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   25-MAY-2022, entry version 49.
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}.
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DR   EMBL; DS985246; EDV24110.1; -; Genomic_DNA.
DR   RefSeq; XP_002113636.1; XM_002113600.1.
DR   AlphaFoldDB; B3RYZ0; -.
DR   SMR; B3RYZ0; -.
DR   STRING; 10228.TriadP57266; -.
DR   EnsemblMetazoa; TriadT57266; TriadP57266; TriadG57266.
DR   GeneID; 6754849; -.
DR   KEGG; tad:TRIADDRAFT_57266; -.
DR   CTD; 6754849; -.
DR   HOGENOM; CLU_1752071_0_0_1; -.
DR   InParanoid; B3RYZ0; -.
DR   OrthoDB; 1496962at2759; -.
DR   PhylomeDB; B3RYZ0; -.
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; IBA:GO_Central.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
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