Q96V54 (CREB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
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
Synonyms:	molB
ORF Names:	AN3587

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › Emericella nidulans › mitosporic Emericella nidulans

Protein attributes

Sequence length	766 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
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. Ref.5 Ref.8
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 Reference proteome
Gene Ontology (GO)
Biological_process	carbon catabolite repression of transcription Inferred from mutant phenotype Ref.1Ref.5. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 766	766	Ubiquitin carboxyl-terminal hydrolase creB		PRO_0000395684
Regions
	Coiled coil	573 – 620	48	Potential
	Compositional bias	547 – 572	26	Pro-rich
Sites
	Active site	64	1	Nucleophile By similarity
	Active site	417	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q96V54 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: A29EC2B530092896	FASTA	766	86,229
	10 20 30 40 50 60 MGSFLKSFRK DVGSAAPSVG APPAKKEPQP LPMTPLEKML TELGPIRGDG SDKFYGMENF 70 80 90 100 110 120 GNTCYCNSIL QCLYYSVPFR EAVLNYPKRT PIEDLEAALA KALRYQDPNA RLEAEALAEK 130 140 150 160 170 180 QKAANSPRPG QPPNPQQKPE DKDSPEYKKK LALQTLPLLE TTDNSVSYGI PESLFSSLKD 190 200 210 220 230 240 MFESIVGSQS RIGIIRPQHF LEVLRRENEM FRTAMHQDAH EFLNLLLNEV VVDVEKAAAK 250 260 270 280 290 300 LLESPQPASD VSDSVIPSSS SGSRTPNTTR WVHELFEGLL TSETQCLTCE KASQRDEVFL 310 320 330 340 350 360 DLSVDLEQHS SVTSCLRKFS AEEMLCERNK FHCDNCGGLQ EAEKRMKIKR LPRILALHLK 370 380 390 400 410 420 RFKYTEDLQR LQKLFHRVVY PYHLRLFNTT DDAEDPDRLY ELYAVVVHIG GGPYHGHYVS 430 440 450 460 470 480 IIKTQDRGWL LFDDEMVEPV DKNYVRNFFG DKPGLACAYV LFYQETTMEA VMKEQEQENT 490 500 510 520 530 540 EPPVEVNAST LKQNGFSSSA TLAHAHSASQ VPTYEDHDRF TGLKRAPTAP QLSTHPEHTT 550 560 570 580 590 600 TDSESLPSPA PDPAPLTSLP PIPPIPETPP APLTSRKSDL QSKKERVKEE KERKAAEKEK 610 620 630 640 650 660 EKQRRKEIET RLKDRQRRED DDLKAALEAS KVSKEDEDRR NHAENGTSKK NAGGLGRFRS 670 680 690 700 710 720 LSQRLSTKES RTSLSRIPPL PNGNHTLSKV PDESEQTHPK SPTPPAPLSR PASQPLNDDL 730 740 750 760 LGSPRADTLA VPTEQEHIKN SKHDRSSHGK WRSFSLRKKS FNILSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Carbon catabolite repression in Aspergillus nidulans involves deubiquitination." Lockington R.A., Kelly J.M. Mol. Microbiol. 40:1311-1321(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]	"The function of CreA, the carbon catabolite repressor of Aspergillus nidulans, is regulated at the transcriptional and post-transcriptional level." Strauss J., Horvath H.K., Abdallah B.M., Kindermann J., Mach R.L., Kubicek C.P. Mol. Microbiol. 32:169-178(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"The WD40-repeat protein CreC interacts with and stabilizes the deubiquitinating enzyme CreB in vivo in Aspergillus nidulans." Lockington R.A., Kelly J.M. Mol. Microbiol. 43:1173-1182(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CREC.
[6]	"Molecular characterization and analysis of the acrB gene of Aspergillus nidulans: a gene identified by genetic interaction as a component of the regulatory network that includes the CreB deubiquitination enzyme." Boase N.A., Lockington R.A., Adams J.R., Rodbourn L., Kelly J.M. Genetics 164:95-104(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"The interaction of induction, repression and starvation in the regulation of extracellular proteases in Aspergillus nidulans: evidence for a role for CreA in the response to carbon starvation." Katz M.E., Bernardo S.M., Cheetham B.F. Curr. Genet. 54:47-55(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Identifying target proteins of the CreB deubiquitination enzyme in the fungus Aspergillus nidulans." Kamlangdee N. Thesis (2008), University of Adelaide, Australia Cited for: INTERACTION WITH CREA AND QUTD, FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF327414 Genomic DNA. Translation: AAL04454.1. AACD01000061 Genomic DNA. Translation: EAA59795.1. BN001302 Genomic DNA. Translation: CBF75829.1.
RefSeq	XP_661191.1. XM_656099.1.
3D structure databases
HSSP	HSSP built from PDB template 1NB8 based on UniProtKB Q93009.
ProteinModelPortal	Q96V54.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00005157; CADANIAP00005157; CADANIAG00005157.
GeneID	2873003.
KEGG	ani:AN3587.2.
Phylogenomic databases
eggNOG	COG5533.
HOGENOM	HOG000192482.
KO	K11872.
OMA	DEMVEPV.
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_EMENI

Accession

Primary (citable) accession number: Q96V54
Secondary accession number(s): C8V4E2, Q5B793

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program