ID   GATC_SALSA              Reviewed;         194 AA.
AC   B5DFW7; B9ENL8;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, 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   Name=gatc;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=White muscle;
RX   PubMed=19878547; DOI=10.1186/1471-2164-10-502;
RA   Andreassen R., Lunner S., Hoyheim B.;
RT   "Characterization of full-length sequenced cDNA inserts (FLIcs) from
RT   Atlantic salmon (Salmo salar).";
RL   BMC Genomics 10:502-502(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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 (qrsl1), B (gatb) and C (gatc) subunits.
CC       {ECO:0000255|HAMAP-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; BT043526; ACH70641.1; -; mRNA.
DR   EMBL; BT057243; ACM09115.1; -; mRNA.
DR   RefSeq; NP_001133076.1; NM_001139604.1.
DR   AlphaFoldDB; B5DFW7; -.
DR   STRING; 8030.ENSSSAP00000104379; -.
DR   GeneID; 100194518; -.
DR   KEGG; sasa:100194518; -.
DR   CTD; 283459; -.
DR   OMA; HINTENV; -.
DR   OrthoDB; 1496962at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa24.
DR   Bgee; ENSSSAG00000075942; Expressed in zone of skin and 16 other 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; 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.
DR   TIGRFAMs; TIGR00135; gatC; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..194
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT                   mitochondrial"
FT                   /id="PRO_0000413292"
FT   CONFLICT        83
FT                   /note="P -> L (in Ref. 2; ACM09115)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22004 MW;  3A2979F02FC83D9E CRC64;
     MYVVVNYTRR LQTLAFNLGS SCYHQGVTGA SITSQDRKSK QNFSCCRWTH LITLVHQYST
     RISNSKVPRV ATWEPVLENQ LPPPCQIPVD LVDKLERLAL VDFRNQEGLA CLEKAIRFAD
     QLHVVDTDGV DPMDSVLEER ALYLREDAVA EGDCAEELLQ LSKNTVEEYF VAPPGNIPLP
     KREERAAMLK HSEF