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Protein

Ubiquitin thioesterase otubain-like

Gene

otub-1

Organism
Caenorhabditis briggsae
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Hydrolase that can remove conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Specifically cleaves 'Lys-48'-linked polyubiquitin (By similarity).By similarity

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei84 – 841By similarity
Active sitei87 – 871NucleophileBy similarity
Active sitei268 – 2681By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase otubain-likeBy similarity (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme otubain-likeBy similarity
Ubiquitin-specific-processing protease otubain-likeBy similarity
Gene namesi
Name:otub-1Imported
ORF Names:CBG11576
OrganismiCaenorhabditis briggsae
Taxonomic identifieri6238 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000008549 Componentsi: Chromosome V, Unassembled WGS sequence

Organism-specific databases

WormBaseiCBG11576; CBP17228; WBGene00032679; Cbr-otub-1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Ubiquitin thioesterase otubain-likePRO_0000394766Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi6238.CBG11576.

Structurei

3D structure databases

ProteinModelPortaliA8XDJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 275200OTUPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C65 family.Sequence Analysis
Contains 1 OTU domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5539.
HOGENOMiHOG000019496.
InParanoidiA8XDJ2.
KOiK09602.
OMAiEDFHETF.
OrthoDBiEOG71K64D.

Family and domain databases

InterProiIPR003323. OTU_dom.
IPR016615. Otubain.
IPR019400. Peptidase_C65_otubain.
[Graphical view]
PfamiPF10275. Peptidase_C65. 1 hit.
[Graphical view]
PIRSFiPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8XDJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNDTSENQP TTAGIVTTTE DELILQDQQM KRIEDEQKAS PLVGEKMPCA
60 70 80 90 100
TLVSLYDQET APAFFEKANE LAKVYSHIRF IRGDGNCFIR AIQVGLVEIL
110 120 130 140 150
LNDKERLVKF IASCKEWTER LVKLGFPDWT CTDFCEFFIE FIEKVRDGIH
160 170 180 190 200
QKEDVFRIFN DDNTANYLLM FFRLITSGYL KEHAAEYEPF LDEGMSLAQY
210 220 230 240 250
CETEIEAMWK ESDHLGIIAL VRALNIRIRI EYMDRNAAPN GGTHHNLPDG
260 270 280
HDNATFTPDI TLLYRPGHYD LIYKAPAETS KPALPPVA
Length:288
Mass (Da):32,949
Last modified:January 15, 2008 - v1
Checksum:iC82E79D93EE5DA87
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE600985 Genomic DNA. Translation: CAP30711.1.
RefSeqiXP_002637711.1. XM_002637665.1.

Genome annotation databases

EnsemblMetazoaiCBG11576; CBG11576; CBG11576.
GeneIDi8579707.
KEGGicbr:CBG11576.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE600985 Genomic DNA. Translation: CAP30711.1.
RefSeqiXP_002637711.1. XM_002637665.1.

3D structure databases

ProteinModelPortaliA8XDJ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6238.CBG11576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiCBG11576; CBG11576; CBG11576.
GeneIDi8579707.
KEGGicbr:CBG11576.

Organism-specific databases

CTDi8579707.
WormBaseiCBG11576; CBP17228; WBGene00032679; Cbr-otub-1.

Phylogenomic databases

eggNOGiCOG5539.
HOGENOMiHOG000019496.
InParanoidiA8XDJ2.
KOiK09602.
OMAiEDFHETF.
OrthoDBiEOG71K64D.

Family and domain databases

InterProiIPR003323. OTU_dom.
IPR016615. Otubain.
IPR019400. Peptidase_C65_otubain.
[Graphical view]
PfamiPF10275. Peptidase_C65. 1 hit.
[Graphical view]
PIRSFiPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AF16.

Entry informationi

Entry nameiOTUBL_CAEBR
AccessioniPrimary (citable) accession number: A8XDJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 15, 2008
Last modified: July 22, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.