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A2Q9N1

- CREB_ASPNC

UniProt

A2Q9N1 - CREB_ASPNC

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Protein

Probable ubiquitin carboxyl-terminal hydrolase creB

Gene
creB, An01g08470
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 sitei66 – 661Nucleophile 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: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 – 63159 Reviewed predictionAdd
BLAST

Compositional bias

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

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: February 19, 2014
This is version 36 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

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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