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Q0CT11 (CREB_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable ubiquitin carboxyl-terminal hydrolase creB
EC=3.4.19.12
Alternative name(s):
Carbon catabolite repression protein B
Deubiquitinating enzyme creB
Ubiquitin thioesterase creB
Ubiquitin-hydrolyzing enzyme creB
Ubiquitin-specific-processing protease creB
Gene names
Name:creB
ORF Names:ATEG_03173
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length768 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ubiquitin thioesterase component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Deubiquitinates the creA catabolic repressor and the quinate permease qutD. Plays also a role in response to carbon starvation and the control of extracellular proteases activity 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).

Subunit structure

Interacts with creA, creC and qutD By similarity.

Sequence similarities

Belongs to the peptidase C19 family.

Sequence caution

The sequence EAU36447.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 768768Probable ubiquitin carboxyl-terminal hydrolase creB
PRO_0000395683

Regions

Coiled coil574 – 63360 Potential
Compositional bias28 – 325Poly-Pro

Sites

Active site641Nucleophile By similarity
Active site4191Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CT11 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: 8ED13742A82E7656

FASTA76886,786
        10         20         30         40         50         60 
MGSLFRSFRR DAGATAPSVG ATPAKKEPPP PPMTPLEKML QDMGAIREDG SDKFFGMENY 

        70         80         90        100        110        120 
GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLTAALA ETLRYPNPNA HLEAEAQAEK 

       130        140        150        160        170        180 
QKAANAQRPG APPNQPQKPE DKDSPEYKKK MALQTFPLLE TKNNAPSYGM SESLFTSLKD 

       190        200        210        220        230        240 
LFESVVGSQS RIGIVRPQHF LDVLRREHEM FRTAMHQDAH EFLNLLLNEV VANVEAEALK 

       250        260        270        280        290        300 
QPSLERSLPP AESSESVEHS GSSGSKTPNT TRWVHELFEG TLTSETQCLT CEKVSQRDEV 

       310        320        330        340        350        360 
FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI KRLPRILALH 

       370        380        390        400        410        420 
LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR LYELYAVVVH IGGGPYHGHY 

       430        440        450        460        470        480 
VAIIKTQDRG WLLFDDEMVE PVDKNYVRNF FGDKPGLACA YVLFYQETTL EAVLREQEQE 

       490        500        510        520        530        540 
NMDPALATTE TNDSLKQNGF AQSPALGLVH SASQIPSHDE PHRLNSLKRA PTAPSLPTHY 

       550        560        570        580        590        600 
EHTDTNSAPS IPKPAMAPPV PPIPETHSMP LSPKKSDLQS RKERAKEEKE RKAAEKERER 

       610        620        630        640        650        660 
QRRKEQEATR KEQEARAREN QRREDAELKA ALEASRASKA DEDRRNQEGQ KDRDPGRSGH 

       670        680        690        700        710        720 
GLSRLKRGSK SFSHRLSKDK DTRVPSSSNP GVPDPNSPPL NNTVVTSEHQ EQEQQPPSDQ 

       730        740        750        760 
QPGASRLSKK HNLNDEERDA NKDPKQDKPG HGKWRSFSLR KKSLGILS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH476597 Genomic DNA. Translation: EAU36447.1. Sequence problems.
RefSeqXP_001212351.1. XM_001212351.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00006518.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00006518; CADATEAP00006518; CADATEAG00006518.
GeneID4317779.

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000192482.
OrthoDBEOG43XZCS.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCREB_ASPTN
AccessionPrimary (citable) accession number: Q0CT11
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: April 3, 2013
This is version 27 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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