ID   SYEC_NOSCE              Reviewed;         614 AA.
AC   C4VBI7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Probable glutamate--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
DE            Short=GluRS;
GN   ORFNames=NCER_102160;
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-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 2 subfamily. {ECO:0000305}.
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DR   EMBL; ACOL01000581; EEQ81415.1; -; Genomic_DNA.
DR   RefSeq; XP_002995086.1; XM_002995040.1.
DR   AlphaFoldDB; C4VBI7; -.
DR   SMR; C4VBI7; -.
DR   STRING; 578460.C4VBI7; -.
DR   EnsemblFungi; EEQ81415; EEQ81415; NCER_102160.
DR   KEGG; nce:NCER_102160; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_102160; -.
DR   HOGENOM; CLU_001882_1_2_1; -.
DR   InParanoid; C4VBI7; -.
DR   OMA; MRFAPNP; -.
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:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 1.10.1160.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF50715; SSF50715; 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..614
FT                   /note="Probable glutamate--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388393"
FT   MOTIF           135..144
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           359..363
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..132
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         303..307
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         359..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   614 AA;  70755 MW;  DD63B17BF1DEA37C CRC64;
     MAVENAINFR EICSLLDISE SYKCTINAFL DNVEKCTDKH YNDALNLLDT FFSNEVKSNS
     LVNDLIFCII NSNFDFLKVF KSNKLRLENL QIVYESAFNE NKPFLKEFSA KDKINKEVKK
     NLYSTPAVTR FAPEPSGCLH IGHLKALLVN YNLAEKSNGT LLLRFDDTNP VKNYEKYEKE
     ILRDLDTLGI TGLKISHSSD YFELLVDEAV SLINKNLAYV DNTDQETMRI ERFEGIESKM
     RNINNSESLK IFKELLQGRA PGYCLRAKID MSNPNKSMRD PVIYRASDKM HGRCKLYKAF
     PTYDFVCPIV DSIEGVTVVC RANEYKDRNE QYKWFLENLE LENKPEFNDF SKLNLEDTVL
     SKRKIDKLIS DSLVTGWDDP RLATIQGIKR LGMHMTALKD YINLQGASNK TNVISWDKIW
     AMNKKVIDPL SPRFMAVEKI NCVRVFITNF EGLKYTKNIP LNKKNTSLGS KDVLFSDTLL
     FSQEDGFVLK ENEEFTLMNW GNAIVEKKVV ENSIVTELYI KLHLEGDYKS TTNKISWVSE
     SGAVTATGIE YGKLLVNEEF NINSKIDKQY YVESSITNLS TDMKHVQFER IGFFYCDSPC
     VFHLVPFTKQ KRTY