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Q4WQI1

- CREB_ASPFU

UniProt

Q4WQI1 - CREB_ASPFU

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Protein

Probable ubiquitin carboxyl-terminal hydrolase creB

Gene

creB

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (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 sitei64 – 641NucleophilePROSITE-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
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:AFUA_4G12910
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775Probable ubiquitin carboxyl-terminal hydrolase creBPRO_0000395680Add
BLAST

Interactioni

Subunit structurei

Interacts with creA, creC and qutD.By similarity

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007967.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 468414USPAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili586 – 65368Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi713 – 73422Gln-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000192482.
InParanoidiQ4WQI1.
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.

Q4WQI1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSFLRSFRH NGGSTAPSVG AVPAKKEPQP PPMTPLEKRL LDMGPIREDG
60 70 80 90 100
SDKFYGMENY GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLEAALA
110 120 130 140 150
KSLRYPNPNA QLEAEAQAEK QKAANAQRPG MPPNPQQKPE DKDSPEYKKK
160 170 180 190 200
MALQTLPLLE TQNNASSYGM SESLFTSLKD IFESVVGSQS RIGIIRPQQF
210 220 230 240 250
LEVLRRDHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK QPPIEKSLPA
260 270 280 290 300
PETADSVDQS SSTGSKTPNT TRWVHELFEG LLTSETQCLT CEKVSQRDEV
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 VAIIKTEDRG WLLFDDEMVE PVDKNYVKNF
460 470 480 490 500
FGDKPGLACA YVLFYQETTL EAVLKEQEQE NMDSNLAATD ANDTILKQNG
510 520 530 540 550
FPQSPLAHVH SASQIPSHED NLRPNGLRRA PTAPQLSTHH EHGDPESAPF
560 570 580 590 600
SPLSPLSPLS PLSPLSQTPP VPPVPERVTT VATPPKNDAL AKKERAREEK
610 620 630 640 650
ERKAAEKERE KAEKLRRKEQ EARMKENQRR EEAELKAALE MSKASKAEED
660 670 680 690 700
RRLSHENGKE KQGGSLSRLK RGSKSLSHRL GKDKETRSVS SDLPPVPIPE
710 720 730 740 750
HSTLSQTGPT SEQQQQQQQQ QSPPNHDQPP NSPQLGKPTI REDEQVNHKD
760 770
SKHERTGHGK WRSFSLRKKS FSILS
Length:775
Mass (Da):87,513
Last modified:July 13, 2010 - v3
Checksum:i035E52A005B5368A
GO

Sequence cautioni

The sequence EAL89503.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL89503.2. Sequence problems.
RefSeqiXP_751541.2. XM_746448.2.

Genome annotation databases

EnsemblFungiiCADAFUAT00007967; CADAFUAP00007967; CADAFUAG00007967.
GeneIDi3509101.
KEGGiafm:AFUA_4G12910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL89503.2 . Sequence problems.
RefSeqi XP_751541.2. XM_746448.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00007967.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00007967 ; CADAFUAP00007967 ; CADAFUAG00007967 .
GeneIDi 3509101.
KEGGi afm:AFUA_4G12910.

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000192482.
InParanoidi Q4WQI1.
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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiCREB_ASPFU
AccessioniPrimary (citable) accession number: Q4WQI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: July 13, 2010
Last modified: October 29, 2014
This is version 48 of the entry and version 3 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