ID A0A0G0VUU2_9BACT Unreviewed; 418 AA.
AC A0A0G0VUU2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Aspartyl-tRNA synthetase {ECO:0000313|EMBL:KKS04600.1};
DE Flags: Fragment;
GN ORFNames=UU56_C0004G0001 {ECO:0000313|EMBL:KKS04600.1};
OS Candidatus Curtissbacteria bacterium GW2011_GWA2_41_24.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1618411 {ECO:0000313|EMBL:KKS04600.1, ECO:0000313|Proteomes:UP000034493};
RN [1] {ECO:0000313|EMBL:KKS04600.1, ECO:0000313|Proteomes:UP000034493}
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:KKS04600.1}.
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DR EMBL; LCBC01000004; KKS04600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0VUU2; -.
DR PATRIC; fig|1618411.3.peg.299; -.
DR Proteomes; UP000034493; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 CDD; cd00777; AspRS_core; 1.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR047090; AspRS_core.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:KKS04600.1}; 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}.
FT DOMAIN 99..389
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKS04600.1"
SQ SEQUENCE 418 AA; 48100 MW; 5D3A3C65407CAE8E CRC64;
FYDLRDASGI IQTVTKKRFD VSAEDVVKIE GVVTKRPQKL INPQIATGEI EVKVDSLTII
GKSETLPFPI DDLGLDIEET LRLKYRYLDL RRERLVTNLK LRHQMINFMR QFLTKRGFVE
IETPILTKAT PEGARDFIVP SRLQPGNFYA LPQSPQQYKQ LLMVAGFEKY FQIARCFRDE
DPRTDRSYGE FSQLDLEMSF VNQEDILQLI EELFAEITEK VFKKKVYKFP FPRISHQEAI
AKYQSDKFDL REKKDPNVLA FAFIVNFPLF ERTQNQPISP SHHPFTAPKD EDIPQLFKDP
MKVRSWQHDL VANGLEIGGG SIRITDPNVQ RKIFKILGYR ESEIEEKFGH LLNAFIYGVP
PHGGIALGLE RILMVATGEE NTREVTAFPM SSSGQTAVMD APSKVDEQTL KELKLKKL
//
