ID   SYVM_MACMU              Reviewed;        1064 AA.
AC   Q5TM74;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 107.
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   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15269276; DOI=10.1093/molbev/msh216;
RA   Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT   "Rhesus macaque class I duplicon structures, organization, and evolution
RT   within the alpha block of the major histocompatibility complex.";
RL   Mol. Biol. Evol. 21:2079-2091(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD69752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB128049; BAD69752.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q5TM74; -.
DR   SMR; Q5TM74; -.
DR   STRING; 9544.ENSMMUP00000024488; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   HOGENOM; CLU_001493_0_2_1; -.
DR   InParanoid; Q5TM74; -.
DR   OMA; HNIKSHF; -.
DR   TreeFam; TF354250; -.
DR   Proteomes; UP000006718; 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..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1064
FT                   /note="Valine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000338001"
FT   REGION          25..65
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..60
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   1064 AA;  118642 MW;  7F226C82C7AB636E CRC64;
     MPHLPLASFR PPFWGLRHSR GLPRFHSVST QSEPHGSPIS RRNREAKQKR LREKQATLET
     DIAGESKSPA ESIKAWSPKE VVLYEIPTKP GEKKDVSGPL PPAYSPRYVE AAWYPWWVRE
     GFFKPEYQAR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDALVRWH RMRGDQVLWV
     PGSDHAGIAT QAVVEKQLWK EQGVRRHELS REAFLREVWQ WKEAKGGEIC EQLRALGASL
     DWDRECFTMD VGSSVAVTEA FVRLYKAGLL YRNRRLGRWM SCPLTQLSRR FQVENRPLPG
     RTQLRLPGCP TPVSFGLLFS VAFPVDGEPD AEVVVGTTRP ETLPGDVAVA VHPDDSRYTH
     LHGRQLRHPL MGQPLPLITD YAVQPHVGTG AVKVTPAHSP ADAEMGARHG LSPLNVIAED
     GTMTSLCGDW LQGLHRFVAR EKIVSVLSER GLFRGLQNHP MVLPICSRSG DVIEYLLKSQ
     WFVRCQEMGA RAAQAVESGA LELSPSFHQK NWQHWFSHIG DWCVSRQLWW GHQIPAYLVV
     EDHAQGEEDC WVVGRSEAEA REVAAELTGR PGAELALERD PDVLDTWFSS ALFPFSALGW
     PQETPDLARF YPLSLLETGS DLLLFWVGRM VMLGTQLTGR LPFSKVLLHP MVRDRQGRKM
     SKSLGNVLDP RHIISGAEMQ VLQEKLRSGN LDPAELAIVA AAQKKDFPHG IPECGTDALR
     FTLCSHGVQG GDLCLSVSEV QSCRHFCNKI WNALRFILNA LGEKFVPQPA KELSPSCHMD
     AWILSRLALT ARECERGFLT RELSLVTHAL HHFWLHNLCD VYLEAVKPVL RHSPCPPGPP
     QVLFSCADIG LRLLAPLMPF LAEELWQRLP PRPGCPPAPS ISVAPYPSPC SLEHWRQPEL
     ERRFSRVQEV VQVLRALRAT YQLTKARPRV LLQSSEPGDQ GLFEAFLEPL GTLSHCGAVG
     LLPPGAAAPS GWAQAPLSDT VQVYMELQGL VDPQIQLPLL AARRSKLQKQ LDGLMARTPS
     EGEAGTQRQQ RLSSLQLELS KLDKAASHLR QLMDEPPAPG SPEL