ID   SYQ_DEIRA               Reviewed;         852 AA.
AC   P56926;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 151.
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};
GN   OrderedLocusNames=DR_2611;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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: In the N-terminal section; belongs to the class-I
CC       aminoacyl-tRNA synthetase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GatB/GatE family.
CC       {ECO:0000305}.
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DR   EMBL; AE000513; AAF12148.1; -; Genomic_DNA.
DR   PIR; A75253; A75253.
DR   RefSeq; NP_296330.1; NC_001263.1.
DR   PDB; 2HZ7; X-ray; 2.30 A; A=2-852.
DR   PDBsum; 2HZ7; -.
DR   AlphaFoldDB; P56926; -.
DR   SMR; P56926; -.
DR   STRING; 243230.DR_2611; -.
DR   PaxDb; 243230-DR_2611; -.
DR   EnsemblBacteria; AAF12148; AAF12148; DR_2611.
DR   KEGG; dra:DR_2611; -.
DR   PATRIC; fig|243230.17.peg.2858; -.
DR   eggNOG; COG0008; Bacteria.
DR   eggNOG; COG0064; Bacteria.
DR   HOGENOM; CLU_001882_3_0_0; -.
DR   InParanoid; P56926; -.
DR   OrthoDB; 9801560at2; -.
DR   BioCyc; MetaCyc:MONOMER-14055; -.
DR   BRENDA; 6.1.1.18; 1856.
DR   EvolutionaryTrace; P56926; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; EXP:DisProt.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00807; GlnRS_core; 1.
DR   DisProt; DP02496; -.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00126; Gln_tRNA_synth; 1.
DR   InterPro; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
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_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; PF02637; GatB_Yqey; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 2.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..852
FT                   /note="Glutamine--tRNA ligase"
FT                   /id="PRO_0000195832"
FT   REGION          1..635
FT                   /note="Glutaminyl-tRNA synthetase"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..852
FT                   /note="GatB-like"
FT   MOTIF           74..84
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   MOTIF           308..312
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   COMPBIAS        533..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..659
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         252
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           85..97
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           116..129
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           140..143
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           144..156
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           167..174
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   TURN            185..188
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           191..202
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   TURN            240..242
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          247..250
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           252..263
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          266..271
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   TURN            275..277
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           278..287
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          295..299
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          302..304
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           311..319
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          322..325
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           334..340
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           344..353
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           365..377
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          385..394
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          401..408
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           410..414
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          424..426
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           431..433
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          435..440
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          442..447
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           448..450
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          467..470
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   TURN            471..473
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          474..483
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          489..496
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   TURN            512..514
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          516..523
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          526..530
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           566..569
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          574..582
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           584..588
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          594..597
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   TURN            598..600
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          601..605
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   HELIX           607..611
FT                   /evidence="ECO:0007829|PDB:2HZ7"
FT   STRAND          621..626
FT                   /evidence="ECO:0007829|PDB:2HZ7"
SQ   SEQUENCE   852 AA;  93471 MW;  82911AA229D25F79 CRC64;
     MGAFGWEQDR GAPFSGRSPR ILTRMTDAPR PTAGADAPAR PPAAPLVAPN FITEIIERDL
     EAGKYPRVVT RFPPDPSGYA HLGHVFASLL DFNTARQYGG QFNLRMDDTN PELARQEYVD
     SIADDLKWLG LDWGEHFYYA SDYFDRYYAY AEQLIRQGDA YVESVSPEEL SRLRGNATTP
     GTPSPYRDRS VEENLDLLRR MKAGEFADGE HVLRAKIDLT APNMKLRDPV LYRIVNKPHF
     RTSDEWHIYP AYDFEHPLQD AIEGVTHSMC SLEFVDNRAI YDWLMEKLNF DPRPHQYEFG
     RRGLEYTITS KRKLRELVQA GRVSGWDDPR MPTLRAQRRL GVTPEAVRAF AAQIGVSRTN
     RTVDIAVYEN AVRDDLNHRA PRVMAVLDPV KVTLTNLDGE KTLSLPYWPH DVVRDSPDGL
     VGMPGGGRVA PEEAVRDVPL TRELYIERDD FSPAPPKGFK RLTPGGTVRL RGAGIIRADD
     FGTDEAGQVT HIRATLLGED AKAAGVIHWV SAERALPAEF RLYDRLFRVP HPEGENADVE
     DDSAGPAEHE AEPGAGQETA PVSQGFMRYL TPDSLRVLRG YVEPSVAGDP ADTRYQFERQ
     GYFWRDPVEL ERVDSREDAL VFGRIITLKD TWGKQGGGTQ QKAEGKKRPS TKGRGPDEVR
     GEGSSSPAKA HAPKAQPLTP EQDAEFTRLL GLGASEGDAR TIARDPALLA FVGGAAPGDT
     FAQVASWTVN ELVAGLRAGE VKVRAADLAP LAEGVASGQL SARIAREALA RAAASGDAPL
     TIIEREGLNA GLSAEALQQV VAQVIAANPD KAEAYRGGKT ALLGFFTGQV MRATAGKADP
     QALAAALKDA LA
//