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A2Q9N1

- CREB_ASPNC

UniProt

A2Q9N1 - CREB_ASPNC

Protein

Probable ubiquitin carboxyl-terminal hydrolase creB

Gene

creB

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    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 sitei66 – 661NucleophilePROSITE-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:An01g08470
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 2R

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 758758Probable ubiquitin carboxyl-terminal hydrolase creBPRO_0000395681Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts with creA, creC and qutD.By similarity

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00000821.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 468412USPAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili573 – 63159Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi530 – 57243Pro-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.

    A2Q9N1-1 [UniParc]FASTAAdd to Basket

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    MGSFLRSFRR DVGSSTPSVG ATPAKKEPLA LPITPLEKML QEMGSDSVRQ    50
    DGSDKFFGME NYGNTCYCNS ILQCLYYSVP FREAVLNYPT RTPIESLEAA 100
    LAKNLRYQNF AANQEAEAQA EKQRLANAQR PGAPPAQPPK PEDKDSSEYK 150
    KKIALQSLPL LETKNNAGSY GMSESLFTSL KDIFESVVAS QSRIGIVRPQ 200
    HFLDVLRREN EMFRSAMHQD AHEFLNLVLN EVVANVEAEA MKQPIPSLPP 250
    ADTTDSSRQS ISSGSKTPNT TRWVHELFEG TLTSETQCLT CENVSQRDEI 300
    FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI 350
    KRLPRILALH LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR 400
    LYELYAVVVH IGGGPYHGHY VSIIKTQDRG WLLFDDEMVE PVDKNYVRNF 450
    FGDKPGLACA YVLFYQETTL EAVLKEQEME NMNASAADAN EAAVKPNGFP 500
    QPAGLAHVHS ASQIPVQDEP QRHTGLRRAP TAPQLPTHTE YPGPDIEPSS 550
    PAVATPPPVP PIPETANRPL SPKKSDIQSK KERAKEEKER KAAEKEMEKQ 600
    RRKEQEARVK ENQRREEAEL KAALEASKAS KADEDRRNPT ENGKDGDPKR 650
    SSNGLSRLKR GSKSFSQRLG KDKESRASSS GLPSVPSAEP LTPNPVPLEP 700
    VQQLSPRKAS PPKESHVVHK PLGQDDEPDA LKSPKGDRAG HGKWRSFSIR 750
    KKSFSILS 758
    Length:758
    Mass (Da):84,902
    Last modified:July 13, 2010 - v2
    Checksum:i66D526B4DA07ED6D
    GO

    Sequence cautioni

    The sequence CAK43937.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM269976 Genomic DNA. Translation: CAK43937.1. Sequence problems.
    RefSeqiXP_001389270.2. XM_001389233.2.

    Genome annotation databases

    GeneIDi4978128.
    KEGGiang:ANI_1_1130014.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM269976 Genomic DNA. Translation: CAK43937.1 . Sequence problems.
    RefSeqi XP_001389270.2. XM_001389233.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00000821.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4978128.
    KEGGi ang:ANI_1_1130014.

    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. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiCREB_ASPNC
    AccessioniPrimary (citable) accession number: A2Q9N1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 37 of the entry and version 2 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