ID A0A1Q6EXU8_9BACT Unreviewed; 475 AA.
AC A0A1Q6EXU8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamine--tRNA ligase {ECO:0000313|EMBL:OKY91473.1};
DE Flags: Fragment;
GN ORFNames=BHV65_16295 {ECO:0000313|EMBL:OKY91473.1};
OS Alistipes sp. 58_9_plus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1896970 {ECO:0000313|EMBL:OKY91473.1, ECO:0000313|Proteomes:UP000186889};
RN [1] {ECO:0000313|EMBL:OKY91473.1, ECO:0000313|Proteomes:UP000186889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=58_9_plus {ECO:0000313|EMBL:OKY91473.1};
RX PubMed=27819664; DOI=10.1038/nbt.3704;
RA Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.;
RT "Measurement of bacterial replication rates in microbial communities.";
RL Nat. Biotechnol. 34:1256-1263(2016).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363037}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKY91473.1}.
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DR EMBL; MNQG01000301; OKY91473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6EXU8; -.
DR Proteomes; UP000186889; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR004514; 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; 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 SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 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 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}.
FT DOMAIN 1..267
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 270..358
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 375..450
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OKY91473.1"
SQ SEQUENCE 475 AA; 55216 MW; 7D211A201E42E28C CRC64;
NFGLAKKYGG KCNLRFDDTN PVKEDVEYVD SIKRDIHWLG FDWAVERYAS DYFDQLYDWA
VVLIKKGLAY VDDQTQEQIR ENRGTVSVPG TPSPWRDRSV EEVLRAKIDM AHPNMLFRDP
IMYRIIHAEH HRTGDKWCIY PMYDYAHGQS DSIEQITHSI CTLEFDVHRP LYDWFIQALE
IFPSHQYEFA RLNLTYTMMS KRKLLKLVQE GAVMGWDDPR MPTICALRRK GYTPASVRNF
AEMVGVAKRD NVIDLGKLEY CVREDLNKVA QRRMAVLNPL KVVITNYDEN KTELFTAINN
PEDVIYIERD DFMEEPPKKF FRLSPGGEVR LRYSYLIKCE EVIKDAEGNV TELRCTYDPM
SGQGSSSDGR RVKGVIHWVS AKDAVEAEIR LFNPLFTKEN PDDVEEGQTW EDNLNPESMV
RIKGYLEPSL RDVPVGQAVQ FERVGYFCPD TDSTPEHLVF NRTVTLKDSW AKINK
//