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Q91FU0 (VF232_IIV6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation By similarity.

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Sequence similarities

Contains 1 OTU domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-templated transcription, termination

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 671671Putative ubiquitin thioesterase 232R
PRO_0000377774

Regions

Domain392 – 521130OTU
Compositional bias255 – 35298Arg/Ser-rich
Compositional bias548 – 58134Glu-rich

Sites

Active site4001 Potential
Active site4031Nucleophile By similarity
Active site5141 Potential

Sequences

Sequence LengthMass (Da)Tools
Q91FU0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1FD36D7AC7D67CCA

FASTA67175,605
        10         20         30         40         50         60 
MNNNQCMRKK LDELRNIARS YNISITGKKK QQLCDEIIDY QKNNPPRRSP SPRRSPSPRR 

        70         80         90        100        110        120 
ISPECEQWLA NKGINPRTGK AIKIGGPTYK KLEMECKEAS PKIPSPVRQP SPVHSPVRSP 

       130        140        150        160        170        180 
VRQPSPVRFV EKTKGALNKM KKDQLIDFAQ SLGLNPGKLL KPALVDLIFV NQKPPRRSPS 

       190        200        210        220        230        240 
PRRSPSPRRS PSPRRSPSPR PVFVEKTKGA LNKMKKDQLI DLAQSLGLNP GKLLKPALVD 

       250        260        270        280        290        300 
LIFVNQKPVE PIRASSSSRS SRSTRRSSST KPSRRSSSRS RRSSSRSRRS SSRSRRSSSR 

       310        320        330        340        350        360 
SRRSSRRSTS RSRSLSKRSI RNISTVGDLE DLVASNLPIA IPESLSRSLS PSRTDFHEAE 

       370        380        390        400        410        420 
IELGSDFDLN NLPENRIAEL KQLNVLAKQN GFRMINVPLD GNCMFSVIGR AFNTSSSVIR 

       430        440        450        460        470        480 
QHTVDYLRRC KGSFDHIPAN IDDPTINWND YIDRLEEDAC WGDNTALFAA SLALNFQAHI 

       490        500        510        520        530        540 
LQVAGGDEGS WIRFGVNETN MGRIVNMGYL DNFHYIALEP FSGRLDILSI PSTHSKCPPP 

       550        560        570        580        590        600 
EISNRRDEEI RRDEEVEDEV IGERIVREAE VIERELRQEE ELTSIVSTKR SLRPSIPPKI 

       610        620        630        640        650        660 
STEHRRTPKL RPSVPRPSSI RQSQPNVAAL ARLETLTKIK DIIDALQRPL ENKLSTLTNT 

       670 
EKAIMQCIGV A 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the first complete DNA sequence of an invertebrate iridovirus: coding strategy of the genome of Chilo iridescent virus."
Jakob N.J., Mueller K., Bahr U., Darai G.
Virology 286:182-196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Comparative genomic analysis of the family Iridoviridae: re-annotating and defining the core set of iridovirus genes."
Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.
Virol. J. 4:11-11(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF303741 Genomic DNA. Translation: AAK82093.1.
RefSeqNP_149695.1. NC_003038.1.

3D structure databases

ProteinModelPortalQ91FU0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1733388.

Phylogenomic databases

ProtClustDBCLSP2511671.

Family and domain databases

InterProIPR014901. 2-cysteine_adaptor.
IPR003323. OTU.
IPR011112. Rho_N.
[Graphical view]
PfamPF08793. 2C_adapt. 1 hit.
PF02338. OTU. 1 hit.
PF07498. Rho_N. 1 hit.
[Graphical view]
SMARTSM00959. Rho_N. 3 hits.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVF232_IIV6
AccessionPrimary (citable) accession number: Q91FU0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families