GATC_BOVIN
ID GATC_BOVIN Reviewed; 136 AA.
AC Q2KIF1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Name=GATC {ECO:0000255|HAMAP-Rule:MF_03149};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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 (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 -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC Rule:MF_03149}.
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DR EMBL; BC112661; AAI12662.1; -; mRNA.
DR RefSeq; NP_001040027.1; NM_001046562.1.
DR AlphaFoldDB; Q2KIF1; -.
DR SMR; Q2KIF1; -.
DR STRING; 9913.ENSBTAP00000016996; -.
DR PaxDb; Q2KIF1; -.
DR PRIDE; Q2KIF1; -.
DR Ensembl; ENSBTAT00000016996; ENSBTAP00000016996; ENSBTAG00000012791.
DR GeneID; 615845; -.
DR KEGG; bta:615845; -.
DR CTD; 283459; -.
DR VEuPathDB; HostDB:ENSBTAG00000012791; -.
DR eggNOG; KOG4247; Eukaryota.
DR GeneTree; ENSGT00390000018351; -.
DR HOGENOM; CLU_105899_0_2_1; -.
DR InParanoid; Q2KIF1; -.
DR OMA; HINTDHV; -.
DR OrthoDB; 1496962at2759; -.
DR TreeFam; TF106133; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000012791; Expressed in triceps brachii and 105 other tissues.
DR ExpressionAtlas; Q2KIF1; baseline and differential.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
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; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03149"
FT CHAIN 28..136
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT mitochondrial"
FT /id="PRO_0000290034"
SQ SEQUENCE 136 AA; 15176 MW; 2192FCA4974D3DA9 CRC64;
MWARAVHLGL RAAARGRRGF TSKADPQGSG RVTGELIQHL ERLSLVDFGS QEAVARLEKA
IAFADRLRAV NTDGVEPMES VLEDRCLYLR SDNVVEGSCA EELLQNSHRV VEEYFVAPPG
NISWSKLDEK QPFSHR