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B0Y4P5

- CREB_ASPFC

UniProt

B0Y4P5 - CREB_ASPFC

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Protein

Probable ubiquitin carboxyl-terminal hydrolase creB

Gene

creB

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (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).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 sitei58 – 581NucleophilePROSITE-ProRule annotation
Active sitei413 – 4131Proton 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.062.

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:AFUB_069810
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767Probable ubiquitin carboxyl-terminal hydrolase creBPRO_0000395678Add
BLAST

Interactioni

Subunit structurei

Interacts with creA, creC and qutD.By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 462414USPAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili574 – 64168Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi701 – 72626Gln-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000192482.
OrthoDBiEOG7TF7JV.
PhylomeDBiB0Y4P5.

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.

B0Y4P5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFCLLLGSTA PSVGAVPAKK EPQPPPMTPL EKRLLDMGPI REDGSDKFYG
60 70 80 90 100
MENYGNTCYC NSILQCLYYS VPFREAVINY PTRTPIESLE AALAKSLRYP
110 120 130 140 150
NPNAQLEAEA QAEKQKAANA QRPGMPPNPQ QKPEDKDSPE YKKKMALQTL
160 170 180 190 200
PLLETQNNAS SYGMSESLFT SLKDIFESVV GSQSRIGIIR PQQFLEVLRR
210 220 230 240 250
DHEMFRTAMH QDAHEFLNLL LNEVVANVEA EASKQPPIEK SLPAPETADS
260 270 280 290 300
VDQSSSTGSK TPNTTRWVHE LFEGLLTSET QCLTCEKVSQ RDEVFLDLSV
310 320 330 340 350
DLEQHSSVTS CLRKFSAEEM LCERNKFHCD NCGGLQEAEK RMKIKRLPRI
360 370 380 390 400
LALHLKRFKY TEDLQRLQKL FHRVVYPYHL RLFNTTDDAE DPDRLYELYA
410 420 430 440 450
VVVHIGGGPY HGHYVAIIKT EDRGWLLFDD EMVEPVDKNY VKNFFGDKPG
460 470 480 490 500
LACAYVLFYQ ETTLEAVLKE QEQENMDSNL AATDANDTIL KQNGFPQSPL
510 520 530 540 550
AHVHSASQIP SHEDNLRPNG LRRAPTAPQL STHHEHGDPE SAPFSPLSPL
560 570 580 590 600
SPLSQTPPVP PVPERVTTVA TPPKNDALAK KERAREEKER KAAEKEREKA
610 620 630 640 650
EKLRRKEQEA RMKENQRREE AELKAALEMS KASKAEEDRR LSHENGKEKQ
660 670 680 690 700
GGSLSRLKRG SKSLSHRLGK DKETRSVSSD LPPVPIPEHS TLSQTGPTSE
710 720 730 740 750
QQQQQQQQQQ QQQSPPNHDQ PPNSPQLGKP TIREDEQVNH KDSKHERTGH
760
GKWRSFSLRK KSFSILS
Length:767
Mass (Da):86,762
Last modified:April 8, 2008 - v1
Checksum:iEFF2CE02A19E94D6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS499598 Genomic DNA. Translation: EDP50644.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00006929; CADAFUBP00006801; CADAFUBG00006929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS499598 Genomic DNA. Translation: EDP50644.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C19.062.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUBT00006929 ; CADAFUBP00006801 ; CADAFUBG00006929 .

Phylogenomic databases

HOGENOMi HOG000192482.
OrthoDBi EOG7TF7JV.
PhylomeDBi B0Y4P5.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiCREB_ASPFC
AccessioniPrimary (citable) accession number: B0Y4P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: April 8, 2008
Last modified: October 29, 2014
This is version 30 of the entry and version 1 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