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Database: UniProt
Entry: G3I589_CRIGR
LinkDB: G3I589_CRIGR
Original site: G3I589_CRIGR 
ID   G3I589_CRIGR            Unreviewed;       204 AA.
AC   G3I589;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03149};
DE            Short=Glu-AdT subunit C {ECO:0000256|HAMAP-Rule:MF_03149};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_03149};
GN   Name=GATC {ECO:0000256|HAMAP-Rule:MF_03149};
GN   ORFNames=I79_018633 {ECO:0000313|EMBL:EGW09251.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW09251.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03149}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03149}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_03149}.
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DR   EMBL; JH001287; EGW09251.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3I589; -.
DR   STRING; 10029.G3I589; -.
DR   InParanoid; G3I589; -.
DR   Proteomes; UP000001075; 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; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   InterPro; IPR003837; GatC.
DR   PANTHER; PTHR15004:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR15004; UNCHARACTERIZED; 1.
DR   Pfam; PF02686; GatC; 1.
DR   SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03149};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  22616 MW;  11AEAFC57523FF0B CRC64;
     MVRAFNPRTQ EAEAGGSLRV RGYPGLQNEF QDSQSYTEKP CLKKQNKKEM WARALRVRFP
     VPLDRGRGFA SKAGPQGKVQ EVRQGTHSPR LASQGAGRVP AAKIEHLERL ALVNFGSREA
     VARLEKAIAF ADQLHALDTD GVEPLESLLE DRCVYLRSDN VAEGNCTEEL LRNSHHVVEE
     YFVPLPGNVS LPDMVNKTPS PTAE
//
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