ID   SYM_MIMIV               Reviewed;         550 AA.
AC   Q5UR82;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=MARS; OrderedLocusNames=MIMI_R639;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
RX   PubMed=17855524; DOI=10.1128/jvi.01107-07;
RA   Abergel C., Rudinger-Thirion J., Giege R., Claverie J.-M.;
RT   "Virus-encoded aminoacyl-tRNA synthetases: structural and functional
RT   characterization of Mimivirus TyrRS and MetRS.";
RL   J. Virol. 81:12406-12417(2007).
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         Evidence={ECO:0000269|PubMed:17855524};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.13 uM for tRNA-Met {ECO:0000269|PubMed:17855524};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AY653733; AAV50900.1; -; Genomic_DNA.
DR   RefSeq; YP_003987159.1; NC_014649.1.
DR   SMR; Q5UR82; -.
DR   PRIDE; Q5UR82; -.
DR   GeneID; 9925283; -.
DR   KEGG; vg:9925283; -.
DR   SABIO-RK; Q5UR82; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IDA:CAFA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IDA:CAFA.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.20.28.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR029038; MetRS_Zn.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR45765; PTHR45765; 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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..550
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139273"
FT   MOTIF           10..22
FT                   /note="'HIGH' region"
FT   MOTIF           336..340
FT                   /note="'KMSKS' region"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  63682 MW;  73B46C988F19465F CRC64;
     MQKFFVTSAL PYPNNSSPHL GNLVGALLSG DVYARFKRNQ GHEVIYLCGT DEYGTTTMIR
     ARKEGVTCRE LCDKYFELHK KVYDWFNIEF DVFGRTSTTK QTEITWEIFN GLYNNGYIEE
     KTTVQAFCEK CDMYLADTYL KGYCYHDGCR ENRVISNGDQ CEICQKMIDV NKLINPFCSI
     CLTPPIQKST DHLYLSLDKL TPLVQQYLDR VEFDSRIMAI SKAWLEIGLN PRCITRDLEW
     GTPIPINLDP KLEKYADKVF YVWFDAPIGY YSILANERDD WREWLNSGVT WVSTQAKDNV
     PFHSIVFPAS VIGSNIELPL IDRICGTDYL LYEGQKFSKS QGVGLFGDKV AEISPKLGIN
     EDYWRFYLMK IRPETQDSSF NLEEFVRIVK TDLVNNIGNF INRVFSLLEK TPYRDLNYQI
     SPEYIEFIKK YEVSMDEFKF RDGLKICLEM SSRGNKFVQS TKPWTMIKDG LDTQEIMTEA
     VGICWILLNL LKPIIPKSAC DMLSNLDTDN QNIFCLIGGS NINIRILNII KLPFKNIDLK
     QLREFIEGKN