ID   SYMM_DICDI              Reviewed;         575 AA.
AC   Q54MZ8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable methionine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.10;
DE   AltName: Full=Mitochondrial methionyl-tRNA synthetase;
DE            Short=MtMetRS;
DE   Flags: Precursor;
GN   Name=mmetS; ORFNames=DDB_G0285759;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000079; EAL64717.1; -; Genomic_DNA.
DR   RefSeq; XP_638145.1; XM_633053.1.
DR   AlphaFoldDB; Q54MZ8; -.
DR   SMR; Q54MZ8; -.
DR   STRING; 44689.DDB0231296; -.
DR   PaxDb; Q54MZ8; -.
DR   PRIDE; Q54MZ8; -.
DR   EnsemblProtists; EAL64717; EAL64717; DDB_G0285759.
DR   GeneID; 8625193; -.
DR   KEGG; ddi:DDB_G0285759; -.
DR   dictyBase; DDB_G0285759; mmetS.
DR   eggNOG; KOG0436; Eukaryota.
DR   HOGENOM; CLU_009710_9_0_1; -.
DR   InParanoid; Q54MZ8; -.
DR   OMA; SDMHGTP; -.
DR   PhylomeDB; Q54MZ8; -.
DR   PRO; PR:Q54MZ8; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; ISS:dictyBase.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; ISS:dictyBase.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..575
FT                   /note="Probable methionine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000328568"
FT   MOTIF           52..62
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           352..356
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   575 AA;  65877 MW;  2F300850EB774150 CRC64;
     MLKLLKQIST TSTFKKPSSI NNGFININLF KNYCTSVKQE DKKKVLITTP IFYVNGPPHI
     GHLYSALLGD ALGRWNRFIG NDTLFMTGTD EHGSKVDEAA KKNGLKTIDY CDKISNRFRE
     LFDKADIKYD DFIRTTEPRH KEAVTAIWNR LLERGYIYKG VYKGWYCTSD ESFLTDDQVT
     EGMSPITPQN PISKKCMISL ESGHEVNWIE EENYMFKLSE FSKTIENWFE EVKPIFPAIH
     VNLLRYMLSQ GIKDLSISRP SSRIPWGIEV PNDPSQTIYV WLDALTNYLT VTGYPNVSPN
     SSQSHWSNAT HIIGKDIIKF HSVYWPSFLI AADYPLPKSI ICHAHWTVNR EKMSKSRGNV
     VDPFLAIDNH GLELIRYFLL KGGGLENDGD WSEHELAVRF KSDLADTYGN LISRCTGKAL
     NPSGEWPKSV TDTSLFTMDD QKLIENSSIL VKSVSTHYDR GDFKSGIFEI MTFLYECNLY
     VQNQAPWKLV PKPNRVGSDL IRLNTIIYIA IEMIRITSLL LSPIIPTSSN LTLNYLSIPL
     ENRSNPSNFK FGYNYHQNQN NLKLPKEILI LFHKK