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   27-MAR-2024, entry version 107.
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; 227321.Q96V54; -.
DR   EnsemblFungi; CBF75829; CBF75829; ANIA_03587.
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; PVLQMDY; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
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:0045013; P:carbon catabolite repression of transcription; IMP:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   CDD; cd02663; Peptidase_C19G; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR24006:SF944; RE52890P; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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
//