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