ID   GATC_LOALO              Reviewed;         190 AA.
AC   E1FU46;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 51.
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=LOAG_04423;
OS   Loa loa (Eye worm) (Filaria loa).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX   NCBI_TaxID=7209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA   Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA   Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Haas B.,
RA   Henn M.R., Nusbaum C., Birren B.;
RT   "The genome sequence of Loa loa.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC       Rule:MF_03149}.
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DR   EMBL; JH712067; EFO24057.1; -; Genomic_DNA.
DR   RefSeq; XP_003140008.1; XM_003139960.1.
DR   AlphaFoldDB; E1FU46; -.
DR   STRING; 7209.EFO24057.1; -.
DR   EnsemblMetazoa; EFO24057.1; EFO24057.1; LOAG_04423.
DR   GeneID; 9941831; -.
DR   KEGG; loa:LOAG_04423; -.
DR   WBParaSite; EN70_4582; EN70_4582; EN70_4582.
DR   CTD; 9941831; -.
DR   eggNOG; KOG4247; Eukaryota.
DR   HOGENOM; CLU_1429500_0_0_1; -.
DR   InParanoid; E1FU46; -.
DR   OMA; HINTENV; -.
DR   OrthoDB; 1496962at2759; -.
DR   Proteomes; UP000095285; 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   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   3: Inferred from homology;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..96
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03149"
FT   CHAIN           97..190
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT                   mitochondrial"
FT                   /id="PRO_0000413316"
FT   REGION          28..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   190 AA;  21494 MW;  013ACEC0071C4B86 CRC64;
     MISFQIILQQ RLRSLRFGKR CKSKRTLKSN STAVGSSDED DEIYVPKKPI PSPIDQSKVE
     EPPVFTKALI THLERLSLVR FSDEQAVLNL KQAVRFANQL KLIDTTGIKP LETLLEDIPC
     PLREDVPGDP MTKAEVLMNA TKVVEDYFVT PPGNIPLEES DKLDLMKIED DAQKEMSKKT
     LLKDSVKKTE