HAMAP rule MF_01262
General rule information
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Accession | MF_01262 |
Dates | 29-JUL-2005 (Created)
17-MAY-2023 (Last updated, Version 19) |
Name | CCA_bact_type2 |
Scope(s) |
Bacteria Pseudomonadota |
Template(s) | P06961 (CCA_ECOLI); Q7SIB1 (CCA_GEOSE); [ Recover all ] |
Triggered by |
HAMAP; MF_01262 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | CCA |
Protein name | 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; |
Gene name | Name=cca; |
Comments
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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 + ATP + 2 CTP = 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 + ATP + 2 CTP = 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; |
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 2 subfamily. |
Keywords
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ATP-binding |
Magnesium |
Metal-binding |
Nucleotide-binding |
Nucleotidyltransferase |
RNA repair |
RNA-binding |
Transferase |
tRNA processing |
Gene Ontology
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GO:0000049; Molecular function:tRNA binding |
GO:0000166; Molecular function:nucleotide binding |
GO:0000287; Molecular function:magnesium ion binding |
GO:0004810; Molecular function:CCA tRNA nucleotidyltransferase activity |
GO:0005524; Molecular function:ATP binding |
GO:0001680; Biological process:tRNA 3'-terminal CCA addition |
Cross-references
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Pfam | PF01743; PolyA_pol; 1; |
Features
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From: CCA_BUCAI (P57169) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 21 | 21 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
[DE] | ||||||||
BINDING | 23 | 23 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | ||||||||
BINDING | 8 | 8 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G | ||||||||
BINDING | 8 | 8 | /ligand="CTP" /ligand_id="ChEBI:CHEBI:37563" |
G | ||||||||
BINDING | 11 | 11 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
BINDING | 11 | 11 | /ligand="CTP" /ligand_id="ChEBI:CHEBI:37563" |
R | ||||||||
BINDING | 91 | 91 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
BINDING | 91 | 91 | /ligand="CTP" /ligand_id="ChEBI:CHEBI:37563" |
R | ||||||||
BINDING | 137 | 137 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
BINDING | 137 | 137 | /ligand="CTP" /ligand_id="ChEBI:CHEBI:37563" |
R | ||||||||
BINDING | 140 | 140 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
BINDING | 140 | 140 | /ligand="CTP" /ligand_id="ChEBI:CHEBI:37563" |
R |
Additional information
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Size range | 360-419 amino acids |
Related rules |
MF_01261 |
Fusion | Nter: None Cter: None |
Comments | The CCA-adding enzyme family consists of 4 different subfamilies: 3 bacterial subfamilies (MF_01261, MF_01262 and MF_01263) and 1 archaeal subfamily (MF_01264). There is no characterized protein in this subfamily. The closest sequence homologs are from type 1 subfamily (MF_01261), which is also a proteobacterial family (E.coli is characterized) but which contains an HD domain associated with phosphohydrolase activities. As the type 2 subfamily does not contain such a domain, it should not possess phosphohydrolase activities. FT lines are propagated from G.stearothermophilus CCA-adding enzyme (type 3 subfamily, MF_01263) whose X-ray structure is known. |