ID   A0A078AZR4_STYLE        Unreviewed;       822 AA.
AC   A0A078AZR4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   13-SEP-2023, entry version 33.
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   Name=Contig18252.g19396 {ECO:0000313|EMBL:CDW86687.1};
GN   ORFNames=STYLEM_15785 {ECO:0000313|EMBL:CDW86687.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW86687.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW86687.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW86687.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001234};
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; CCKQ01014886; CDW86687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078AZR4; -.
DR   EnsemblProtists; CDW86687; CDW86687; STYLEM_15785.
DR   InParanoid; A0A078AZR4; -.
DR   OMA; HLNTTEY; -.
DR   OrthoDB; 1341752at2759; -.
DR   Proteomes; UP000039865; 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; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 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; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 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:UP000039865}.
FT   DOMAIN          250..649
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          665..821
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   822 AA;  94341 MW;  10C1C754AA533DE5 CRC64;
     MQKKDISQTS AIKAKITIVN QNLSSFFIEN LLKVLNVDVP VKKQTSANPV NSLDVTNVKL
     QIENGPTIYG ELNVADFLVS QHNKTLSQAD VAGGKQLLTL GKDLSFDHWA YYLNAHLKGT
     VHAFQTDKTN AIKELLKKQL KEISDNLYAD LFEEDGKFSG QSGLFLQVLF YSFVQPVQQQ
     NNNDIKKKMP VFRDLHKLPT SEEYKGSEQE KAAPKKIVNQ KEVTYCTSDA KIKRVNFHRN
     LVPNKEQRNI LITSALPYVN NVPHLGNIIG CVLSADVFAR YARLMGYNTL YICGTDEYGT
     ATETKALEEK KTPKEICDHY FEIHKRIYEW FDCDFDHFGR TTTKQQTKIA QDIFKRLHEN
     GYTYEEIVDQ QFCLKCERFL ADRLVAGTCP LCNFYDAKGD QCDGCGKLLN ANELIDPKCK
     VCASTPEIRQ SQHIFIDLAK IQPQHEAWFD KAHLKGQWAS NAIQFTNALL KEGLKGRCIT
     RDLKWGTSVP LDEYSNKVFY VWFDAPIGYL SITANYNEEN WEKWWLNNDD VQLYQFMGKD
     NITFHTVIFP CTLVGTHDPY TMLHHIATTE FLNYEIDPLT KKPKKFSKTR QTGVFGDDAI
     KTGIPSEVWR YYLLINRPES QDTVFLWNDL QAKNNNELLA NPGNFSNRLL KFVQSSLNQK
     IPDYSGEIHA DDSKFIEAIY SQFQLYVEQM EHVKIKDALK TVMNFSSLCN VYMQDNKPWD
     LKKQNNNERC SQVVNTALNA LRLLCSLFEP FMPSFSAKVY EQLNHERTVD DETVLGQING
     HPERILKLLK AGHQIGAPAP IFREISNEEI GRWRKEFGGG NQ
//