ID   GATF_YARLI              Reviewed;         176 AA.
AC   Q6CDJ8;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03151};
DE            Short=Glu-AdT subunit F {ECO:0000255|HAMAP-Rule:MF_03151};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03151};
GN   Name=GTF1 {ECO:0000255|HAMAP-Rule:MF_03151};
GN   OrderedLocusNames=YALI0B23386g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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). Required for
CC       proper protein synthesis within the mitochondrion. {ECO:0000255|HAMAP-
CC       Rule:MF_03151}.
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_03151};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatFAB amidotransferase (AdT)
CC       complex, composed of A, B and F subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_03151}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03151}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03151}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03151}.
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_03151}.
CC   -!- SIMILARITY: Belongs to the GatF family. {ECO:0000255|HAMAP-
CC       Rule:MF_03151}.
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DR   EMBL; CR382128; CAG83517.1; -; Genomic_DNA.
DR   RefSeq; XP_501264.1; XM_501264.1.
DR   AlphaFoldDB; Q6CDJ8; -.
DR   STRING; 4952.CAG83517; -.
DR   EnsemblFungi; CAG83517; CAG83517; YALI0_B23386g.
DR   GeneID; 2906853; -.
DR   KEGG; yli:YALI0B23386g; -.
DR   VEuPathDB; FungiDB:YALI0_B23386g; -.
DR   HOGENOM; CLU_1526368_0_0_1; -.
DR   InParanoid; Q6CDJ8; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005743; C:mitochondrial inner membrane; 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   HAMAP; MF_03151; GatF; 1.
DR   InterPro; IPR027499; GatF.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..176
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT                   mitochondrial"
FT                   /id="PRO_0000413408"
SQ   SEQUENCE   176 AA;  19683 MW;  8F12D9C224E2AE8F CRC64;
     MLRIARVSHN AVKMASSRGI HFSSDGFIKM KDQKHILKVM NSPENQWSTD ELLSHSDHSS
     DEITSETLQK VSKKLAPIFK SAALPMPDSD ETMFSLIKTL RTQVNLVSHI HDIDVSGVAP
     LTCLTPIKDF TYEQLTAEDS GEPGPEVLWD ALSCAEKKDG RFFVVSRDIK QEEPTQ