CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020697
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial 
Protein Synonyms/Alias
 Glu-AdT subunit A; Glutaminyl-tRNA synthase-like protein 1 
Gene Name
 Qrsl1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
57KQAEESEKRYKQGQSacetylation[1, 2]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
 Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity). 
Sequence Annotation
 ACT_SITE 76 76 Charge relay system (By similarity).
 ACT_SITE 168 168 Charge relay system (By similarity).
 ACT_SITE 192 192 Acyl-ester intermediate (By similarity).  
Keyword
 ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 525 AA 
Protein Sequence
MLGRTLREVS AALKQGQVTP TELCKNCLSL IKKTKYLNAY ITVSEEVALK QAEESEKRYK 60
QGQSLGDLDG IPVAVKDNFS TTGIETTCAS NMLKGYVPPY NATVVQKLLD QGALLMGKTN 120
LDEFAMGSGS TDGVFGPVRN PWTYSKQYRE RSRQDAGDDS HWLITGGSSG GSAAAVAAFT 180
CFAALGSDTG GSTRNPAAHC GIVGFKPSYG LVSRHGLIPL VNSMDVPGIL TRCVDDTAIV 240
LGTLAGHDPK DSTTVRNPAQ PASVPGGMDV SRLCIGIPKE YLVPELSSEV RSLWSQAADL 300
FESEGAKVIE VSLPHTCYSI VCYHVLCTSE VASNMARFDG LQYGHRSGVD VSTEAMYAAT 360
RQEGFNDVVR GRILSGNFFL LKENYENYFV KAQKVRRLIV KDFVDVFESG VDVLLTPTTL 420
TEAVPYLEFI KEDNRTRSAQ DDIFTQAVNM AGLPAVSVPV ALSNQGLPIG LQLIGRAFCD 480
QQLLTVAKWF EKQVQFPVIQ LQGLMDDGSL VLENGKLTSA SLTQR 525 
Gene Ontology
 GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:HAMAP.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
 GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:HAMAP.
 GO:0032543; P:mitochondrial translation; IEA:HAMAP. 
Interpro
 IPR000120; Amidase.
 IPR023631; Amidase_dom.
 IPR004412; GatA. 
Pfam
 PF01425; Amidase 
SMART
  
PROSITE
 PS00571; AMIDASES 
PRINTS