Reviewed,
UniProtKB/Swiss-Prot P03186 (DUB_EBVB9)
Last modified
November 3, 2009.
Version 51.
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 B95-8) (HHV-4) (Human herpesvirus 4) [Complete proteome] | ||
| Taxonomic identifier | 10377 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 3149 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. Ref.3 |
| 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 – 3149 | 3149 | Ubiquitin thiolesterase BPLF1 | PRO_0000116038 | |||||
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 | ||||||
| Region | 1 – 269 | 269 | Deubiquitination activity By similarity | ||||||
| Region | 335 – 374 | 40 | 8 X 5 AA repeats of P-A-S-A-A | ||||||
| Coiled coil | 1100 – 1130 | 31 | Potential | ||||||
| Coiled coil | 1394 – 1446 | 53 | Potential | ||||||
| Coiled coil | 1706 – 1735 | 30 | Potential | ||||||
| Coiled coil | 1875 – 1904 | 30 | Potential | ||||||
| Motif | 425 – 435 | 11 | Nuclear localization signal By similarity | ||||||
| Compositional bias | 336 – 376 | 41 | Ala-rich | ||||||
| Compositional bias | 527 – 530 | 4 | Poly-Ala | ||||||
| Compositional bias | 532 – 535 | 4 | Poly-Thr | ||||||
| Compositional bias | 1356 – 1359 | 4 | Poly-Asn | ||||||
| Compositional bias | 1475 – 1483 | 9 | Poly-Ala | ||||||
| Compositional bias | 1558 – 1563 | 6 | Poly-Gly | ||||||
| Compositional bias | 1656 – 1659 | 4 | Poly-Pro | ||||||
| Compositional bias | 1830 – 1833 | 4 | Poly-Ala | ||||||
| Compositional bias | 2085 – 2088 | 4 | Poly-Arg | ||||||
| Compositional bias | 2100 – 2103 | 4 | Poly-Ala | ||||||
| Compositional bias | 2845 – 2948 | 104 | Ala-rich | ||||||
Sites | |||||||||
| Active site | 61 | 1 | By similarity | ||||||
| Active site | 195 | 1 | Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed: 6087149] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Proteins of purified Epstein-Barr virus." Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E., Illanes D., Sarracino D., Kieff E. Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004) [PubMed: 15534216] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [3] | "The EBV deubiquitinating enzyme, BPLF1, reduces EBV ribonucleotide reductase activity." Whitehurst C.B., Ning S., Bentz G.L., Dufour F., Gershburg E., Shackelford J., Langelier Y., Pagano J.S. J. Virol. 83:4345-4353(2009) [PubMed: 19244336] [Abstract] Cited for: FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| V01555 Genomic DNA. Translation: CAA24839.1. AJ507799 Genomic DNA. Translation: CAD53402.1. | |
| PIR | QQBE8. G93065. |
| RefSeq | YP_401652.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3783726. |
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_EBVB9 | ||||||||
| Accession | Primary (citable) accession number: P03186 Secondary accession number(s): Q777G4 | ||||||||
| Entry history |
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| 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


