ID   SYMM_TAKRU              Reviewed;         590 AA.
AC   Q90YI3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Methionine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase 2;
DE   AltName: Full=Mitochondrial methionyl-tRNA synthetase;
DE            Short=MtMetRS;
DE   Flags: Precursor;
GN   Name=mars2;
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].
RA   Goode D., Elgar G.;
RT   "Three way comparative genomic analysis of the BTK locus between man, mouse
RT   and Fugu.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ290422; CAC44631.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90YI3; -.
DR   SMR; Q90YI3; -.
DR   STRING; 31033.ENSTRUP00000031960; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   HOGENOM; CLU_009710_9_0_1; -.
DR   InParanoid; Q90YI3; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 788159at2759; -.
DR   TreeFam; TF105709; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326; PTHR43326; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 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..590
FT                   /note="Methionine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000045495"
FT   REGION          570..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           342..346
FT                   /note="'KMSKS' region"
FT   COMPBIAS        574..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   590 AA;  67664 MW;  6DF12F9213457F1D CRC64;
     MRTRFLFLTS GCKAVPELHK IVLANAAPVK NPEIRYASTE NRNYYITTPI FYVNASPHLG
     HLYSAVIADC FHRHKQLQGF NSRFATGTDE HGLKIQQAAE AAGKEPLEFC TTVSERFRHL
     FSSCNISNTD YIRTTEQRHH RAVQHFWSVL CSKGLIYKGS YEGWYSTQDE SFLTPSQVTT
     ALDSTGKEIK VSLESGHKVE WMKEENYMFR LSGFRSQLLD WLRENPRAIQ PERFHHSVLQ
     WLQEELPDLS VSRQKSRLQW GIPVPEDDGQ TIYVWLDALV NYLTVVGYPN NHERWWNVAH
     HIIGKDILKF HAIYWPSFLL GAGLPLPQTI HVHSHWTVAG KKMSKSLGNV IDPQERSQLF
     TTDGLRYFLL RQGVPDTDCD YRDDKVVKLL NAELADALGG LLNRCTATAL NPAQVYASFC
     PDSFPRERGG RADDDDYRML ESVRHLPAVV EQHFEDMHVY KALEAVSTCV RQTNGFVQRH
     APWKLDRKDS ADQRWLGTII HVSLECLRIY GTLLQPVVPE ISNKLLSRLG VQPHERSWTN
     LNFLPRFEGK DCPFEGRALG SDSGVLFSRL ESQRADQQKN RKMEKGSNLK