ID A0A1G4K145_9SACH Unreviewed; 573 AA.
AC A0A1G4K145;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=LAMI_0F09296G {ECO:0000313|EMBL:SCU97227.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU97227.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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DR EMBL; LT598467; SCU97227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4K145; -.
DR STRING; 1230905.A0A1G4K145; -.
DR OrthoDB; 166496at2759; -.
DR Proteomes; UP000191024; Chromosome f.
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; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024}.
FT DOMAIN 17..409
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 451..534
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 573 AA; 65193 MW; 8196AE58D1BA9722 CRC64;
MRSYRRFSSS LSRAVHHVTT PIFYPNAKPH LGHLYSSLLC DASRRWQKMV GFQTLMTTGT
DEHGLKIQTA SEAQNFASPK QFVDVLYKEF IKLDQNADIE YSRFIRTTDQ DHIDNVQKLW
KLCEDRGYIY KGEHAGWYSI SDESFYPTSK VVKVALDGTK SPLEPGQTSG NCKFINTETN
NEVIYQSEIN YFFKLSAVYD QLVHFLVEER PDFISPQSRR SEILKELLSS PLSDLSISRP
ASRIRWGIDV PQDSSQKIYV WFDALCNYLT SLGGIDAIRD NTLVELKHTG LSSTDCPAKW
WENTTHVVGK DISRFHVIYW PSFLIAAGLK LPKKVMVHGH WLSGGVKMSK SLGNVVDPQV
MLSHYGSDIL RLFLLENSHL SSDCDFSEER LHNTSEKLAS KWGNLISRCC GSKFSLERAS
RTFASKPFDK FERIISDAEA RKAYGMVING LLKLKGEYSK RMTNFDYRGA ILLVWDLIDK
ANNFLQIAKP WTKTGEEQDL IIFTAIEAAR ISAVLCHPII PGLSAKFLNR IDVEPEKRTI
AFASFGSDST YGCKSNTRGR ELPFARIPRR PDL
//