Multifunctional CCA protein (P06961)

Identification
Name:Multifunctional CCA protein
Synonyms:
  • CCA-adding enzyme
  • tRNA CCA-pyrophosphorylase
  • tRNA adenylyl-/cytidylyl-transferase
  • tRNA nucleotidyltransferase
  • tRNA-NT
  • 2'-nucleotidase
  • 2',3'-cyclic phosphodiesterase
  • Phosphatase
Gene Name:cca
Enzyme Class:
Biological Properties
General Function:Involved in RNA binding
Specific Function:Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent phosphodiesterase activity toward 2',3'-cAMP, 2',3'-cGMP, and 2',3'-cCMP. Without metal or in the presence of Mg(2+), this protein hydrolyzes 2',3'-cyclic substrates with the formation of 2'-nucleotides, whereas in the presence of Ni(2+), it also produces some 3'-nucleotides. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0tRNA precursor+2.0Thumb+1.0Thumb ↔ 1.0tRNA with a 3' CCA end+3.0Thumb
1.0tRNA precursor + 2.0Cytidine triphosphate + 1.0Adenosine triphosphate ↔ 1.0tRNA with a 3' CCA end + 3.0Pyrophosphate
ReactionCard
1.0tRNA precursor+1.0Thumb ↔ 1.0tRNA with a 3' cytidine+1.0Thumb
1.0tRNA precursor + 1.0Cytidine triphosphate ↔ 1.0tRNA with a 3' cytidine + 1.0Pyrophosphate
ReactionCard
1.0tRNA with a 3' cytidine+1.0Thumb ↔ 1.0tRNA with a 3' CC end+1.0Thumb
1.0tRNA with a 3' cytidine + 1.0Cytidine triphosphate ↔ 1.0tRNA with a 3' CC end + 1.0Pyrophosphate
ReactionCard
1.0tRNA with a 3' CC end+1.0Thumb ↔ 1.0tRNA with a 3' CCA end+1.0Thumb
1.0tRNA with a 3' CC end + 1.0Adenosine triphosphate ↔ 1.0tRNA with a 3' CCA end + 1.0Pyrophosphate
ReactionCard
1.0tRNA precursor+2.0Thumb+1.0Thumb+1.0tRNA with a 3' cytidine+1.0tRNA with a 3' CC end ↔ 1.0tRNA with a 3' CCA end+3.0Thumb
1.0tRNA precursor + 2.0Cytidine triphosphate + 1.0Adenosine triphosphate + 1.0tRNA with a 3' cytidine + 1.0tRNA with a 3' CC end ↔ 1.0tRNA with a 3' CCA end + 3.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0A tRNA precursor+2.0Thumb+1.0Thumb → 1.0a tRNA with a 3' CCA end+3.0Thumb
1.0A tRNA precursor + 2.0Cytidine triphosphate + 1.0Adenosine triphosphate → 1.0a tRNA with a 3' CCA end + 3.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00082Cytidine triphosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
adenylyltransferase activity
ATP binding
binding
catalytic activity
nucleic acid binding
nucleoside binding
nucleotidyltransferase activity
purine nucleoside binding
RNA binding
transferase activity
transferase activity, transferring phosphorus-containing groups
tRNA adenylyltransferase activity
Process
cellular macromolecule metabolic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
RNA metabolic process
RNA processing
tRNA 3'-end processing
tRNA 3'-terminal CCA addition
tRNA metabolic process
tRNA processing
Gene Properties
Blattner:b3056
Gene OrientationClockwise
Centisome Percentage:68.97
Left Sequence End3199913
Right Sequence End3201151
Gene Sequence:
>1239 bp
ATGAAAGCATTGACTTATCACGGCCCACATCACGTTCAGGTAGAAAATGTTCCCGATCCG
GGCGTTGAACAGGCAGATGATATTATTCTGCGTATTACGGCAACGGCGATCTGTGGCTCT
GACCTCCATCTTTATCGAGGCAAAATACCTCAGGTTAAACATGGCGATATTTTTGGTCAT
