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 26-FEB-2020, entry version 43. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03149}; DE Short=Glu-AdT subunit C {ECO:0000255|HAMAP-Rule:MF_03149}; DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03149}; GN ORFNames=TRIADDRAFT_57266; OS Trichoplax adhaerens (Trichoplax reptans). OC Eukaryota; Metazoa; Placozoa; Trichoplacidae; 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., Dellaporta S.L., RA 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 glutamine and CC ATP through an activated gamma-phospho-Glu-tRNA(Gln). CC {ECO:0000255|HAMAP-Rule:MF_03149}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate; CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03149}; CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT) CC complex, composed of A, B and C subunits. {ECO:0000255|HAMAP- CC Rule:MF_03149}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149}. CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal CC transit peptide but none has been predicted. {ECO:0000255|HAMAP- CC Rule:MF_03149}. CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP- CC Rule:MF_03149}. 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 STRING; 10228.TriadP57266; -. DR EnsemblMetazoa; TriadT57266; TriadP57266; TriadG57266. DR GeneID; 6754849; -. DR KEGG; tad:TRIADDRAFT_57266; -. DR eggNOG; KOG4247; Eukaryota. DR eggNOG; ENOG4111XXR; LUCA. DR HOGENOM; CLU_1752071_0_0_1; -. DR InParanoid; B3RYZ0; -. DR KO; K02435; -. DR OrthoDB; 1496962at2759; -. DR Proteomes; UP000009022; Unassembled WGS sequence. DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule. DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR Gene3D; 1.10.20.60; -; 1. DR HAMAP; MF_00122; GatC; 1. DR InterPro; IPR003837; Asp/Glu-ADT_csu. DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c. DR PANTHER; PTHR15004; PTHR15004; 1. DR Pfam; PF02686; Glu-tRNAGln; 1. DR SUPFAM; SSF141000; SSF141000; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1..149 FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C, FT mitochondrial" FT /id="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 //