ID   SYMM_CANAX              Reviewed;         577 AA.
AC   O74634;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Methionine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=MSM1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9714830; DOI=10.1016/s0378-1119(98)00292-3;
RA   Lee S.W., Jo Y.J., Kim S.;
RT   "Cloning and characterization of mitochondrial methionyl-tRNA synthetase
RT   from a pathogenic fungi Candida albicans.";
RL   Gene 215:311-318(1998).
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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AB006140; BAA33373.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74634; -.
DR   SMR; O74634; -.
DR   VEuPathDB; FungiDB:C5_04650C_A; -.
DR   VEuPathDB; FungiDB:CAWG_04833; -.
DR   BRENDA; 6.1.1.10; 1096.
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:EnsemblFungi.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
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; 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.
FT   CHAIN           1..577
FT                   /note="Methionine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000139270"
FT   MOTIF           25..37
FT                   /note="'HIGH' region"
FT   MOTIF           329..333
FT                   /note="'KMSKS' region"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   577 AA;  67120 MW;  129413ACD5B14728 CRC64;
     MRFKIRGPLI QLRYKSTKAF YITTPIFYVN AAPHIGHLYS MLIADTRNKW EKLNPSKESF
     MLTGTDEHGL KIQSTAEKLG LEPKVLVDKV SQNFSKLAEQ FDVNYDRFIR TTDNDHIELV
     RYFWNLMMEK GFIYTDTHSG WYSISDETFF PETQIEEVVK NGKAVKISSE TKNEVVYQEE
     TNYFFKLSMF QEQLIQFLKQ NPEFIKPKHR YQFILKELED TKLPDLSISR PSSRLKWSIE
     VPNDSTQKIY VWFDALLNYL TATKFPHGFE VQDSKFVTPE NSIWPATHVI GKDIIRFHCI
     YWPIFLMAAG IELPKQVIVH SHWLCDGFKM SKSLGNLVDP MEISEYYGVD PVRFFLVENS
     NIDDDCKFSE ELLQRSRDAV LGKYCNLISR IGGKNFSIEE AVKSFASGEF NNIREIIETY
     TINKDSVEGL LSSLNKLTTD LNDLYNQMDH YFTNFDYIRA IQCWWSVINQ ANQIFQSAEP
     WTYVKLINSP ETPAELKEKY RILNNYFVYL CAETTRISSI LIQPVMPQLS KKILDRLNVS
     GRTSEFTTLS ADLQYGSGAN SKSHKVPLEK IAPRDIK