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| Annotation rule MF_01262 |
General rule information
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| Accession | MF_01262 |
| Dates | 29-JUL-2005 (Created) 19-NOV-2019 (Last updated, Version 12) |
| Name | CCA_bact_type2 |
| Scope | Bacteria; Proteobacteria |
| Templates | P06961 (CCA_ECOLI); Q7SIB1 (CCA_GEOSE): [Recover all] |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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| Gene name |
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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. |
| Catalytic activity | RHEA:14433: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
EC 2.7.7.72 |
| Cofactor | Mg(2+) |
| 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
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: tRNA adenylyltransferase activity.
GO:0005524; Molecular function: ATP binding.
GO:0016437; Molecular function: tRNA cytidylyltransferase activity.
GO:0001680; Biological process: tRNA 3'-terminal CCA addition.
GO:0000166; Molecular function: nucleotide binding.
GO:0000287; Molecular function: magnesium ion binding.
GO:0004810; Molecular function: tRNA adenylyltransferase activity.
GO:0005524; Molecular function: ATP binding.
GO:0016437; Molecular function: tRNA cytidylyltransferase activity.
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 | ||||||
| METAL | 21 | 21 | Magnesium | [DE] | ||||||||
| METAL | 23 | 23 | Magnesium | D | ||||||||
| BINDING | 8 | 8 | ATP or CTP; via amide nitrogen | G | ||||||||
| BINDING | 11 | 11 | ATP or CTP | R | ||||||||
| BINDING | 91 | 91 | ATP or CTP | R | ||||||||
| BINDING | 137 | 137 | ATP or CTP | R | ||||||||
| BINDING | 140 | 140 | ATP or CTP | R | ||||||||
Additional information
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| Size range | 360-419 amino acids |
| Related rules | MF_01261 (CCA supersedes the current rule) |
| Fusion | 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 B.stearothermophilus CCA-adding enzyme (type 3 subfamily, MF_01263) whose X-ray structure is known. |