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Database: UniProt
Entry: A0A3P8RAA3_ASTCA
LinkDB: A0A3P8RAA3_ASTCA
Original site: A0A3P8RAA3_ASTCA 
ID   A0A3P8RAA3_ASTCA        Unreviewed;       192 AA.
AC   A0A3P8RAA3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03149};
DE            Short=Glu-AdT subunit C {ECO:0000256|HAMAP-Rule:MF_03149};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_03149};
GN   Name=GATC {ECO:0000256|HAMAP-Rule:MF_03149};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000038920.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000038920.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000038920.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03149};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_03149}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03149}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_03149}.
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DR   AlphaFoldDB; A0A3P8RAA3; -.
DR   STRING; 8154.ENSACLP00000038920; -.
DR   Ensembl; ENSACLT00000039844.1; ENSACLP00000038920.1; ENSACLG00000026251.1.
DR   GeneTree; ENSGT00390000018351; -.
DR   OMA; HINTENV; -.
DR   OrthoDB; 3084936at2759; -.
DR   Proteomes; UP000265100; Chromosome 12.
DR   Bgee; ENSACLG00000026251; Expressed in liver and 8 other cell types or tissues.
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   HAMAP; MF_00122; GatC; 1.
DR   InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   InterPro; IPR003837; GatC.
DR   NCBIfam; TIGR00135; gatC; 1.
DR   PANTHER; PTHR15004:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR15004; UNCHARACTERIZED; 1.
DR   Pfam; PF02686; GatC; 1.
DR   SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03149}.
SQ   SEQUENCE   192 AA;  21457 MW;  5D43A783D84DA49D CRC64;
     MSVFSLAASR TFRGVSVKIP RMLFSLLPND GYSITILNSK RISWPQSHSA NTTRLLSSEP
     LNQKIPKVAT WEPVPEEQLP PPAHIPADLV DKLERLALVD FRTKQGLACL EKAIRFADQL
     HVVDTTGVEP MDSVLEDRVL YLREDAVMEG DCAEKLLQLS KTTVEEYFVA PPGNIPLPKG
     EERTAMLKNS EF
//
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