UniProt Accession

 CCA_ECOLI; P06961; Q2M9E9 

Genbank Protein ID

 M12788; U28379; U00096; AP009048 

Genbank Nucleotide ID

 AAA23541.1; AAA89136.1; AAC76092.1; BAE77107.1 

Protein Name

 Multifunctional CCA protein 

Protein Synonyms/Alias

 CCA-adding enzyme; CCA tRNA nucleotidyltransferase; tRNA CCA-pyrophosphorylase; tRNA adenylyl-/cytidylyl-transferase; tRNA nucleotidyltransferase; tRNA-NT; 2'-nucleotidase; 2',3'-cyclic phosphodiesterase; Phosphatase 

Gene Name

 cca 

Gene Synonyms/Alias

 b3056; JW3028 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
179	LTPERVWKETESALT	acetylation	[1]
259	TLCHDLGKGLTPPEL	acetylation	[1]
279	GHGPAGVKLVEQLCQ	acetylation	[1]
321	LNPKTIVKLFDSIDA	acetylation	[1]
404	IAAVASWKEQRCPKP	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 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. 

Sequence Annotation

 METAL 21 21 Magnesium (By similarity).
 METAL 23 23 Magnesium (By similarity).
 BINDING 8 8 ATP or CTP; via amide nitrogen (By
 BINDING 11 11 ATP or CTP (By similarity).
 BINDING 91 91 ATP or CTP (By similarity).
 BINDING 137 137 ATP or CTP (By similarity).
 BINDING 140 140 ATP or CTP (By similarity).  

Keyword

 ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nickel; Nucleotide-binding; Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding; Transferase; tRNA processing. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 412 AA 

Protein Sequence

Gene Ontology

 GO:0005524; F:ATP binding; IEA:HAMAP.
 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:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0016791; F:phosphatase activity; IEA:HAMAP.
 GO:0004810; F:tRNA adenylyltransferase activity; IDA:EcoCyc.
 GO:0000049; F:tRNA binding; IEA:HAMAP.
 GO:0016437; F:tRNA cytidylyltransferase activity; IDA:EcoCyc.
 GO:0016311; P:dephosphorylation; IEA:GOC.
 GO:0042245; P:RNA repair; IMP:EcoCyc.
 GO:0001680; P:tRNA 3'-terminal CCA addition; IDA:EcoCyc. 

Interpro

 IPR012006; CCA_bact.
 IPR003607; HD/PDEase_dom.
 IPR006674; HD_domain.
 IPR002646; PolA_pol_head_dom. 

Pfam

 PF01966; HD
 PF01743; PolyA_pol 

SMART

 SM00471; HDc 

PROSITE

  

PRINTS