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Database: UniProt
Entry: A0A285NYE0_9PSED
LinkDB: A0A285NYE0_9PSED
Original site: A0A285NYE0_9PSED 
ID   A0A285NYE0_9PSED        Unreviewed;       562 AA.
AC   A0A285NYE0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Glutamine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00126};
DE            EC=6.1.1.18 {ECO:0000256|HAMAP-Rule:MF_00126};
DE   AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00126};
DE            Short=GlnRS {ECO:0000256|HAMAP-Rule:MF_00126};
GN   Name=glnS {ECO:0000256|HAMAP-Rule:MF_00126};
GN   ORFNames=SAMN05660463_02257 {ECO:0000313|EMBL:SNZ12906.1};
OS   Pseudomonas sp. URIL14HWK12:I9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1261633 {ECO:0000313|EMBL:SNZ12906.1, ECO:0000313|Proteomes:UP000232228};
RN   [1] {ECO:0000313|EMBL:SNZ12906.1, ECO:0000313|Proteomes:UP000232228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URIL14HWK12:I9 {ECO:0000313|EMBL:SNZ12906.1,
RC   ECO:0000313|Proteomes:UP000232228};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-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, ECO:0000256|HAMAP-
CC         Rule:MF_00126};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00126}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00126}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00126,
CC       ECO:0000256|RuleBase:RU363037}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00126}.
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DR   EMBL; OBEM01000004; SNZ12906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285NYE0; -.
DR   OrthoDB; 9801560at2; -.
DR   Proteomes; UP000232228; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00807; GlnRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00126; Gln_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004514; Gln-tRNA-synth.
DR   InterPro; IPR022861; Gln_tRNA_ligase_bac.
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; GLUTAMINE-TRNA LIGASE; 1.
DR   PANTHER; PTHR43097:SF5; GLUTAMYL-TRNA SYNTHETASE; 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|HAMAP-Rule:MF_00126};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00126};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00126};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00126};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00126};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00126}; Reference proteome {ECO:0000313|Proteomes:UP000232228}.
FT   DOMAIN          37..346
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          349..448
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          464..540
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT   MOTIF           277..281
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT   BINDING         44..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT   BINDING         50..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT   BINDING         76
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT   BINDING         221
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT   BINDING         240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT   BINDING         270..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
SQ   SEQUENCE   562 AA;  63884 MW;  EC4AE244EC51BBE0 CRC64;
     MSKPTADSSA AKAPVAPTNF LRPIVQADLD AGKHTAIVTR FPPEPNGYLH IGHAKSICVN
     FGLAQEFGGA CNLRFDDTNP AKEDQEYIDA IKSDVQWLGF QWAGEPRYAS DYFDQLHDWA
     VELITAGKAY VCDLTPEQAR EYRGSLTEPG KNSPFRDRPV EESLDLFARM KAGEFEDGAR
     VLRAKIDMAS PNMNLRDPIL YRIRHAHHHQ TGDKWCIYPN YDFTHGQSDA IEGVTHSICT
     LEFEGHRPLY DWFLDNLSVP CKPRQYEFSR LNLNYTITSK RKLKQLVDEK HVAGWDDPRM
     STLQGFRRRG YTPASIRNFC DMIGTNRSDG VVDMNMLEFS IREDLDQNAP RAMCVLRPLK
     VVITNYPENE AQTLELVRHP KQDMGTRQLP FARELYIDRE DFMEAPPKGY KRLEPGGEVR
     LRGAYVIRAD EAVKDAQGNI VELRCSYDPD TLGKNPEGRK VKGVIHWVPA QASVECEVRL
     YDRLFRSPNP EKTEEGGTFL DNINPDSLKV LSGCRAEPSL AQAAPEDRFQ FEREGYFCAD
     LKDHTAAKPV FNLTVTLRDS WS
//
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