ID A0A0G1C5H7_9BACT Unreviewed; 480 AA.
AC A0A0G1C5H7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Asparagine-tRNA ligase {ECO:0000313|EMBL:KKS80659.1};
GN ORFNames=UV54_C0001G0009 {ECO:0000313|EMBL:KKS80659.1};
OS Candidatus Beckwithbacteria bacterium GW2011_GWA2_43_10.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1618369 {ECO:0000313|EMBL:KKS80659.1, ECO:0000313|Proteomes:UP000034213};
RN [1] {ECO:0000313|EMBL:KKS80659.1, ECO:0000313|Proteomes:UP000034213}
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 -!- 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:KKS80659.1}.
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DR EMBL; LCEW01000001; KKS80659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1C5H7; -.
DR STRING; 1618369.UV54_C0001G0009; -.
DR Proteomes; UP000034213; Unassembled WGS sequence.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02142; MGS; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR PROSITE; PS51855; MGS; 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, ECO:0000313|EMBL:KKS80659.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 355..480
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 480 AA; 55038 MW; 445EB47CF88B4006 CRC64;
MKKLSFNDHF ANLTKINASL NSGAREHYKN CGLTYVDVPE IVGITGACEN VDTLFKVGNR
LDIPLFFTQT GQLSLEQALQ SFGGVFTVIH SGRDEELEDE RHLRQFRLTE EEFDCTLAGM
TRKNYDEEKM FMALLNHIQT TVQGMIREVL KDNSKILKTA YHRDVTKLEQ AAKINFLKIN
YEDVVKVLNK NDFNQLKFGD DLKAEHEQMV VKLLNKKGSE LPVFIMRYPK EIKFFNMKVS
TQDPRVVLSA DLIFPYSGEG TGSAVREHDF NKLNQRLLTS TMYKLHLQRG GTYADFSWYL
KIIKSKKTNP HAGYGIGNER VIQYIFGEED IRNVSLFSLL NKQSQDWHLK RYGQAALFSA
DKKQLLLTIG KLTDKKKLLP YIAKLNKNFT LYATQKTHEF LKVKGVKTAR VYKISEIGQK
PNINDLLKRR VFDVVINIPR GKTDALTDGK LIRRATAEAG VSLITDMNMA KMVIENLCRR
//
