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Q4WQI1 (CREB_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 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:AFUA_4G12910
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length775 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.

Contains 1 USP domain.

Sequence caution

The sequence EAL89503.2 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 775775Probable ubiquitin carboxyl-terminal hydrolase creB
PRO_0000395680

Regions

Domain55 – 468414USP
Coiled coil586 – 65368 Potential
Compositional bias713 – 73422Gln-rich

Sites

Active site641Nucleophile By similarity
Active site4191Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WQI1 [UniParc].

Last modified July 13, 2010. Version 3.
Checksum: 035E52A005B5368A

FASTA77587,513
        10         20         30         40         50         60 
MGSFLRSFRH NGGSTAPSVG AVPAKKEPQP PPMTPLEKRL LDMGPIREDG SDKFYGMENY 

        70         80         90        100        110        120 
GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLEAALA KSLRYPNPNA QLEAEAQAEK 

       130        140        150        160        170        180 
QKAANAQRPG MPPNPQQKPE DKDSPEYKKK MALQTLPLLE TQNNASSYGM SESLFTSLKD 

       190        200        210        220        230        240 
IFESVVGSQS RIGIIRPQQF LEVLRRDHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK 

       250        260        270        280        290        300 
QPPIEKSLPA PETADSVDQS SSTGSKTPNT TRWVHELFEG LLTSETQCLT 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 
VAIIKTEDRG WLLFDDEMVE PVDKNYVKNF FGDKPGLACA YVLFYQETTL EAVLKEQEQE 

       490        500        510        520        530        540 
NMDSNLAATD ANDTILKQNG FPQSPLAHVH SASQIPSHED NLRPNGLRRA PTAPQLSTHH 

       550        560        570        580        590        600 
EHGDPESAPF SPLSPLSPLS PLSPLSQTPP VPPVPERVTT VATPPKNDAL AKKERAREEK 

       610        620        630        640        650        660 
ERKAAEKERE KAEKLRRKEQ EARMKENQRR EEAELKAALE MSKASKAEED RRLSHENGKE 

       670        680        690        700        710        720 
KQGGSLSRLK RGSKSLSHRL GKDKETRSVS SDLPPVPIPE HSTLSQTGPT SEQQQQQQQQ 

       730        740        750        760        770 
QSPPNHDQPP NSPQLGKPTI REDEQVNHKD SKHERTGHGK WRSFSLRKKS FSILS 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000005 Genomic DNA. Translation: EAL89503.2. Sequence problems.
RefSeqXP_751541.2. XM_746448.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00007967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007967; CADAFUAP00007967; CADAFUAG00007967.
GeneID3509101.
KEGGafm:AFUA_4G12910.

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000192482.
KOK11872.
OrthoDBEOG7TF7JV.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCREB_ASPFU
AccessionPrimary (citable) accession number: Q4WQI1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: February 19, 2014
This is version 46 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries