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SYMC_ENCCU
ID   SYMC_ENCCU              Reviewed;         550 AA.
AC   Q8SQW5;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable methionine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   OrderedLocusNames=ECU11_0890;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590450; CAD25999.1; -; Genomic_DNA.
DR   RefSeq; NP_586395.1; NM_001042228.1.
DR   AlphaFoldDB; Q8SQW5; -.
DR   SMR; Q8SQW5; -.
DR   STRING; 284813.Q8SQW5; -.
DR   GeneID; 860048; -.
DR   KEGG; ecu:ECU11_0890; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0890; -.
DR   HOGENOM; CLU_009710_1_2_1; -.
DR   InParanoid; Q8SQW5; -.
DR   OMA; MTTQLYC; -.
DR   OrthoDB; 333013at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.20.28.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   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   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..550
FT                   /note="Probable methionine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388397"
FT   MOTIF           10..20
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           328..332
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  63533 MW;  A1846D3602AEFBDD CRC64;
     MKKFITSALP YVNNQPHLGN IIGSVLSGDV YSRYCKKKGE VSVYICGTDE YGTAIEMEAI
     SQGVTPLEIC EKNRKLHKQV YDWFNIDFDY FGFTSSATHT GLVQDLFMKM YDNGHFSEVE
     IEQFYCEHCG LFLADRFIVG ECKFCGDGRA RGDQCDSCGH TYNSLELLSP RCSICSSSPV
     VRATTHLFFD LEAFRPSLEE LYRTNGHLWS QNAQNIFRQW ISMEFYPRCM TRDLKFNWGV
     PVPLEKFKEK VFYVWFDAPI GYLTFLKELV GEDFGEWCKD AELVQFMGKD NVAFHTVIFP
     AMLYATGEKY PVVRRLSATE YLQFENEKFS KSRRHGIFGL DLVGGGLGKS CMWRYYLLKI
     RPESTKDSNF TFSDFRQSVT ADLINNLGNF VNRVLKYIQS KCNSRVSLLE LDSGDKKCIE
     DVNELYCKYK AKMEEIKLRE ALQVVMEICR RGNEYIQEGV RSRDRKGHFF CLGFSIIGLV
     GTLLHPFIPV TSLEILRMCN LEETMFPESM RIVDGHTMGS DIRPLFEDFT TEQIEEMKRY
     DRPQSTGCSK
 
 
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