HAMAP rule MF_01261

General rule information [?]

PURL	https://purl.expasy.org/hamap/rule/MF_01261
Accession	MF_01261
Dates	29-JUL-2005 (Created) 03-SEP-2024 (Last updated, Version 26)
Name	CCA_bact_type1
Scope(s)	Bacteria Pseudomonadota
Template(s)	P06961; Q7SIB1; [ Recover all ]
Triggered by	HAMAP; MF_01261 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	CCA
Protein name	RecName: Full=Multifunctional CCA protein; Includes: RecName: Full=CCA-adding enzyme; EC=2.7.7.72; AltName: Full=CCA tRNA nucleotidyltransferase; AltName: Full=tRNA CCA-pyrophosphorylase; AltName: Full=tRNA adenylyl-/cytidylyl-transferase; AltName: Full=tRNA nucleotidyltransferase; AltName: Full=tRNA-NT; Includes: RecName: Full=2'-nucleotidase; EC=3.1.3.-; Includes: RecName: Full=2',3'-cyclic phosphodiesterase; EC=3.1.4.-; Includes: RecName: Full=Phosphatase; EC=3.1.3.-;
Gene name	Name=cca;

Comments [?]

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. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
CATALYTIC ACTIVITY	Reaction=a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA- COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CATALYTIC ACTIVITY	Reaction=a tRNA with a 3' CCA end + 2 CTP + ATP = a tRNA with a 3' CCACCA end + 3 diphosphate; Xref=Rhea:RHEA:76235, Rhea:RHEA- COMP:10468, Rhea:RHEA-COMP:18655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:83071, ChEBI:CHEBI:195187; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76236;
COFACTOR	Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Magnesium is required for nucleotidyltransferase activity.;
COFACTOR	Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Nickel for phosphatase activity.;
SUBUNIT	Monomer. Can also form homodimers and oligomers.
DOMAIN	Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities.
MISCELLANEOUS	A single active site specifically recognizes both ATP and CTP and is responsible for their addition.
SIMILARITY	Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.

Keywords [?]

Multifunctional enzyme

Nickel

Nucleotide-binding

Nucleotidyltransferase

Gene Ontology [?]

GO:0000049; Molecular function:tRNA binding

GO:0000166; Molecular function:nucleotide binding

GO:0000287; Molecular function:magnesium ion binding

GO:0004112; Molecular function:cyclic-nucleotide phosphodiesterase activity

GO:0004810; Molecular function:CCA tRNA nucleotidyltransferase activity

GO:0005524; Molecular function:ATP binding

GO:0016791; Molecular function:phosphatase activity

GO:0001680; Biological process:tRNA 3'-terminal CCA addition

Cross-references [?]

Pfam	PF01966; HD; 1;
Pfam	PF01743; PolyA_pol; 1;
PROSITE	PS51831; HD; 1;

Features [?]

From: CCA_ECOLI (P06961)

Key

From

Description

Tag

Condition

FTGroup

BINDING

/ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"

[DE]

BINDING

/ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"

BINDING