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Database: UniProt
Entry: A0A2D6LPA2_9ARCH
LinkDB: A0A2D6LPA2_9ARCH
Original site: A0A2D6LPA2_9ARCH 
ID   A0A2D6LPA2_9ARCH        Unreviewed;       549 AA.
AC   A0A2D6LPA2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030865};
DE            EC=6.1.1.17 {ECO:0000256|ARBA:ARBA00012835};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN   ORFNames=CL944_00840 {ECO:0000313|EMBL:MAG18002.1};
OS   Candidatus Diapherotrites archaeon.
OC   Archaea; Candidatus Diapherotrites.
OX   NCBI_TaxID=2026736 {ECO:0000313|EMBL:MAG18002.1, ECO:0000313|Proteomes:UP000226712};
RN   [1] {ECO:0000313|Proteomes:UP000226712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) 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:MAG18002.1}.
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DR   EMBL; NZBD01000004; MAG18002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D6LPA2; -.
DR   Proteomes; UP000226712; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.240.100; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00463; gltX_arch; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 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}.
FT   DOMAIN          94..401
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
SQ   SEQUENCE   549 AA;  63511 MW;  71FA29989C24FBDF CRC64;
     MSIKEDAYRY AVKNAFEHAG KSEIGPLIGK LKALHKDTPV PELMPVAIEV VKKVNGMTSK
     EIEEAFNGFQ EGYELKPKPE REGLPELDWA DKEKVITRYA PNPNGPFHLG NARAAYLSYA
     YAEKYGGKFI LRFEDTDPKI KKPIDNPEKV FREDLTWLGI KIGKVFFASD RMETYYSYMR
     KLLEQGNAYV CKCESESWRE LIKQKKACEH REQPSEVQLK EFEKMVSNEL KEGQAVLRIK
     TDLEHKDTSV RDWWLARIVD NPDNPRIKGT YHVWPSYMFQ SGIDDHEMGI TFILRGQEHS
     QNQTKQEFLY NYLKWDYPNA VHFGRLKIGE MVLSTSKIKE GIENEEYTDW DDIRLGTIKA
     LRRRGFKPEA LHKIIIDSGL TTSDANISME KMGAYNKELI QEEAERTTYI IDPIKLEVHL
     PEAIDAEKEG EKFSLEQGIQ EFMISESAIK KIKDSVFRLR NIGNVKVENK EGLLLNGQFV
     GKETTGKQVV QWLRETMDLE LLLPNGQKEV GAIEKKNLKK GQYLYLEKKG YCIIDSIDEG
     RPKAWFCHE
//
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