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Database: UniProt
Entry: A0A1G5CLQ5_9FIRM
LinkDB: A0A1G5CLQ5_9FIRM
Original site: A0A1G5CLQ5_9FIRM 
ID   A0A1G5CLQ5_9FIRM        Unreviewed;       572 AA.
AC   A0A1G5CLQ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN   ORFNames=SAMN02910292_00662 {ECO:0000313|EMBL:SCY03415.1};
OS   Lachnospiraceae bacterium XBB2008.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520826 {ECO:0000313|EMBL:SCY03415.1, ECO:0000313|Proteomes:UP000199089};
RN   [1] {ECO:0000313|EMBL:SCY03415.1, ECO:0000313|Proteomes:UP000199089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XBB2008 {ECO:0000313|EMBL:SCY03415.1,
RC   ECO:0000313|Proteomes:UP000199089};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000948};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363037}.
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DR   EMBL; FMVL01000004; SCY03415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5CLQ5; -.
DR   STRING; 1520826.SAMN02910292_00662; -.
DR   OrthoDB; 9801560at2; -.
DR   Proteomes; UP000199089; 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:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004514; Gln-tRNA-synth.
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; 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   NCBIfam; TIGR00440; glnS; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 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 {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363037};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363037};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199089}.
FT   DOMAIN          39..352
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          356..455
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          472..545
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
SQ   SEQUENCE   572 AA;  65533 MW;  E3C04516B73260B0 CRC64;
     MSEISPANTT EEVKEQSDSR NFIQRMIDED LKEGVYDTVN TRFPPEPNGY LHIGHAKSIL
     LNYGLAKEYG GKFNLRFDDT NPTKEKTEFV ESIKADVKWL GADFEDRLFF ASDYFDKMYE
     GAITLIKKGK AYVSDLTADE IREYRGTLTE PGKDDPSRNR SVEENLELFE KMKNGEYADG
     EKTLRAKIDM AAANINMRDP IIYRVAHMTH HNTGDKWCIY PMYDYAHPIE DAIEGITNSI
     CTLEFEDHRP LYDWVLIETG YKNAPNEAPK QTEFAKMYLT NVVTGKRYIK KLVEDGIVDG
     WDDPRLVSIA ALRRRGFTPE SIQMFVELCG VSKANASAEY SMLEYCIRED LKVKRPRVMA
     VLDPVKLIID NYPEGVTEEL EVQNNLENES LGMRKVPFSR ELYIDREDFM EEPPKKYFRL
     FPGNEVRLMN AYFVTCTSFE KDADGNVTVI HCTYDPESKG GNSPDGRKVK GTIHWVNAAT
     ALKCTVRLYE NIIDEEKGVY NEDGSLNLNP NSLTTLDNCF VEPSLKDAKA YESFQFVRQG
     FFTVDYKDSK PGEPVFNRIV SLKSSFVLPK KD
//
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