Reviewed,
UniProtKB/Swiss-Prot Q1HVH9 (DUB_EBVA8)
Last modified
November 3, 2009.
Version 13.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ubiquitin thiolesterase BPLF1 EC=3.1.2.15 Alternative name(s): Large tegument protein Short name=LTP | ||
| Gene names |
| ||
| Organism | Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4) [Complete proteome] | ||
| Taxonomic identifier | 82830 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 3154 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Plays an important role in viral replication by acting as a deubiquitinating enzyme. The deubiquitinating activity cleaves both K48 and K63-linked ubiquitin chains. Therefore, the protein is likely involved in protecting substrates from proteasomal degradation and may have additional regulatory functions By similarity. |
| Catalytic activity | Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol. |
| Subcellular location | Virion tegument By similarity. Host nucleus By similarity. |
| Sequence similarities | Belongs to the herpesviridae large tegument protein family. Contains 1 peptidase C76 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Cellular component | Host nucleus Virion Virion tegument |
| Domain | Coiled coil Repeat |
| Molecular function | Hydrolase Protease Thiol protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | viral tegument Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase 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 – 3154 | 3154 | Ubiquitin thiolesterase BPLF1 | PRO_0000375969 | |||||
Regions | |||||||||
| Repeat | 335 – 339 | 5 | 1 | ||||||
| Repeat | 340 – 344 | 5 | 2 | ||||||
| Repeat | 345 – 349 | 5 | 3 | ||||||
| Repeat | 350 – 354 | 5 | 4 | ||||||
| Repeat | 355 – 359 | 5 | 5 | ||||||
| Repeat | 360 – 364 | 5 | 6 | ||||||
| Repeat | 365 – 369 | 5 | 7 | ||||||
| Repeat | 370 – 374 | 5 | 8 | ||||||
| Repeat | 375 – 379 | 5 | 9 | ||||||
| Region | 1 – 269 | 269 | Deubiquitination activity By similarity | ||||||
| Region | 335 – 379 | 45 | 9 X 5 AA repeats of P-A-S-A-A | ||||||
| Coiled coil | 1105 – 1135 | 31 | Potential | ||||||
| Coiled coil | 1399 – 1443 | 45 | Potential | ||||||
| Coiled coil | 1711 – 1740 | 30 | Potential | ||||||
| Coiled coil | 1880 – 1909 | 30 | Potential | ||||||
| Motif | 430 – 440 | 11 | Nuclear localization signal By similarity | ||||||
| Compositional bias | 336 – 381 | 46 | Ala-rich | ||||||
| Compositional bias | 532 – 535 | 4 | Poly-Ala | ||||||
| Compositional bias | 1361 – 1364 | 4 | Poly-Asn | ||||||
| Compositional bias | 1480 – 1488 | 9 | Poly-Ala | ||||||
| Compositional bias | 1563 – 1568 | 6 | Poly-Gly | ||||||
| Compositional bias | 1661 – 1664 | 4 | Poly-Pro | ||||||
| Compositional bias | 1835 – 1838 | 4 | Poly-Ala | ||||||
| Compositional bias | 2090 – 2093 | 4 | Poly-Arg | ||||||
| Compositional bias | 2105 – 2108 | 4 | Poly-Ala | ||||||
| Compositional bias | 2850 – 2953 | 104 | Ala-rich | ||||||
Sites | |||||||||
| Active site | 61 | 1 | By similarity | ||||||
| Active site | 195 | 1 | Potential | ||||||
Sequences
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References
| [1] | "The genome of Epstein-Barr virus type 2 strain AG876." Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J. Virology 350:164-170(2006) [PubMed: 16490228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| DQ279927 Genomic DNA. Translation: ABB89229.1. | |
| RefSeq | YP_001129449.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5176165. |
Family and domain databases | |
| InterPro | IPR006928. Pept_C76_UL36-USP. [Graphical view] |
| Pfam | PF04843. Herpes_teg_N. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DUB_EBVA8 | ||||||||
| Accession | Primary (citable) accession number: Q1HVH9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


