ID A0A0G1KWI5_9BACT Unreviewed; 197 AA.
AC A0A0G1KWI5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000313|EMBL:KKT60657.1};
GN ORFNames=UW55_C0047G0002 {ECO:0000313|EMBL:KKT60657.1};
OS Candidatus Giovannonibacteria bacterium GW2011_GWA2_44_26.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1618648 {ECO:0000313|EMBL:KKT60657.1, ECO:0000313|Proteomes:UP000033945};
RN [1] {ECO:0000313|EMBL:KKT60657.1, ECO:0000313|Proteomes:UP000033945}
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:KKT60657.1}.
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DR EMBL; LCIT01000047; KKT60657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KWI5; -.
DR PATRIC; fig|1618648.3.peg.1125; -.
DR Proteomes; UP000033945; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.410; -; 1.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR018027; Asn/Gln_amidotransferase.
DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 2.
PE 4: Predicted;
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:KKT60657.1}.
FT DOMAIN 69..197
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 197 AA; 22225 MW; 8952C3297594B850 CRC64;
MKESAHDYRY FPDPDLPALI IGEIPEFDEK VLIASLPELP WQKRERYKRD FGLKDGDIEI
YVRQPEWGRL LEEVTEILGN RDLVQLTSNY ITSDLKTLVP ARSLAEVVEM ISAGEISSRG
AKDILKIIQE KGGEPRVIAN DKNLIQESDG EVLKKIAEEV LRENPGAPID FLVGQAMKVT
KGSANPQVLK EIFIKIL
//
