ID A0A291ISP7_9MOLU Unreviewed; 511 AA.
AC A0A291ISP7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228};
DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228};
DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228};
GN Name=metG {ECO:0000256|HAMAP-Rule:MF_01228,
GN ECO:0000313|EMBL:MCL8216675.1};
GN ORFNames=CP520_03215 {ECO:0000313|EMBL:ATG97721.1}, LD118_00257
GN {ECO:0000313|EMBL:MCL8216675.1};
OS Mesoplasma lactucae ATCC 49193.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Entomoplasmataceae; Mesoplasma.
OX NCBI_TaxID=81460 {ECO:0000313|EMBL:ATG97721.1, ECO:0000313|Proteomes:UP000232227};
RN [1] {ECO:0000313|EMBL:ATG97721.1, ECO:0000313|Proteomes:UP000232227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=831-C4 {ECO:0000313|EMBL:ATG97721.1,
RC ECO:0000313|Proteomes:UP000232227};
RA Knight T.F., Rubinstein R., Citino T.;
RT "SPAdes assembly of the Mesoplasma lactucae genome.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MCL8216675.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 49193 {ECO:0000313|EMBL:MCL8216675.1};
RA Green E.A., Klassen J.;
RT "Mollicute symbiont genomes associated with the fungus-growing ant,
RT Trachymyrmex septentrionalis.";
RL Submitted (FEB-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC also for the initiation of all mRNA translation through initiator
CC tRNA(fMet) aminoacylation. {ECO:0000256|ARBA:ARBA00003314,
CC ECO:0000256|HAMAP-Rule:MF_01228}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01228};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01228}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
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DR EMBL; CP023668; ATG97721.1; -; Genomic_DNA.
DR EMBL; JAKNSY010000001; MCL8216675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291ISP7; -.
DR KEGG; mlac:CP520_03215; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000232227; Chromosome.
DR Proteomes; UP001139645; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 1.
DR Pfam; PF09334; tRNA-synt_1g; 2.
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|HAMAP-Rule:MF_01228};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01228};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01228}; Reference proteome {ECO:0000313|Proteomes:UP000232227}.
FT DOMAIN 7..142
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 144..364
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 384..474
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 14..24
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 301..305
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ SEQUENCE 511 AA; 59639 MW; 08624AFCD7EFD245 CRC64;
MNNKKTFYVT TPIYYPSGEL HIGHAYTTTL ADILNRYKKN DGYETFFLTG SDEHGEKIEI
KSAEMGLPPL QFLEEKVNKF KELWKALGIH YSKFIRTTDK YHEDAVKRIF TKLLEQGDIY
KGFYEGKYCI SCEEFLTTEQ IDENGFCKIS HTLPTDVKEE TYFLKTSAYQ EFITDLLNSN
FIIPDYRKNE MLKNFVEPGL KDLSVTRISF KWGIPITEDP KHVIYVWLDA LTNYITALGY
MQKNHELFDK FWSEDTEIVQ LVGKEITRFH SIYWPIILKM LDLRIPNKLV SHGWILSNND
KMSKSLGNVV NPMDYIEEFG ADGLRFYIAN ELPIDKDGNF SREMFIESYN AYLANNIGNL
ISRVNNMITK YFDGHLGDDL SVSDEFIDSK ISQLIDDYKA NMDKYDIYTA TRKIVEFSAI
CNKYIEDKEP WNLDKENKTE ELRTVLMSLQ KAITVISFLL KPILVFTYDD MIEQTGIKDP
ENLTYGALKT FDNLSFNKLG DKKVLFQRIK K
//
