TRNT1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1OU5, 4X4W

Identifiers

Aliases

TRNT1, CCA1, MtCCA, CGI-47, SIFD, tRNA nucleotidyl transferase 1, RPEM

External IDs

MGI: 1917297 HomoloGene: 9333 GeneCards: TRNT1

Gene ontology
Molecular function	• CTP:3'-cytidine-tRNA cytidylyltransferase activity • transferase activity • nucleotide binding • tRNA binding • nucleotidyltransferase activity • tRNA adenylyltransferase activity • ATP binding • CTP:tRNA cytidylyltransferase activity • ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity • RNA binding • 5'-3' RNA polymerase activity
Cellular component	• mitochondrial matrix • intracellular • mitochondrion • nucleoplasm
Biological process	• protein targeting to mitochondrion • RNA processing • tRNA 3'-terminal CCA addition • tRNA 3'-end processing • mitochondrial tRNA 3'-end processing • tRNA processing
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


51095


70047

Ensembl


ENSG00000072756


ENSMUSG00000013736

UniProt


Q96Q11


Q8K1J6

RefSeq (mRNA)


NM_001302946 NM_016000 NM_182916


NM_001242358 NM_001242360 NM_027296

RefSeq (protein)


NP_001289875.1 NP_886552.2


NP_001229287.1 NP_001229289.1 NP_081572.1

Location (UCSC)

Chr 3: 3.13 – 3.15 Mb

Chr 6: 106.77 – 106.78 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

tRNA-nucleotidyltransferase 1, is an enzyme that in humans is encoded by the TRNT1 gene.^[3]^[4]^[5] This enzyme adds the nucleotide sequence CCA to the 3' end of tRNA, using ATP and CTP as substrates. The sequence creates the binding site for an amino acid.^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (Aug 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
↑ Nagaike T, Suzuki T, Tomari Y, Takemoto-Hori C, Negayama F, Watanabe K, Ueda T (Oct 2001). "Identification and characterization of mammalian mitochondrial tRNA nucleotidyltransferases". J Biol Chem. 276 (43): 40041–9. doi:10.1074/jbc.M106202200. PMID 11504732.
↑ "Entrez Gene: TRNT1 tRNA nucleotidyl transferase, CCA-adding, 1".
↑ Lizano E, Scheibe M, Rammelt C, Betat H, Mörl M (May 2008). "A comparative analysis of CCA-adding enzymes from human and E. coli: differences in CCA addition and tRNA 3'-end repair". Biochimie. 90 (5): 762–72. doi:10.1016/j.biochi.2007.12.007. PMID 18226598.

Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
Reichert AS, Thurlow DL, Mörl M (2002). "A eubacterial origin for the human tRNA nucleotidyltransferase?". Biol. Chem. 382 (10): 1431–8. doi:10.1515/BC.2001.176. PMID 11727826.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Augustin MA, Reichert AS, Betat H, et al. (2003). "Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization". J. Mol. Biol. 328 (5): 985–94. doi:10.1016/S0022-2836(03)00381-4. PMID 12729736.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
Lizano E, Schuster J, Müller M, et al. (2007). "A splice variant of the human CCA-adding enzyme with modified activity". J. Mol. Biol. 366 (4): 1258–65. doi:10.1016/j.jmb.2006.12.016. PMID 17204286.

PDB gallery

1ou5: Crystal structure of human CCA-adding enzyme

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase

2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase

2.7.3: N acceptor	Creatine

2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I II III IV V RNA-directed DNA polymerase Reverse transcriptase Telomerase DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase

RNA nucleotidyltransferase	RNA polymerase/DNA-directed RNA polymerase RNA polymerase I RNA polymerase II RNA polymerase III RNA polymerase IV Primase RNA-dependent RNA polymerase PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase

Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases

2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases

2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

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TRNT1

References

Further reading