GATC_CAEEL
ID GATC_CAEEL Reviewed; 175 AA.
AC Q9BI40;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 ORFNames=Y66D12A.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- 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; AL161712; CAC35907.1; -; Genomic_DNA.
DR RefSeq; NP_499495.1; NM_067094.3.
DR AlphaFoldDB; Q9BI40; -.
DR STRING; 6239.Y66D12A.7; -.
DR EPD; Q9BI40; -.
DR PaxDb; Q9BI40; -.
DR PeptideAtlas; Q9BI40; -.
DR EnsemblMetazoa; Y66D12A.7.1; Y66D12A.7.1; WBGene00013433.
DR GeneID; 176590; -.
DR KEGG; cel:CELE_Y66D12A.7; -.
DR UCSC; Y66D12A.7; c. elegans.
DR CTD; 176590; -.
DR WormBase; Y66D12A.7; CE26457; WBGene00013433; -.
DR eggNOG; KOG4247; Eukaryota.
DR GeneTree; ENSGT00390000018351; -.
DR HOGENOM; CLU_105899_0_0_1; -.
DR InParanoid; Q9BI40; -.
DR OMA; HINTENV; -.
DR OrthoDB; 1496962at2759; -.
DR PhylomeDB; Q9BI40; -.
DR PRO; PR:Q9BI40; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013433; Expressed in germ line (C elegans) and 4 other tissues.
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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..175
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT mitochondrial"
FT /id="PRO_0000413314"
SQ SEQUENCE 175 AA; 20272 MW; 3A5854FBEA548EE2 CRC64;
MNLIFTRIIR RFGEGKRKTP FPGDPILVPD EPYDSKIQES QLSPMPQIDA KLINHLERLS
LVRFDSEQAV ANLRSSIRVA KRLELVDVEG VEPMHTVWED QECPTFEDVE EDPLPIEEVF
RNASLRFDDF FVTPPGNLPL ESKERFDLNV INEWDTIGKP VAPEVKLTRM TERKK