GAATTTATGGGGGAAGTAGTTGAAACCGGAAAGGACGTAAAAAATTTGCAAAAAGGCGAC
CGAGTGGTAATTCCGTTCGTCATTGCTTGTGGCGACTGTTTTTTCTGTCGATTGCAACAA
TATGCCGCCTGCGAAAATACCAATGCGGGTAAAGGCGCTGCGCTCAATAAAAAACAGATA
CCAGCTCCAGCGGCATTGTTTGGTTATAGTCACCTGTATGGCGGCGTTCCTGGTGGGCAG
GCGGAATATGTCCGCGTCCCTAAAGGGAATGTGGGGCCGTTTAAAGTACCGCCTTTGCTT
TCAGATGATAAAGCGCTTTTCCTTTCTGATATTCTGCCAACGGCATGGCAGGCAGCAAAA
AATGCGCAGATCCAACAAGGTTCAAGCGTTGCAGTCTATGGTGCTGGTCCTGTGGGATTG
TTGACAATCGCCTGTGCACGGTTGCTCGGTGCGGAACAGATTTTTGTTGTTGATCATCAT
CCCTACCGCTTGCATTTCGCCGCCGACCGCTACGGCGCGATCCCGATTAATTTTGATGAA
GACAGCGATCCGGCACAGTCAATTATTGAACAAACGGCAGGTCACCGGGGCGTGGATGCA
GTAATAGACGCCGTCGGTTTTGAAGCGAAAGGCAGCACCACGGAAACGGTGCTGACTAAC
CTGAAACTGGAGGGCAGCAGCGGTAAAGCGTTGCGTCAGTGTATTGCGGCGGTCAGGCGT
GGCGGCATTGTTAGCGTACCGGGCGTCTACGCTGGATTTATTCACGGTTTCCTGTTTGGC
GACGCCTTTGATAAAGGGTTGTCGTTTAAAATGGGACAGACCCACGTTCACGCATGGCTG
GGAGAATTATTACCGTTAATTGAGAAAGGATTACTGAAACCAGAAGAAATTGTTACCCAC
TATATGCCGTTTGAAGAGGCCGCCCGGGGATATGAGATTTTCGAAAAACGTGAAGAGGAG
TGCCGTAAGGTGATTCTGGTACCCGGTGCACAAAGCGCAGAGGCGGCGCAGAAGGCGGTT
TCAGGTCTGGTGAATGCGATGCCGGGGGGAACAATATGA
Protein Properties
Pfam Domain Function:
Protein Residues:412
Protein Molecular Weight:46467
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Multifunctional CCA protein
MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYAL
ARTERKSGSGYTGFTCYAAPDVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRL
LRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALMREMTHAGELEHLTPERVWKE
TESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPAKWHPEIDTGIHTLMTLSMAA
MLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARL
VAEFHDLIHTFPMLNPKTIVKLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQG
RWLREAWEVAQSVPTKAVVEAGFKGVEIREELTRRRIAAVASWKEQRCPKPE
References
External Links:
ResourceLink
Uniprot ID:P06961
Uniprot Name:CCA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062224
Ecogene ID:EG10136
Ecocyc:EG10136
ColiBase:b3056
Kegg Gene:b3056
EchoBASE ID:EB0134
CCDB:CCA_ECOLI
BacMap:16130952
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Cudny, H., Deutscher, M. P. (1986). "High-level overexpression, rapid purification, and properties of Escherichia coli tRNA nucleotidyltransferase." J Biol Chem 261:6450-6453. Pubmed: 3516995
  • Cudny, H., Lupski, J. R., Godson, G. N., Deutscher, M. P. (1986). "Cloning, sequencing, and species relatedness of the Escherichia coli cca gene encoding the enzyme tRNA nucleotidyltransferase." J Biol Chem 261:6444-6449. Pubmed: 3009457
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Yakunin, A. F., Proudfoot, M., Kuznetsova, E., Savchenko, A., Brown, G., Arrowsmith, C. H., Edwards, A. M. (2004). "The HD domain of the Escherichia coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities." J Biol Chem 279:36819-36827. Pubmed: 15210699
  • Zhu, L. Q., Cudny, H., Deutscher, M. P. (1986). "A mutation in Escherichia coli tRNA nucleotidyltransferase that affects only AMP incorporation is in a sequence often associated with nucleotide-binding proteins." J Biol Chem 261:14875-14877. Pubmed: 3533927