGTQLTGQ LPFSKVLLHS MVRDRQGRKM
     SKSLGNVLDP RDIINGVELQ VLQEKLRDGN LDPAELAIAA AAQKKDFPHG IPECGTDALR
     FTLCSHGVLG GDLHLSVSEV LSFRHFCNKI WNALRFILNA LGEKFIPQPL EELCPTSPMD
     AWILSCLART AQECERGFLT RELALVTHAL HHFWLHNLCD VYLEAVKPVL SHSPRPPGPP
     QVLFSCADVG LRLLAPLMPF LAEELWQRLP LRPGNTTAPS ICVAPYPSAH SLEHWHQPEL
     ERRFSRVQEA VQALRALRAT YQLTKARPRV LLQTSEPGEQ GLFEAFLGPL STLGHCGAVG
     FLPPGAAAPS SWAQASLSDT AQVYMELQGL VDPQTHLPRL AARRQKLQKQ LDSLLARTPS
     EGEAESQSQQ RLSSLQLELS KLDKAASHLR QLMDASPSPG EL