SYQ_DEIRA
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 03-AUG-2022, entry version 143.
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=DR_2611;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; 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 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
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 RefSeq; WP_010889235.1; NZ_CP015081.1.
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 PRIDE; P56926; -.
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 OMA; INNFCAQ; -.
DR OrthoDB; 142899at2; -.
DR BioCyc; MetaCyc:MON-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:0006425; P:glutaminyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR DisProt; DP02496; -.
DR Gene3D; 1.10.10.410; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 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_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF02637; GatB_Yqey; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR SUPFAM; SSF89095; SSF89095; 1.
DR TIGRFAMs; TIGR00440; glnS; 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
