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   11-NOV-2015, entry version 30.
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};
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-
CC       tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03149}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC       {ECO:0000255|HAMAP-Rule:MF_03149}.
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase
CC       (AdT) complex, composed of A, B and C subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_03149}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03149}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC       Rule:MF_03149}.
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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   InParanoid; B3RYZ0; -.
DR   KO; K02435; -.
DR   OrthoDB; EOG7HTHJN; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
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. {ECO:0000255|HAMAP-
FT                                Rule:MF_03149}.
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
//