CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017213
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CCA tRNA nucleotidyltransferase 1, mitochondrial 
Protein Synonyms/Alias
 mitochondrial tRNA nucleotidyl transferase, CCA-adding; mt CCA-adding enzyme; mt tRNA CCA-diphosphorylase; mt tRNA CCA-pyrophosphorylase; mt tRNA adenylyltransferase 
Gene Name
 Trnt1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
283EEFNKVSKNVEGFSPacetylation[1]
367ARVCELLKYQGEHGLacetylation[2]
395VSGHDIRKVGISSGKacetylation[1]
402KVGISSGKEIGALLQacetylation[1, 2, 3, 4, 5]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates (By similarity). 
Sequence Annotation
 ACT_SITE 77 77 By similarity.
 ACT_SITE 79 79 By similarity.
 ACT_SITE 121 121 By similarity.
 MOD_RES 400 400 Phosphoserine (By similarity).
 MOD_RES 402 402 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Magnesium; Mitochondrion; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Reference proteome; RNA-binding; Transferase; Transit peptide; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 434 AA 
Protein Sequence
MQSVLYPWHR QVLRCSWSRL CLLKRYLFTM KLQSPEFQSL FTEGLKSLTE LFAKENHELR 60
IAGGAVRDLL NGVKPQDVDF ATTATPTQMK EMFQSAGIRM INNKGEKHGT ITARLHEENF 120
EVTTLRIDVT TDGRHAEVEF TTDWQKDAER RDLTINSMFL GFDGTLFDYF NGYADLKNKK 180
VRFVGHAKQR IQEDYLRILR YFRFYGRIVD RPGDHDHETL EAIAENAKGL AGISGERIWV 240
ELKKILTGDH VNHLIHLIYD LGVAPHIGLP ANANLEEFNK VSKNVEGFSP KPMTLLASLF 300
KVQDDVTKLD LRLKISKEEK NLGLFIVKNR KDLIKATDSS EPLKPYQDFV IDSREPDATA 360
RVCELLKYQG EHGLLKEMQQ WSVPPFPVSG HDIRKVGISS GKEIGALLQQ LREQWKKSGY 420
RMEKDELLSY IKKT 434 
Gene Ontology
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:EC.
 GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:EC.
 GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:EC.
 GO:0004810; F:tRNA adenylyltransferase activity; ISS:UniProtKB.
 GO:0000049; F:tRNA binding; ISS:UniProtKB.
 GO:0009022; F:tRNA nucleotidyltransferase activity; ISO:MGI.
 GO:0042780; P:tRNA 3'-end processing; ISS:UniProtKB.
 GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:EC. 
Interpro
 IPR002646; PolA_pol_head_dom.
 IPR026973; Trnt1. 
Pfam
 PF01743; PolyA_pol 
SMART
  
PROSITE
  
PRINTS