ID A0A139STK3_9BACT Unreviewed; 630 AA.
AC A0A139STK3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN ORFNames=AXK12_01100 {ECO:0000313|EMBL:KXU37790.1};
OS Cephaloticoccus capnophilus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Cephaloticoccus.
OX NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU37790.1, ECO:0000313|Proteomes:UP000071392};
RN [1] {ECO:0000313|EMBL:KXU37790.1, ECO:0000313|Proteomes:UP000071392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV41 {ECO:0000313|EMBL:KXU37790.1,
RC ECO:0000313|Proteomes:UP000071392};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {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:KXU37790.1}.
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DR EMBL; LSZP01000004; KXU37790.1; -; Genomic_DNA.
DR RefSeq; WP_068710817.1; NZ_LSZP01000004.1.
DR AlphaFoldDB; A0A139STK3; -.
DR STRING; 1548208.AXK12_01100; -.
DR OrthoDB; 9801560at2; -.
DR Proteomes; UP000071392; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000071392}.
FT DOMAIN 59..403
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 410..509
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 528..601
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 136..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 70447 MW; 87FFE5BA7960B21A CRC64;
MITPTDTGLE SDSSAATPAP AAAATSASAL AADAALRTSP TDFIRDIVAA HVAENRYPQI
VTRFPPEPNG YLHLGHARAI CLNFGIAREN AGRCHLRFDD TNPAKEDAHY VAAITRDIRW
LIHDWADAQL TFKPRGAGPA AHRSADGHPD HLVPHAPADA PDTEPYAASD YFDALYDYAL
ELIRRGKAYV CDLSPEDTER YRGTPTTPGQ NSPYRDRSVE ENLDLFARMR AGEFPDGART
LRAKIDMASP NLWLRDPLLY RIRHITHHNT ADRWCIYPLY DYAHCLSDYL EGVTHSCCSL
EFVAHRPLYD WVLDSLDLPR PRPYQYEFAK LIPSYTLMSK RNLLRLVKER AVNGWDDPRM
PTLAGLRRRG IPAAALRRFV IETGITTHDG GLTDIALFEH TLRDELNKTA PRRLAVLHPL
KLILTNLPEG EVIPCQATND PQNDAPSTRT VSLTREVFIE RDDFAEVPPP KFHRLKPGGE
VRLKYACIIT LDEIVKDPAT GAVTELRATA QLDTRAGQPN SNKKVKGTIH WVSAPESIEA
EVRLYERLFT VPEPAAEDDF LKVLNPHSLE TVYGARLEPA LASAQPNEPV QFERLGYFTL
DVAENEDAAA DGDARLIFNR TITLRDTWAK
//
