GATC2_CULQU
ID GATC2_CULQU Reviewed; 166 AA.
AC B0W041;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C-2, mitochondrial;
DE Short=Glu-AdT subunit C-2 {ECO:0000255|HAMAP-Rule:MF_03149};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03149};
GN ORFNames=CPIJ000405;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) 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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS231816; EDS37613.1; -; Genomic_DNA.
DR RefSeq; XP_001842075.1; XM_001842023.1.
DR AlphaFoldDB; B0W041; -.
DR SMR; B0W041; -.
DR STRING; 7176.CPIJ000405-PA; -.
DR KEGG; cqu:CpipJ_CPIJ000405; -.
DR VEuPathDB; VectorBase:CPIJ000405; -.
DR VEuPathDB; VectorBase:CQUJHB009367; -.
DR eggNOG; KOG4247; Eukaryota.
DR HOGENOM; CLU_105899_0_1_1; -.
DR InParanoid; B0W041; -.
DR OrthoDB; 1496962at2759; -.
DR PhylomeDB; B0W041; -.
DR Proteomes; UP000002320; Partially assembled 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..166
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C-2,
FT mitochondrial"
FT /id="PRO_0000413298"
SQ SEQUENCE 166 AA; 19037 MW; 02A61D20441DA5D8 CRC64;
MIQSCRKLFR SDRCPNLHRK KPAYLEAGQR GFPEKSTRQK INYHELKHLS KVPQRPHKPT
IDGQSTPTRI PVDAQTVRLS LVDLDSAEAH RTLEDAIEFA SQILSVDTDG VEPLYTVLER
DRLTLREDRV SDGNIQQDVL RNARVTEEEY FVAPPGNIPL EQEPKK
