B0Y4P5 (CREB_ASPFC) 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:	AFUB_069810

Organism

Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]

Taxonomic identifier

451804 [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	767 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Coiled coil
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete 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 – 767	767	Probable ubiquitin carboxyl-terminal hydrolase creB		PRO_0000395678
Regions
	Coiled coil	574 – 641	68	Potential
	Compositional bias	701 – 726	26	Gln-rich
Sites
	Active site	58	1	Nucleophile By similarity
	Active site	413	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0Y4P5 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: EFF2CE02A19E94D6	FASTA	767	86,762
	10 20 30 40 50 60 MFCLLLGSTA PSVGAVPAKK EPQPPPMTPL EKRLLDMGPI REDGSDKFYG MENYGNTCYC 70 80 90 100 110 120 NSILQCLYYS VPFREAVINY PTRTPIESLE AALAKSLRYP NPNAQLEAEA QAEKQKAANA 130 140 150 160 170 180 QRPGMPPNPQ QKPEDKDSPE YKKKMALQTL PLLETQNNAS SYGMSESLFT SLKDIFESVV 190 200 210 220 230 240 GSQSRIGIIR PQQFLEVLRR DHEMFRTAMH QDAHEFLNLL LNEVVANVEA EASKQPPIEK 250 260 270 280 290 300 SLPAPETADS VDQSSSTGSK TPNTTRWVHE LFEGLLTSET QCLTCEKVSQ RDEVFLDLSV 310 320 330 340 350 360 DLEQHSSVTS CLRKFSAEEM LCERNKFHCD NCGGLQEAEK RMKIKRLPRI LALHLKRFKY 370 380 390 400 410 420 TEDLQRLQKL FHRVVYPYHL RLFNTTDDAE DPDRLYELYA VVVHIGGGPY HGHYVAIIKT 430 440 450 460 470 480 EDRGWLLFDD EMVEPVDKNY VKNFFGDKPG LACAYVLFYQ ETTLEAVLKE QEQENMDSNL 490 500 510 520 530 540 AATDANDTIL KQNGFPQSPL AHVHSASQIP SHEDNLRPNG LRRAPTAPQL STHHEHGDPE 550 560 570 580 590 600 SAPFSPLSPL SPLSQTPPVP PVPERVTTVA TPPKNDALAK KERAREEKER KAAEKEREKA 610 620 630 640 650 660 EKLRRKEQEA RMKENQRREE AELKAALEMS KASKAEEDRR LSHENGKEKQ GGSLSRLKRG 670 680 690 700 710 720 SKSLSHRLGK DKETRSVSSD LPPVPIPEHS TLSQTGPTSE QQQQQQQQQQ QQQSPPNHDQ 730 740 750 760 PPNSPQLGKP TIREDEQVNH KDSKHERTGH GKWRSFSLRK KSFSILS

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CEA10 / CBS 144.89 / FGSC A1163.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS499598 Genomic DNA. Translation: EDP50644.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUBT00006929; CADAFUBP00006801; CADAFUBG00006929.
Phylogenomic databases
HOGENOM	HOG000192482.
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_ASPFC

Accession

Primary (citable) accession number: B0Y4P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	April 8, 2008
Last modified:	May 16, 2012
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program