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Database: UniProt
Entry: A0A1G6VWA3_PEPNI
LinkDB: A0A1G6VWA3_PEPNI
Original site: A0A1G6VWA3_PEPNI 
ID   A0A1G6VWA3_PEPNI        Unreviewed;       555 AA.
AC   A0A1G6VWA3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN   ORFNames=SAMN04489866_104140 {ECO:0000313|EMBL:SDD57096.1};
OS   Peptococcus niger.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Peptococcus.
OX   NCBI_TaxID=2741 {ECO:0000313|EMBL:SDD57096.1, ECO:0000313|Proteomes:UP000198995};
RN   [1] {ECO:0000313|EMBL:SDD57096.1, ECO:0000313|Proteomes:UP000198995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20475 {ECO:0000313|EMBL:SDD57096.1,
RC   ECO:0000313|Proteomes:UP000198995};
RA   de Groot N.N.;
RL   Submitted (OCT-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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363037}.
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DR   EMBL; FNAF01000004; SDD57096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6VWA3; -.
DR   STRING; 2741.SAMN04489866_104140; -.
DR   OrthoDB; 9801560at2; -.
DR   Proteomes; UP000198995; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198995}.
FT   DOMAIN          26..339
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          342..443
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          460..532
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
SQ   SEQUENCE   555 AA;  63974 MW;  5B2E3C13937351E4 CRC64;
     MEDHTIQKNF IEQIIDADLQ AGMTAIATRF PPEPNGYLHI GHAKSIFLNF GLAKTYDGTC
     FLRFDDTNPI KEEDEFVESI MQDVHWLGGE WDGDVRFASD YFEAFYEMAE CLIEKGLAYV
     DDQSAEAIRE TRGTLTEPGT DSPYRNRSVA ENMDLFRRMR QGEFADGEKV LRAKIDMASP
     NMNMRDPVIY RILHASHHRT GDKWCIYPMY DYAHPLEDAI EGITHSICTL EFQDHRPLYN
     WFIEQLAEDE HLKSRPQQIE FARLEIENTM TSKRRLKALV DAGLVDGWDD PRLPTVSGLR
     RRGYTPAALK EFCQRIGVAK TNSVVEQNYL TFCLREDLNR VAPRAMAVLN PLKLTLTNYP
     EDQIEWVQGV VNPNDETMGT YEMPFGKHLY IEQEDFREEA NRKYHRLKPG AEVRLMYGYI
     IKCEDFIKDP ETGEILEVLC TYDPMTKSGM PDADRKVKGT LHWVEATHAV DATVHVLDDL
     MDEDKPQDAD ILERFNQHSL EVLKGCKVEP RLAKAQVGQA YQFMRKGYYC ADSRYHTAEA
     PVFNLTVGLR DKFKG
//
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