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Database: UniProt
Entry: A0A1Z9W3B5_9GAMM
LinkDB: A0A1Z9W3B5_9GAMM
Original site: A0A1Z9W3B5_9GAMM 
ID   A0A1Z9W3B5_9GAMM        Unreviewed;       548 AA.
AC   A0A1Z9W3B5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
DE   AltName: Full=50S ribosomal protein L25 {ECO:0000256|ARBA:ARBA00035479};
GN   ORFNames=CBC51_00745 {ECO:0000313|EMBL:OUX72117.1};
OS   Oceanospirillales bacterium TMED91.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX   NCBI_TaxID=1986769 {ECO:0000313|EMBL:OUX72117.1, ECO:0000313|Proteomes:UP000196344};
RN   [1] {ECO:0000313|EMBL:OUX72117.1, ECO:0000313|Proteomes:UP000196344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED91 {ECO:0000313|EMBL:OUX72117.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, 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:OUX72117.1}.
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DR   EMBL; NHES01000005; OUX72117.1; -; Genomic_DNA.
DR   Proteomes; UP000196344; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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|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}.
FT   DOMAIN          24..332
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          336..435
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          454..524
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
SQ   SEQUENCE   548 AA;  62529 MW;  3DFF4F2B3F6DA4E8 CRC64;
     MSEKPTNFIR TKIADQIKQG QISEIVTRFP PEPNGYLHVG HAKSICLNFG LAEEFGGRCH
     LRFDDTNPEK ESQEYIDAIE NDVRWLGFEW SKLCHTADYF EQLFDWALHL IRNGDAYVDE
     QSAEAMRLNR GTLTEPGIDS PYRDRSPEEN EALFCKMRDG ELPEGAAVLR AKISMSAPNV
     NLRDPALYRI RNIAHPRAGD QWCIYPTYDY AHGQSDAIEG XTHSLCTLEF EDHRPLYEWL
     LKKLPVPSRP KQTEFSRLEL EGTVTSKRKL NALVQXXHVS GWDDPRMPTX AGMRRRGYSP
     EGIRLFCERI GVTRKPNTIE LQXLEGSVRD DLEGRAHKAM XVLDPLKVVV TNWDQXPLEL
     TVPWXXXRPE FGSRTMXFGR ELYXDRSDFA LXPPEGFFRL IPGGSVRLKY GFIVDFDDVV
     IGDDGQVSEV HVRYDPATRS GQDQSGRKVK GTXHWVHAEX XCAVDVHLYD RLFTVPDPGS
     YDDPASVINX ESLRVGXAWA EPSLQTLMPE AYFQFERVGF FKQDXASEAG RMIYNRSVTX
     KDAWAKKQ
//
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