CREB_ASPNC
ID CREB_ASPNC Reviewed; 758 AA.
AC A2Q9N1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable 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; ORFNames=An01g08470;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 (By similarity).
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK43937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM269976; CAK43937.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001389270.2; XM_001389233.2.
DR AlphaFoldDB; A2Q9N1; -.
DR SMR; A2Q9N1; -.
DR PaxDb; A2Q9N1; -.
DR PRIDE; A2Q9N1; -.
DR EnsemblFungi; CAK43937; CAK43937; An01g08470.
DR GeneID; 4978128; -.
DR KEGG; ang:ANI_1_1130014; -.
DR VEuPathDB; FungiDB:An01g08470; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0045013; P:carbon catabolite repression of transcription; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS: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 3: Inferred from homology;
KW Coiled coil; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..758
FT /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT /id="PRO_0000395681"
FT DOMAIN 57..468
FT /note="USP"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..631
FT /evidence="ECO:0000255"
FT COMPBIAS 249..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 758 AA; 84902 MW; 66D526B4DA07ED6D CRC64;
MGSFLRSFRR DVGSSTPSVG ATPAKKEPLA LPITPLEKML QEMGSDSVRQ DGSDKFFGME
NYGNTCYCNS ILQCLYYSVP FREAVLNYPT RTPIESLEAA LAKNLRYQNF AANQEAEAQA
EKQRLANAQR PGAPPAQPPK PEDKDSSEYK KKIALQSLPL LETKNNAGSY GMSESLFTSL
KDIFESVVAS QSRIGIVRPQ HFLDVLRREN EMFRSAMHQD AHEFLNLVLN EVVANVEAEA
MKQPIPSLPP ADTTDSSRQS ISSGSKTPNT TRWVHELFEG TLTSETQCLT CENVSQRDEI
FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI KRLPRILALH
LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR LYELYAVVVH IGGGPYHGHY
VSIIKTQDRG WLLFDDEMVE PVDKNYVRNF FGDKPGLACA YVLFYQETTL EAVLKEQEME
NMNASAADAN EAAVKPNGFP QPAGLAHVHS ASQIPVQDEP QRHTGLRRAP TAPQLPTHTE
YPGPDIEPSS PAVATPPPVP PIPETANRPL SPKKSDIQSK KERAKEEKER KAAEKEMEKQ
RRKEQEARVK ENQRREEAEL KAALEASKAS KADEDRRNPT ENGKDGDPKR SSNGLSRLKR
GSKSFSQRLG KDKESRASSS GLPSVPSAEP LTPNPVPLEP VQQLSPRKAS PPKESHVVHK
PLGQDDEPDA LKSPKGDRAG HGKWRSFSIR KKSFSILS
