ID   A0A081ICC2_PLAVN        Unreviewed;       899 AA.
AC   A0A081ICC2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN   ORFNames=YYE_03918 {ECO:0000313|EMBL:KEG01330.1};
OS   Plasmodium vinckei vinckei.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=54757 {ECO:0000313|EMBL:KEG01330.1, ECO:0000313|Proteomes:UP000030681};
RN   [1] {ECO:0000313|EMBL:KEG01330.1, ECO:0000313|Proteomes:UP000030681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=vinckei {ECO:0000313|Proteomes:UP000030681};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium vinckei vinckei.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; KL446952; KEG01330.1; -; Genomic_DNA.
DR   RefSeq; XP_008625785.1; XM_008627563.1.
DR   AlphaFoldDB; A0A081ICC2; -.
DR   EnsemblProtists; KEG01330; KEG01330; YYE_03918.
DR   GeneID; 19962124; -.
DR   KEGG; pvv:PVVCY_0501920; -.
DR   Proteomes; UP000030681; Unassembled WGS sequence.
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; IPR041872; Anticodon_Met.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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:SF2; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF19303; Anticodon_3; 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; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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}.
FT   DOMAIN          237..369
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          384..591
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          621..738
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   899 AA;  104883 MW;  5F31A5705F4BCDE5 CRC64;
     MILYPNKYLL SGTLKCMLAA HIYKLPVELS DDFFFTRTFE VEKSLVVNKR PLLIYENKFV
     SSTNAICFLL HRLRNKGINV KSLDDKLRLY LTWIEWSDVL EKNIERLNKK KIIESLDLLE
     SYLSENINKE FICDGAEEIK REDGCDETDQ SQENGTCGIT LADIYVYTSL KYSNIVICNE
     SWSHINSYVE RINNLEDVQK VIETVEKVHK LKNIYSLFIS KICEKNINDH VKNENFYITT
     AINYVNGDPH IGHAYEIVLA DTIARYHRNL GRDLFFTTGA DEHGLKIANQ AARNNITPQE
     LCDQNVIKFK KLNKDLHTTE DYYVRTTAEI HKNIAQSIWT QCMENGDIYL GEYEGWYNVR
     EETYIPENEA KLMNYMDPLN NVKLEKMKEP SYFFRMSKYQ DRLLQHIHDN PDFIQPEKNR
     NEILQRLKEP LEDLSCSRTK FSWGIPVPND PKHVMYVWMD ALINYYSNCF INNQERMKYW
     PADIHIIGKD IVWFHAVIFP TILMSINIEL PKCIFSHGFV LAGDGKKMSK SLKNVIDPKE
     IIEAYGSDAF RFHVVKESKR GYDMRFDVDN LVDMCNSDLA DTIGNLVQRT LSLCFLSNNA
     KIPPLYDDID VELPFCMLHF INRIEYYMKN FHIHKFCEKT VNVCKDLNKF LTDLAPWKYK
     KESEQNKKLH IIRLMLESIY FIAHYIDIVV PMIASQIFSQ LNTPKKKIVD LNPWLNNLEE
     GVIINNDHVL FKKFEVESVK IKIQKVIMKL SKVIKVIEHG ELKNSTLYEI ETDDGKYIAL
     LNLPHNESHI NTLTVAIMNI KPLTINNITV TSIIPHVHKE IFKFSPDENI PVGTLIHAKN
     YKTLVKQRDN LTKKEINSLQ LSIINNNCFY EKNVPLVFGS SDNPFYHATQ TSGTLNFFS
//