ID A0A257TRG0_9BACT Unreviewed; 191 AA.
AC A0A257TRG0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000313|EMBL:OYV88024.1};
DE Flags: Fragment;
GN ORFNames=B7Z63_01540 {ECO:0000313|EMBL:OYV88024.1};
OS Ignavibacteriae bacterium 37-53-5.
OC Bacteria; Ignavibacteriota.
OX NCBI_TaxID=1970532 {ECO:0000313|EMBL:OYV88024.1, ECO:0000313|Proteomes:UP000225652};
RN [1] {ECO:0000313|EMBL:OYV88024.1, ECO:0000313|Proteomes:UP000225652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37-53-5 {ECO:0000313|EMBL:OYV88024.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYV88024.1}.
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DR EMBL; NCBO01000071; OYV88024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257TRG0; -.
DR Proteomes; UP000225652; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transferase {ECO:0000313|EMBL:OYV88024.1}.
FT DOMAIN 28..112
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 130..191
FT /note="Aminoacyl-tRNA synthetase class II (D/K/N)"
FT /evidence="ECO:0000259|Pfam:PF00152"
FT NON_TER 191
FT /evidence="ECO:0000313|EMBL:OYV88024.1"
SQ SEQUENCE 191 AA; 21885 MW; EC9C49169AB4D130 CRC64;
MSETVSLRGK KRTHTCGELR ANNINDVVTL NGWVDGRRDL GGVIFIDLRD RYGKTQVVFA
PQHNESVYQT AKQLRSEDVL AVVGKVERRP EGTRNKSLPT GEIEVLGDDL VILSEAETPP
FPIEDVIDTS EELRLKYRFL DLRLHQMQSN LAVRHRMAQT VRRYMDSLNF LEIETPFLMR
STPEGARDYL V
//
