SYEC_ENTBH
ID SYEC_ENTBH Reviewed; 631 AA.
AC A9CSZ1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=EBI_22577;
OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterocytozoon.
OX NCBI_TaxID=481877;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA Keeling P.J.;
RT "Patterns of genome evolution among the microsporidian parasites
RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT bieneusi.";
RL PLoS ONE 2:E1277-E1277(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT Enterocytozoon bieneusi.";
RL PLoS Pathog. 5:E1000261-E1000261(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; ABGB01000003; EDQ31175.1; -; Genomic_DNA.
DR RefSeq; XP_001828010.1; XM_001827958.1.
DR AlphaFoldDB; A9CSZ1; -.
DR SMR; A9CSZ1; -.
DR STRING; 481877.A9CSZ1; -.
DR EnsemblFungi; EDQ31175; EDQ31175; EBI_22577.
DR VEuPathDB; MicrosporidiaDB:EBI_22577; -.
DR HOGENOM; CLU_001882_1_2_1; -.
DR InParanoid; A9CSZ1; -.
DR Proteomes; UP000001742; 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..631
FT /note="Probable glutamate--tRNA ligase, cytoplasmic"
FT /id="PRO_0000388392"
FT MOTIF 144..153
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 367..371
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 139..141
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 311..315
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 367..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 631 AA; 73962 MW; 4DC6852631BEA04D CRC64;
MLENISKSEF VNFLLEKKHN IEPKTLPILE QHIREQKLDD FFLDFSIDFT DEELNNFLSK
LDYWLKNTKL NSSKADVIFG LLYSCNKFIK LIKNPTFSFV EIKQFYNDIL NTNKNYIIEY
NKKDKGKINI AVEGNVVTRF PPEPSGFLHI GHIKAALLND LMAKNGKLLI RFDDTNPIKE
EKMYENVIIE DLHTLGIKNY TIVRSSDHFD SLYNYAIQLI QLGLAYCDNT DQLQMREERT
KGIPSKNRNT DIETNLSIFS KMSSGNCLDY CLRAKIDYTN LNKALRDPVI YRHIEKEHNI
TKNKYKIYPT YDFACPIIDS LDGVTLALRT NEYRDRNEQY YWFLEKLNLP NKPKIYDFSR
LNFENTVLSK RQMKFYVDNH FVSGWDDPRL STLRGILRLG MDIDTLKEYI INQGSSQKSS
VISWDKVWSL NKKNIDHKSA RYSAIPKLYC VECLILDKNN NEIITKTEDI PKFKKNLSLG
NKTIIKSSHI LISQEDANIL NNNEEFTLMN WGNMKVKEKQ IVNGIIIKII LEENLAGDVK
TTKNKLTWVN KENIIEFKIL EYDTLQNDKN TDNLAEKFNT NSKKEEIWLG EKALISVSPK
TYIQIERIGF FICDKPLEFI LIPYTKQKRM R
