Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q4WQI1

- CREB_ASPFU

UniProt

Q4WQI1 - CREB_ASPFU

Protein

Probable ubiquitin carboxyl-terminal hydrolase creB

Gene

creB

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 3 (13 Jul 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.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 – 641NucleophilePROSITE-ProRule annotation
    Active sitei419 – 4191Proton acceptorPROSITE-ProRule annotation

    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

    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 creBPRO_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 – 468414USPAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili586 – 65368Sequence AnalysisAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

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

    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

    « Hide

    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: October 1, 2014
    This is version 47 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