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Database: UniProt
Entry: A0A0F0CRN8_9BACT
LinkDB: A0A0F0CRN8_9BACT
Original site: A0A0F0CRN8_9BACT 
ID   A0A0F0CRN8_9BACT        Unreviewed;       250 AA.
AC   A0A0F0CRN8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN   ORFNames=OMAG_000177 {ECO:0000313|EMBL:KJJ85993.1};
OS   Candidatus Omnitrophus magneticus.
OC   Bacteria; Candidatus Omnitrophota; Omnitrophus.
OX   NCBI_TaxID=1609969 {ECO:0000313|EMBL:KJJ85993.1, ECO:0000313|Proteomes:UP000033428};
RN   [1] {ECO:0000313|EMBL:KJJ85993.1, ECO:0000313|Proteomes:UP000033428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKK-01 {ECO:0000313|EMBL:KJJ85993.1};
RA   Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT   "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT   conserved set of magnetosome genes.";
RL   Submitted (FEB-2015) 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:KJJ85993.1}.
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DR   EMBL; JYNY01000032; KJJ85993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0CRN8; -.
DR   PATRIC; fig|1609969.3.peg.213; -.
DR   Proteomes; UP000033428; Unassembled WGS sequence.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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   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|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033428}.
FT   DOMAIN          38..249
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
SQ   SEQUENCE   250 AA;  29121 MW;  34D63A64E8202CEF CRC64;
     MANYVLFEKN MDTIKPVENF ITEIIDSGLK ENKYGGRVHT RFPPEPNGYL HIGHAKSICL
     NFGLAEQYKG LCNRRFDDTN PEKEEVEYVN SIMEDVKWLG FTWDDRLYYA SDYFEEIYGH
     ALTLIKKGKA YVCELSVDEI REYRGTLTSP GKDSPYRNRS IEENLKLFFA MRSGEFAEGA
     KVLRAKINMA SPNIVMRDPV LYRIKKVAHH RVKDKWCIYP TYDFTHCISD SIEGITHSIC
     TLEFEINREL
//
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