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Q4WQI1

- CREB_ASPFU

UniProt

Q4WQI1 - CREB_ASPFU

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Protein
Probable ubiquitin carboxyl-terminal hydrolase creB
Gene
creB, AFUA_4G12910
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 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 sitei64 – 641Nucleophile By similarity
Active sitei419 – 4191Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. carbon catabolite repression of transcription Source: UniProtKB
  2. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:creB
ORF Names:AFUA_4G12910
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775Probable ubiquitin carboxyl-terminal hydrolase creB
PRO_0000395680Add
BLAST

Interactioni

Subunit structurei

Interacts with creA, creC and qutD By similarity.

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007967.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 468414USP
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili586 – 65368 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi713 – 73422Gln-rich
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 USP domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000192482.
KOiK11872.
OrthoDBiEOG7TF7JV.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4WQI1-1 [UniParc]FASTAAdd to Basket

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MGSFLRSFRH NGGSTAPSVG AVPAKKEPQP PPMTPLEKRL LDMGPIREDG    50
SDKFYGMENY GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLEAALA 100
KSLRYPNPNA QLEAEAQAEK QKAANAQRPG MPPNPQQKPE DKDSPEYKKK 150
MALQTLPLLE TQNNASSYGM SESLFTSLKD IFESVVGSQS RIGIIRPQQF 200
LEVLRRDHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK QPPIEKSLPA 250
PETADSVDQS SSTGSKTPNT TRWVHELFEG LLTSETQCLT CEKVSQRDEV 300
FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI 350
KRLPRILALH LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR 400
LYELYAVVVH IGGGPYHGHY VAIIKTEDRG WLLFDDEMVE PVDKNYVKNF 450
FGDKPGLACA YVLFYQETTL EAVLKEQEQE NMDSNLAATD ANDTILKQNG 500
FPQSPLAHVH SASQIPSHED NLRPNGLRRA PTAPQLSTHH EHGDPESAPF 550
SPLSPLSPLS PLSPLSQTPP VPPVPERVTT VATPPKNDAL AKKERAREEK 600
ERKAAEKERE KAEKLRRKEQ EARMKENQRR EEAELKAALE MSKASKAEED 650
RRLSHENGKE KQGGSLSRLK RGSKSLSHRL GKDKETRSVS SDLPPVPIPE 700
HSTLSQTGPT SEQQQQQQQQ QSPPNHDQPP NSPQLGKPTI REDEQVNHKD 750
SKHERTGHGK WRSFSLRKKS FSILS 775
Length:775
Mass (Da):87,513
Last modified:July 13, 2010 - v3
Checksum:i035E52A005B5368A
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL89503.2. Sequence problems.
RefSeqiXP_751541.2. XM_746448.2.

Genome annotation databases

EnsemblFungiiCADAFUAT00007967; CADAFUAP00007967; CADAFUAG00007967.
GeneIDi3509101.
KEGGiafm:AFUA_4G12910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL89503.2 . Sequence problems.
RefSeqi XP_751541.2. XM_746448.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00007967.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00007967 ; CADAFUAP00007967 ; CADAFUAG00007967 .
GeneIDi 3509101.
KEGGi afm:AFUA_4G12910.

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000192482.
KOi K11872.
OrthoDBi EOG7TF7JV.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiCREB_ASPFU
AccessioniPrimary (citable) accession number: Q4WQI1
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

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