SYMC_NOSCE
ID SYMC_NOSCE Reviewed; 560 AA.
AC C4V943;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Probable methionine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN ORFNames=NCER_101052;
OS Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX NCBI_TaxID=578460;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRL01;
RX PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT pathogen of honey bees.";
RL PLoS Pathog. 5:E1000466-E1000466(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEQ82257.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; ACOL01000084; EEQ82257.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_002995928.1; XM_002995882.1.
DR AlphaFoldDB; C4V943; -.
DR SMR; C4V943; -.
DR STRING; 578460.C4V943; -.
DR EnsemblFungi; EEQ82257; EEQ82257; NCER_101052.
DR KEGG; nce:NCER_101052; -.
DR HOGENOM; CLU_009710_1_2_1; -.
DR InParanoid; C4V943; -.
DR Proteomes; UP000009082; Unassembled WGS sequence.
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..560
FT /note="Probable methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000388398"
FT MOTIF 16..26
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 347..351
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 560 AA; 65264 MW; A52A29503EC6867A CRC64;
MKKKFLVKKI ITSALPYVNN QPHLGNIIGC VLSADMYARF CRKNNEDVVF LSGTDEYGTA
IEMAAFAQNK TPLQICEENR IIHKKIYDWF NIDFDFFGHT TSTAHTKNVQ DFFNKIHNNG
FFTEQEIEQF FCDKCQIFLA DRYVVGTCKF CKYTDAKGDQ CDGCGHTYKS LDLIDAKCTL
CHSFPNIKST RHLFFDFNNF KDKLQKLFNT NSQYWSENGK QITKSWLDQE LLPRCMTRDL
KNRWGVPVPL KDFEEKVFYV WFDAVIGYFT FYKEYVAARS ESKELDKNNV FATDNILQDC
ELVQFMGKDN VFFHTIVFPS LIFATNDSYP LIKKLSVTEF LLFENEKFSK SRGHGIFGLD
LVDNTMGQSC LWRYYLAKIR PEKCDSNFSF THFTNVIDAD LNNNIGNFCN RVLKYIKNKN
DKLISIDKLE HRDDLMVQTI DKIYKEYLTS FSAIRIREAL EKILEISKVG NEYVQQVVSS
KIEVPKGFQV AFSIVVLIGQ LLEPFIPVSS EKLLKMCNRK KENFCESFYI IKSAEIGDDI
KPLFNKLDDS LIERIKNFKK