ID A0A0G1MPC4_9BACT Unreviewed; 215 AA.
AC A0A0G1MPC4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Aspartate-tRNA ligase {ECO:0000313|EMBL:KKT73879.1};
DE Flags: Fragment;
GN ORFNames=UW70_C0074G0001 {ECO:0000313|EMBL:KKT73879.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWA2_44_7.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619057 {ECO:0000313|EMBL:KKT73879.1, ECO:0000313|Proteomes:UP000034415};
RN [1] {ECO:0000313|EMBL:KKT73879.1, ECO:0000313|Proteomes:UP000034415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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:KKT73879.1}.
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DR EMBL; LCJI01000074; KKT73879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1MPC4; -.
DR STRING; 1619057.UW70_C0074G0001; -.
DR PATRIC; fig|1619057.3.peg.1177; -.
DR Proteomes; UP000034415; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
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 PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55261; GAD domain-like; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKT73879.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 49..185
FT /note="Aminoacyl-tRNA synthetase class II (D/K/N)"
FT /evidence="ECO:0000259|Pfam:PF00152"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKT73879.1"
SQ SEQUENCE 215 AA; 24279 MW; 70AA725DCDE14969 CRC64;
ADEQDAFKKE TKIADGDLVF FTADQFNVAC TSLGQVRIAC ADEFKLRDPN VFAFLWVIDF
PMFEWSKEDN CLTAAHHPFC SIKIEDIPLL EKTPLKARAK AYDFVLNGVE VGGGSIRIHK
PEVQAKIFDI LSITKEDAHH RFGHMLEAFT YGAPPHGGIA WGLDRLIMIF CNEPNIREVI
VFPKDNRAHD LMLDAPSELP EKQVAEMHIK TIKKA
//
