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Q2UUG8

- CREB_ASPOR

UniProt

Q2UUG8 - CREB_ASPOR

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Protein

Probable ubiquitin carboxyl-terminal hydrolase creB

Gene

creB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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 sitei63 – 631NucleophilePROSITE-ProRule annotation
Active sitei418 – 4181Proton 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

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:AO090009000320
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 754754Probable ubiquitin carboxyl-terminal hydrolase creBPRO_0000395682Add
BLAST

Interactioni

Subunit structurei

Interacts with creA, creC and qutD.By similarity

Protein-protein interaction databases

STRINGi5062.CADAORAP00003720.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 467414USPAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili580 – 62950Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi675 – 6806Poly-Ser

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000192482.
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.

Q2UUG8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSFLRSLRR DGPPTPSVGA TPAKKEPPVP PVTPLEKMLQ DMGAIREDGS
60 70 80 90 100
DKFFGMENYG NTCYCNSILQ CLYYSVPFRE AVVNYPTRTP IESLEAALAN
110 120 130 140 150
TLRYQNFAAN LEAEALAEKQ KAANAQRPGA PPNQPQKPED KDSPEYKKKM
160 170 180 190 200
ALQTLPLLET KNNATSYGMS ESLFTSLKDL FESVVASQSR IGIIRPQHFL
210 220 230 240 250
DVLRREHEMF RTAMHQDAHE FLNLLLNEVV ANVEAEASKQ PEPERSLPPA
260 270 280 290 300
ESADSTELSG SSGSKTPNTT RWVHELFEGT LTSETQCLTC EKVSQRDEVF
310 320 330 340 350
LDLSVDLEQH SSVTSCLRKF SAEEMLCERN KFHCDNCGGL QEAEKRMKIK
360 370 380 390 400
RLPRILALHL KRFKYTEDLQ RLQKLFHRVV YPYHLRLFNT TDDAEDPDRL
410 420 430 440 450
YELYAVVVHI GGGPYHGHYV AIIKTQDRGW LLFDDEMVEP VDKNYVRNFF
460 470 480 490 500
GDRPGLACAY VLFYQETTLE AVMKEQEQEN MDLNTSVADI NDSTLKQNGY
510 520 530 540 550
PLSPGLAHVH SASQIPSPSE PARFSNLQRA PTAPPLFPHP EHADSESSPA
560 570 580 590 600
DPSTTASATP PVPPIPDIHS LPLSPKKSDS HFKKERAKEE KERKANEKEK
610 620 630 640 650
EKQRRRDQEA RIREQRREDA EIRAALEASK ASKAEEDRRH SPDDTKKSSH
660 670 680 690 700
GLSRLKRGSK SFSHRLGKDK ENRVSSSSHS ATPIAEHPPS RNGASESQQQ
710 720 730 740 750
LPNGQSPGSH GLHTRHTGLD EERDTLKDPK HDRSGHHGKW RSFSLKKKSF

SILS
Length:754
Mass (Da):84,965
Last modified:July 13, 2010 - v2
Checksum:i5C2FE319F4111992
GO

Sequence cautioni

The sequence BAE54797.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007150 Genomic DNA. Translation: BAE54797.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007150 Genomic DNA. Translation: BAE54797.1 . Sequence problems.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00003720.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000192482.
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 Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiCREB_ASPOR
AccessioniPrimary (citable) accession number: Q2UUG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: October 1, 2014
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