Reviewed,
UniProtKB/Swiss-Prot Q5UQX1 (MCE_MIMIV)
Last modified
November 25, 2008.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable mRNA-capping enzyme Including the following 3 domains: 1- Recommended name: Polynucleotide 5'-triphosphatase EC=3.1.3.33 Alternative name(s): mRNA 5'-triphosphatase Short name=TPase 2- Recommended name: mRNA guanylyltransferase EC=2.7.7.50 Alternative name(s): GTP--RNA guanylyltransferase Short name=GTase 3- Recommended name: mRNA (guanine-N(7)-)-methyltransferase EC=2.1.1.56 | ||
| Gene names |
| ||
| Organism | Acanthamoeba polyphaga mimivirus (APMV) [Complete proteome] | ||
| Taxonomic identifier | 212035 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Mimiviridae › Mimivirus | ||
| Virus host | Acanthamoeba polyphaga (Amoeba) [TaxID: 5757] |
Protein attributes
| Sequence length | 1170 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Responsible for methylating the 5'-cap structure of mRNAs. |
| Catalytic activity | A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate. GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the viral GTase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | mRNA capping mRNA processing |
| Cellular component | Virion |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Hydrolase Nucleotidyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Multifunctional enzyme |
Gene Ontology (GO) | |
| Biological process | mRNA capping Inferred from electronic annotation. Source: InterPro |
| Cellular component | virion Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | mRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: EC mRNA guanylyltransferase activityInferred from electronic annotation. Source: InterPro polynucleotide 5'-phosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1170 | 1170 | Probable mRNA-capping enzyme | PRO_0000210133 | |||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||
| Active site | 292 | 1 | N6-GMP-lysine intermediate Potential | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Helix | 17 – 32 | 16 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 36 – 45 | 10 | |||||||||||||||||||||||||||||||||||||
| Helix | 47 – 60 | 14 | |||||||||||||||||||||||||||||||||||||
| Helix | 63 – 65 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 66 – 77 | 12 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 83 – 88 | 6 | |||||||||||||||||||||||||||||||||||||
| Helix | 91 – 101 | 11 | |||||||||||||||||||||||||||||||||||||
| Helix | 106 – 113 | 8 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 137 | 18 | |||||||||||||||||||||||||||||||||||||
| Helix | 138 – 140 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 142 – 152 | 11 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 169 – 183 | 15 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 186 – 198 | 13 | |||||||||||||||||||||||||||||||||||||
| Turn | 199 – 201 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 202 – 204 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 208 – 217 | 10 | |||||||||||||||||||||||||||||||||||||
| Helix | 221 – 235 | 15 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "The 1.2-megabase genome sequence of Mimivirus." Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M. Science 306:1344-1350(2004) [PubMed: 15486256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Rowbotham-Bradford. |
| [2] | "Mimivirus giant particles incorporate a large fraction of anonymous and unique gene products." Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H., Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D. J. Virol. 80:11678-11685(2006) [PubMed: 16971431] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AY653733 Genomic DNA. Translation: AAV50651.1. | |||||||||||||||||||||||||
| RefSeq | YP_142736.1. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| GeneID | 3162607. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR001339. mRNA_cap_enzyme. IPR004971. Pox_MCEL. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF01331. mRNA_cap_enzyme. 1 hit. PF03291. Pox_MCEL. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | MCE_MIMIV | ||||||||
| Accession | Primary (citable) accession number: Q5UQX1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


