ID A0A1V3RR75_9BURK Unreviewed; 426 AA.
AC A0A1V3RR75;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
DE Flags: Fragment;
GN ORFNames=B0E41_24400 {ECO:0000313|EMBL:OOG79317.1};
OS Hydrogenophaga sp. A37.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG79317.1, ECO:0000313|Proteomes:UP000189189};
RN [1] {ECO:0000313|EMBL:OOG79317.1, ECO:0000313|Proteomes:UP000189189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A37 {ECO:0000313|EMBL:OOG79317.1,
RC ECO:0000313|Proteomes:UP000189189};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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 -!- 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:OOG79317.1}.
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DR EMBL; MUNZ01000184; OOG79317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3RR75; -.
DR STRING; 1945864.B0E41_24400; -.
DR OrthoDB; 9801560at2; -.
DR Proteomes; UP000189189; 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: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; IPR014729; Rossmann-like_a/b/a_fold.
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 PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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 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|RuleBase:RU363037};
KW Reference proteome {ECO:0000313|Proteomes:UP000189189}.
FT DOMAIN 66..385
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 426
FT /evidence="ECO:0000313|EMBL:OOG79317.1"
SQ SEQUENCE 426 AA; 48395 MW; 889C3DCA747B8186 CRC64;
MSSNTPSNAP KNNANATAAE GEHKVSNFLR QIIENDLEKG TYSQRRWAGT PGDAAHHAAG
QPDPAKIRTR FPPEPNGYLH IGHAKSICLN FGLARDYGGV CHMRFDDTNP EKEDTEYVNS
ILDAVQWLGF QWEANGQSHL FQASDYFDFM YRAAEYLIEA GHAYVDEQTG EQMRAARGDF
GKPGVDSPFR SRTPEQNLAR FREMRDGAHE DGSMVLRATI DMASPNINLR DPAIYRIRRA
THHNTGDTWC IYPMYTFAHP IEDALEQITH SICTLEFEDQ RPFYDWLMDR LCEGGLLAHP
APHQYEFARL NLTYVITSKR KLAQLVYDHK VSGWDDPRMP TIVGLRRRGY TPESIQLFAE
RIGVTKSDSW IDYSTLEGCL REDLENKAHR GMAVLDPVKL VLTNWAEAFG ADDYTEDCTQ
PALPHH
//
