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SYQ_ALISL
ID   SYQ_ALISL               Reviewed;         552 AA.
AC   B6EHL7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126};
DE            EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126};
DE   AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126};
DE            Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126};
GN   Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126}; OrderedLocusNames=VSAL_I0832;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00126};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00126}.
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DR   EMBL; FM178379; CAQ78517.1; -; Genomic_DNA.
DR   RefSeq; WP_012549619.1; NC_011312.1.
DR   AlphaFoldDB; B6EHL7; -.
DR   SMR; B6EHL7; -.
DR   STRING; 316275.VSAL_I0832; -.
DR   PRIDE; B6EHL7; -.
DR   EnsemblBacteria; CAQ78517; CAQ78517; VSAL_I0832.
DR   KEGG; vsa:VSAL_I0832; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_001882_2_3_6; -.
DR   OMA; INNFCAQ; -.
DR   OrthoDB; 142899at2; -.
DR   Proteomes; UP000001730; Chromosome 1.
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   Gene3D; 2.40.240.10; -; 2.
DR   Gene3D; 3.40.50.620; -; 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; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00440; glnS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..552
FT                   /note="Glutamine--tRNA ligase"
FT                   /id="PRO_1000095476"
FT   MOTIF           34..44
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   MOTIF           268..272
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         35..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         41..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         67
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         212
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         261..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         269..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ   SEQUENCE   552 AA;  63726 MW;  706EECD302DEB027 CRC64;
     MSETETRPTN FIRQIIDEDL KSGKHSSVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYQG
     QCNLRFDDTN PEKEDIEYVE SIKNDVKWLG FDWSGDIHYS SNYFDKLYDY AVELIEKGLA
     YVDELTSDQI REYRGSLKEP GKNSPYRDRS VEENLALFEQ MRDGKFKEGT ICLRAKIDMA
     SSFIVMRDPV IYRIRFATHH QTGDKWCIYP MYDFTHCISD ALEGITHSIC TLEFQDNRRL
     YDWVLENITI DCQPHQYEFS RLNLEYTIMS KRKLNELVTE KLVNGWDDPR MPTVSGLRRR
     GFTAGSIREF CKRIGVTKQE NMIEFGSLES CIRDDLNENA PRAMAVLEPV KVVIENYEEG
     KVETLNVANH PNKPEMGTRE VPFTREIYIE QDDFREEANK KYKRLVLGKE VRLRGAYVIQ
     ANRIEKDEAG NITTIFCSYD TETLGKNPAD GRKVKGVIHW VSADKAFPAE IRLYDRLFTV
     PNSAALEDFS ESINPESLIT KQGFVEPSLV TAEAEAGYQF ERTGYFCIDN KDSTPEALVF
     NRTVGLRDTW EG
 
 
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