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Database: UniProt
Entry: Q6YQZ0_ONYPE
LinkDB: Q6YQZ0_ONYPE
Original site: Q6YQZ0_ONYPE 
ID   Q6YQZ0_ONYPE            Unreviewed;       520 AA.
AC   Q6YQZ0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 133.
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:BAD04318.1};
GN   OrderedLocusNames=PAM_233 {ECO:0000313|EMBL:BAD04318.1};
OS   Onion yellows phytoplasma (strain OY-M).
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX   NCBI_TaxID=262768 {ECO:0000313|EMBL:BAD04318.1, ECO:0000313|Proteomes:UP000002523};
RN   [1] {ECO:0000313|EMBL:BAD04318.1, ECO:0000313|Proteomes:UP000002523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY-M {ECO:0000313|Proteomes:UP000002523};
RX   PubMed=14661021; DOI=10.1038/ng1277;
RA   Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA   Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT   "Reductive evolution suggested from the complete genome sequence of a
RT   plant-pathogenic phytoplasma.";
RL   Nat. Genet. 36:27-29(2004).
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|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|HAMAP-Rule:MF_01228}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
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; AP006628; BAD04318.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6YQZ0; -.
DR   STRING; 262768.PAM_233; -.
DR   KEGG; poy:PAM_233; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_14; -.
DR   BioCyc; OYEL262768:G1G26-279-MONOMER; -.
DR   Proteomes; UP000002523; Chromosome.
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; IPR041872; Anticodon_Met.
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: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.
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}; Cytoplasm {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}.
FT   DOMAIN          143..365
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          404..493
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   MOTIF           18..28
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   MOTIF           302..306
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   520 AA;  60083 MW;  06760C0ACEEA47F8 CRC64;
     MKTTPNQKPK FFLSTAIAYA SGIPHIGNVY ESILADAIAR FKRLEGFDVL FQTGTDEHGQ
     KIAAKALQQG KNPQEYVDQI SLEIKRIYDL MQVSYDKFAK TTNPHHKQTV QAIFYKLWQQ
     GDIYLGKYQG LYSVAEESYV AAKDLIDGKT FNGETPILIS EETYFFKLSK YQAQLLQYLE
     NNPSLIKPDA QRKELLNLLK EPLADLSVSR TSFKWGIPVP FDPKHVIYVW IDALSNYLTG
     LDYNPTSKNS QFNRYWPCDM HVIGKDILRF HLIYWPILLM ALEISLPKQF LTHPWILFDK
     NKMSKSKGNV LYVDDLLKYF PVDSIRYFVL SEIPYAQDGN ITYELLVERH NSDLANVLGN
     LVHRVFGMVK SYRQNNLSKT LITTNLDPKF DLSKQALATL PLVRLKMQDC KVGDSLKEIM
     NLARFANKYI DLVEPWNLFK NPEKQQLLDH TLYSLVETLR FLGVLLQPFL PQTAHKILTQ
     LKASDITFES LDTFGLLSSQ KLDNYHILFN RLEIDEVLPR
//
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