Reviewed,
UniProtKB/Swiss-Prot Q775U0 (MCEL_CAMPS)
Last modified
January 19, 2010.
Version 23.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: mRNA-capping enzyme large subunit Including the following 2 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 | ||
| Gene names |
| ||
| Organism | Camelpox virus (strain CMS) | ||
| Taxonomic identifier | 203172 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus | ||
| Virus host | Camelus [TaxID: 9836] |
Protein attributes
| Sequence length | 844 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the first two reactions in the mRNA cap formation pathway. |
| Catalytic activity | A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate. GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. |
| Subunit structure | Heterodimer of a large and a small subunit By similarity. |
| Sequence similarities | Belongs to the viral GTase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | mRNA capping mRNA processing |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Hydrolase Nucleotidyltransferase Transferase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA guanylyltransferase activityInferred from electronic annotation. Source: EC polynucleotide 5'-phosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The sequence of camelpox virus shows it is most closely related to variola virus, the cause of smallpox." Gubser C., Smith G.L. J. Gen. Virol. 83:855-872(2002) [PubMed: 11907336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY009089 Genomic DNA. Translation: AAG37576.1. |
3D structure databases | |
| SMR | Q775U0. Positions 545-844. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR019602. mRNA_cap_ATPase/GuylTrfase_vir. IPR004971. Pox_MCEL. [Graphical view] |
| Pfam | PF10640. Pox_ATPase-GT. 1 hit. PF03291. Pox_MCEL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MCEL_CAMPS | ||||||||
| Accession | Primary (citable) accession number: Q775U0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

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