ID   SYQ_ENTBH               Reviewed;         691 AA.
AC   A9CSU5;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Probable glutamine--tRNA ligase;
DE            EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE   AltName: Full=Glutaminyl-tRNA synthetase;
DE            Short=GlnRS;
GN   ORFNames=EBI_22570;
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-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC         glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC         Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC         ChEBI:CHEBI:456215; EC=6.1.1.18;
CC         Evidence={ECO:0000250|UniProtKB:P47897};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; ABGB01000003; EDQ31158.1; -; Genomic_DNA.
DR   RefSeq; XP_001827993.1; XM_001827941.1.
DR   AlphaFoldDB; A9CSU5; -.
DR   SMR; A9CSU5; -.
DR   STRING; 481877.A9CSU5; -.
DR   VEuPathDB; MicrosporidiaDB:EBI_22570; -.
DR   HOGENOM; CLU_001882_2_3_1; -.
DR   InParanoid; A9CSU5; -.
DR   OMA; FAWRIMG; -.
DR   OrthoDB; 934at2759; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..691
FT                   /note="Probable glutamine--tRNA ligase"
FT                   /id="PRO_0000388382"
FT   MOTIF           196..206
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           436..440
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         197..199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         203..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         229
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         381
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         429..430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         437..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
SQ   SEQUENCE   691 AA;  80660 MW;  1F11DE3091ADF9CF CRC64;
     MNLDDKLRGI SLSDEKINEL KTKPNLIKNM EVIVNTGNNF TKMQYSLACI APKNCNLIEL
     SNLIEEGYVT NDSLLKGLVK LGKKSKDEYI DFCKKHTYNE QDIINFIRLL KEKKETKATI
     SSKLKEQYLY YDTKIFLKEM ENYNLNVPME KYTKNWLDEG EIKFLHKPGE NPQKTKKIME
     DHLKRTGGKV ITRFPPEPNG NLHIGHAKAL NLSFEYAKKF NGITYLRFDD TNPKNESNEL
     YNGIIEDVKW LGFEPYAITA SSDHFEAMHE MAKTLIKKNK SYVCFCSLEE IRARRSKYQK
     ERDEGNDDPL ILSPYRNTSV EQNLIEFEKM LKGEYKDGEA VLRFKMPLKS KNPLMLDLVG
     ARIINMVHDR KQKNYIVYPS YEFALCVCDS LEDITHSFCS REFYTRQEPY HWLLQELDMY
     EPVQWEFSRL NISNTVLSKR KLTKIVDEGL NWDDPRFYTI KGMRRRGFPA SAINKFVQSV
     GITFSETIID VKILESFVLK ELMQIAKKAT CIINPLKVYI NKCTTGIISN EPVDVNNIIY
     IDKDDFDETN NSDFLRLTKI QPVGLINLGV LKYIKDESDG IRCELLTVDE CKPNKFIQWL
     PNLDNKVELR MYKPLFKSFD PDEIGYMNDI DLTNSLEIID GYVDNTVLNT HIEDKFQFIR
     IGFFCCDFDS IINDNQKKLV FNLTLPLNKN Y
//