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Protein

Probable ubiquitin carboxyl-terminal hydrolase creB

Gene

creB

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: 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).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. ubiquitinyl hydrolase activity Source: InterPro

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 Componenti: 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

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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

« Hide

        10         20         30         40         50
MGSFLRSFRR DVGSSTPSVG ATPAKKEPLA LPITPLEKML QEMGSDSVRQ
60 70 80 90 100
DGSDKFFGME NYGNTCYCNS ILQCLYYSVP FREAVLNYPT RTPIESLEAA
110 120 130 140 150
LAKNLRYQNF AANQEAEAQA EKQRLANAQR PGAPPAQPPK PEDKDSSEYK
160 170 180 190 200
KKIALQSLPL LETKNNAGSY GMSESLFTSL KDIFESVVAS QSRIGIVRPQ
210 220 230 240 250
HFLDVLRREN EMFRSAMHQD AHEFLNLVLN EVVANVEAEA MKQPIPSLPP
260 270 280 290 300
ADTTDSSRQS ISSGSKTPNT TRWVHELFEG TLTSETQCLT CENVSQRDEI
310 320 330 340 350
FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI
360 370 380 390 400
KRLPRILALH LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR
410 420 430 440 450
LYELYAVVVH IGGGPYHGHY VSIIKTQDRG WLLFDDEMVE PVDKNYVRNF
460 470 480 490 500
FGDKPGLACA YVLFYQETTL EAVLKEQEME NMNASAADAN EAAVKPNGFP
510 520 530 540 550
QPAGLAHVHS ASQIPVQDEP QRHTGLRRAP TAPQLPTHTE YPGPDIEPSS
560 570 580 590 600
PAVATPPPVP PIPETANRPL SPKKSDIQSK KERAKEEKER KAAEKEMEKQ
610 620 630 640 650
RRKEQEARVK ENQRREEAEL KAALEASKAS KADEDRRNPT ENGKDGDPKR
660 670 680 690 700
SSNGLSRLKR GSKSFSQRLG KDKESRASSS GLPSVPSAEP LTPNPVPLEP
710 720 730 740 750
VQQLSPRKAS PPKESHVVHK PLGQDDEPDA LKSPKGDRAG HGKWRSFSIR

KKSFSILS
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AM269976 Genomic DNA. Translation: CAK43937.1. Sequence problems.
RefSeqiXP_001389270.2. XM_001389233.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00000821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4978128.
KEGGiang:ANI_1_1130014.

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000192482.
KOiK11872.
OrthoDBiEOG7TF7JV.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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]
ProtoNetiSearch...

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: March 4, 2015
This is version 40 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.