Q4WQI1 (CREB_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	creB
ORF Names:	AFUA_4G12910

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	775 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 activity	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).
Subunit structure	Interacts with creA, creC and qutD By similarity.
Sequence similarities	Belongs to the peptidase C19 family.
Sequence caution	The sequence EAL89503.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Coiled coil
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbon catabolite repression of transcription Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 775	775	Probable ubiquitin carboxyl-terminal hydrolase creB		PRO_0000395680
Regions
	Coiled coil	586 – 653	68	Potential
	Compositional bias	713 – 734	22	Gln-rich
Sites
	Active site	64	1	Nucleophile By similarity
	Active site	419	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WQI1 [UniParc]. Last modified July 13, 2010. Version 3. Checksum: 035E52A005B5368A	FASTA	775	87,513
	10 20 30 40 50 60 MGSFLRSFRH NGGSTAPSVG AVPAKKEPQP PPMTPLEKRL LDMGPIREDG SDKFYGMENY 70 80 90 100 110 120 GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLEAALA KSLRYPNPNA QLEAEAQAEK 130 140 150 160 170 180 QKAANAQRPG MPPNPQQKPE DKDSPEYKKK MALQTLPLLE TQNNASSYGM SESLFTSLKD 190 200 210 220 230 240 IFESVVGSQS RIGIIRPQQF LEVLRRDHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK 250 260 270 280 290 300 QPPIEKSLPA PETADSVDQS SSTGSKTPNT TRWVHELFEG LLTSETQCLT CEKVSQRDEV 310 320 330 340 350 360 FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI KRLPRILALH 370 380 390 400 410 420 LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR LYELYAVVVH IGGGPYHGHY 430 440 450 460 470 480 VAIIKTEDRG WLLFDDEMVE PVDKNYVKNF FGDKPGLACA YVLFYQETTL EAVLKEQEQE 490 500 510 520 530 540 NMDSNLAATD ANDTILKQNG FPQSPLAHVH SASQIPSHED NLRPNGLRRA PTAPQLSTHH 550 560 570 580 590 600 EHGDPESAPF SPLSPLSPLS PLSPLSQTPP VPPVPERVTT VATPPKNDAL AKKERAREEK 610 620 630 640 650 660 ERKAAEKERE KAEKLRRKEQ EARMKENQRR EEAELKAALE MSKASKAEED RRLSHENGKE 670 680 690 700 710 720 KQGGSLSRLK RGSKSLSHRL GKDKETRSVS SDLPPVPIPE HSTLSQTGPT SEQQQQQQQQ 730 740 750 760 770 QSPPNHDQPP NSPQLGKPTI REDEQVNHKD SKHERTGHGK WRSFSLRKKS FSILS

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000005 Genomic DNA. Translation: EAL89503.2. Sequence problems.
RefSeq	XP_751541.2. XM_746448.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00007967.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00007967; CADAFUAP00007967; CADAFUAG00007967.
GeneID	3509101.
KEGG	afm:AFUA_4G12910.
Phylogenomic databases
eggNOG	COG5533.
HOGENOM	HOG000192482.
KO	K11872.
OrthoDB	EOG43XZCS.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CREB_ASPFU

Accession

Primary (citable) accession number: Q4WQI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	July 13, 2010
Last modified:	May 1, 2013
This is version 43 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program