CREB_EMENI
ID CREB_EMENI Reviewed; 766 AA.
AC Q96V54; C8V4E2; Q5B793;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase creB;
DE EC=3.4.19.12;
DE AltName: Full=Carbon catabolite repression protein B;
DE AltName: Full=Deubiquitinating enzyme creB;
DE AltName: Full=Ubiquitin thioesterase creB;
DE AltName: Full=Ubiquitin-hydrolyzing enzyme creB;
DE AltName: Full=Ubiquitin-specific-processing protease creB;
GN Name=creB; Synonyms=molB; ORFNames=AN3587;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11442830; DOI=10.1046/j.1365-2958.2001.02474.x;
RA Lockington R.A., Kelly J.M.;
RT "Carbon catabolite repression in Aspergillus nidulans involves
RT deubiquitination.";
RL Mol. Microbiol. 40:1311-1321(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION.
RX PubMed=10216870; DOI=10.1046/j.1365-2958.1999.01341.x;
RA Strauss J., Horvath H.K., Abdallah B.M., Kindermann J., Mach R.L.,
RA Kubicek C.P.;
RT "The function of CreA, the carbon catabolite repressor of Aspergillus
RT nidulans, is regulated at the transcriptional and post-transcriptional
RT level.";
RL Mol. Microbiol. 32:169-178(1999).
RN [5]
RP FUNCTION, AND INTERACTION WITH CREC.
RX PubMed=11918805; DOI=10.1046/j.1365-2958.2002.02811.x;
RA Lockington R.A., Kelly J.M.;
RT "The WD40-repeat protein CreC interacts with and stabilizes the
RT deubiquitinating enzyme CreB in vivo in Aspergillus nidulans.";
RL Mol. Microbiol. 43:1173-1182(2002).
RN [6]
RP FUNCTION.
RX PubMed=12750323; DOI=10.1093/genetics/164.1.95;
RA Boase N.A., Lockington R.A., Adams J.R., Rodbourn L., Kelly J.M.;
RT "Molecular characterization and analysis of the acrB gene of Aspergillus
RT nidulans: a gene identified by genetic interaction as a component of the
RT regulatory network that includes the CreB deubiquitination enzyme.";
RL Genetics 164:95-104(2003).
RN [7]
RP FUNCTION.
RX PubMed=18512059; DOI=10.1007/s00294-008-0198-6;
RA Katz M.E., Bernardo S.M., Cheetham B.F.;
RT "The interaction of induction, repression and starvation in the regulation
RT of extracellular proteases in Aspergillus nidulans: evidence for a role for
RT CreA in the response to carbon starvation.";
RL Curr. Genet. 54:47-55(2008).
RN [8]
RP INTERACTION WITH CREA AND QUTD, AND FUNCTION.
RA Kamlangdee N.;
RT "Identifying target proteins of the CreB deubiquitination enzyme in the
RT fungus Aspergillus nidulans.";
RL Thesis (2008), University of Adelaide, Australia.
CC -!- FUNCTION: Ubiquitin thioesterase component of the regulatory network
CC controlling carbon source utilization through ubiquitination and
CC deubiquitination involving creA, creB, creC, creD and acrB.
CC Deubiquitinates the creA catabolic repressor and the quinate permease
CC qutD. Also plays a role in response to carbon starvation and the
CC control of extracellular proteases activity.
CC {ECO:0000269|PubMed:10216870, ECO:0000269|PubMed:11442830,
CC ECO:0000269|PubMed:11918805, ECO:0000269|PubMed:12750323,
CC ECO:0000269|PubMed:18512059, ECO:0000269|Ref.8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- SUBUNIT: Interacts with creA, creC and qutD.
CC {ECO:0000269|PubMed:11918805, ECO:0000269|Ref.8}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF327414; AAL04454.1; -; Genomic_DNA.
DR EMBL; AACD01000061; EAA59795.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF75829.1; -; Genomic_DNA.
DR RefSeq; XP_661191.1; XM_656099.1.
DR AlphaFoldDB; Q96V54; -.
DR SMR; Q96V54; -.
DR STRING; 162425.CADANIAP00005157; -.
DR EnsemblFungi; CBF75829; CBF75829; ANIA_03587.
DR EnsemblFungi; EAA59795; EAA59795; AN3587.2.
DR GeneID; 2873003; -.
DR KEGG; ani:AN3587.2; -.
DR VEuPathDB; FungiDB:AN3587; -.
DR eggNOG; KOG1864; Eukaryota.
DR HOGENOM; CLU_008279_0_1_1; -.
DR InParanoid; Q96V54; -.
DR OMA; HRVVYPF; -.
DR OrthoDB; 378361at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0045013; P:carbon catabolite repression of transcription; IMP:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..766
FT /note="Ubiquitin carboxyl-terminal hydrolase creB"
FT /id="PRO_0000395684"
FT DOMAIN 55..466
FT /note="USP"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..620
FT /evidence="ECO:0000255"
FT COMPBIAS 247..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 64
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 766 AA; 86229 MW; A29EC2B530092896 CRC64;
MGSFLKSFRK DVGSAAPSVG APPAKKEPQP LPMTPLEKML TELGPIRGDG SDKFYGMENF
GNTCYCNSIL QCLYYSVPFR EAVLNYPKRT PIEDLEAALA KALRYQDPNA RLEAEALAEK
QKAANSPRPG QPPNPQQKPE DKDSPEYKKK LALQTLPLLE TTDNSVSYGI PESLFSSLKD
MFESIVGSQS RIGIIRPQHF LEVLRRENEM FRTAMHQDAH EFLNLLLNEV VVDVEKAAAK
LLESPQPASD VSDSVIPSSS SGSRTPNTTR WVHELFEGLL TSETQCLTCE KASQRDEVFL
DLSVDLEQHS SVTSCLRKFS AEEMLCERNK FHCDNCGGLQ EAEKRMKIKR LPRILALHLK
RFKYTEDLQR LQKLFHRVVY PYHLRLFNTT DDAEDPDRLY ELYAVVVHIG GGPYHGHYVS
IIKTQDRGWL LFDDEMVEPV DKNYVRNFFG DKPGLACAYV LFYQETTMEA VMKEQEQENT
EPPVEVNAST LKQNGFSSSA TLAHAHSASQ VPTYEDHDRF TGLKRAPTAP QLSTHPEHTT
TDSESLPSPA PDPAPLTSLP PIPPIPETPP APLTSRKSDL QSKKERVKEE KERKAAEKEK
EKQRRKEIET RLKDRQRRED DDLKAALEAS KVSKEDEDRR NHAENGTSKK NAGGLGRFRS
LSQRLSTKES RTSLSRIPPL PNGNHTLSKV PDESEQTHPK SPTPPAPLSR PASQPLNDDL
LGSPRADTLA VPTEQEHIKN SKHDRSSHGK WRSFSLRKKS FNILSS
