ID GATC_TRIAD Reviewed; 149 AA. AC B3RYZ0; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial; DE Short=Glu-AdT subunit C; DE EC=6.3.5.-; DE Flags: Precursor; GN ORFNames=TRIADDRAFT_57266; OS Trichoplax adhaerens (Trichoplax reptans). OC Eukaryota; Metazoa; Placozoa; Trichoplax. OX NCBI_TaxID=10228; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Grell-BS-1999; RX PubMed=18719581; DOI=10.1038/nature07191; RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U., RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L., RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J., RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., RA Dellaporta S.L., Rokhsar D.S.; RT "The Trichoplax genome and the nature of placozoans."; RL Nature 454:955-960(2008). CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) CC through the transamidation of misacylated Glu-tRNA(Gln) in the CC mitochondria. The reaction takes place in the presence of CC glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) CC (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase CC (AdT) complex, composed of A, B and C subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the GatC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS985246; EDV24110.1; -; Genomic_DNA. DR RefSeq; XP_002113636.1; XM_002113600.1. DR EnsemblMetazoa; TriadT57266; TriadP57266; TriadG57266. DR GeneID; 6754849; -. DR KEGG; tad:TRIADDRAFT_57266; -. DR eggNOG; NOG251156; -. DR KO; K02435; -. DR OrthoDB; EOG7HTHJN; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR HAMAP; MF_00122; GatC; 1. DR InterPro; IPR003837; Asp/Glu-ADT_csu. DR Pfam; PF02686; Glu-tRNAGln; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Mitochondrion; KW Nucleotide-binding; Protein biosynthesis; Reference proteome; KW Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 149 Glutamyl-tRNA(Gln) amidotransferase FT subunit C, mitochondrial. FT /FTId=PRO_0000413325. SQ SEQUENCE 149 AA; 17121 MW; 11561FA7D0CE2B2E CRC64; MAVKPSANLG KAFQLPHPFN SCVYIQIPPQ PTWSINEYWE RNPNKQYLDE SDTTYLEELT LTPIEKHQAL EKLNTIISAA DRLQEVDTKN VDPMYTCVDE REMYMNSGQD GETVNKEEIL GNAHKIFQDY FTAPTSEKMR SSSDLNAKE //