ID   CREB_ASPTN              Reviewed;         768 AA.
AC   Q0CT11;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   27-MAR-2024, entry version 64.
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=ATEG_03173;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU36447.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476597; EAU36447.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001212351.1; XM_001212351.1.
DR   AlphaFoldDB; Q0CT11; -.
DR   SMR; Q0CT11; -.
DR   STRING; 341663.Q0CT11; -.
DR   GeneID; 4317779; -.
DR   eggNOG; KOG1864; Eukaryota.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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:0006511; P:ubiquitin-dependent protein catabolic process; ISS: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   3: Inferred from homology;
KW   Coiled coil; Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..768
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT                   /id="PRO_0000395683"
FT   DOMAIN          55..468
FT                   /note="USP"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          574..633
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        247..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..568
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..754
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        419
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   768 AA;  86786 MW;  8ED13742A82E7656 CRC64;
     MGSLFRSFRR DAGATAPSVG ATPAKKEPPP PPMTPLEKML QDMGAIREDG SDKFFGMENY
     GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLTAALA ETLRYPNPNA HLEAEAQAEK
     QKAANAQRPG APPNQPQKPE DKDSPEYKKK MALQTFPLLE TKNNAPSYGM SESLFTSLKD
     LFESVVGSQS RIGIVRPQHF LDVLRREHEM FRTAMHQDAH EFLNLLLNEV VANVEAEALK
     QPSLERSLPP AESSESVEHS GSSGSKTPNT TRWVHELFEG TLTSETQCLT CEKVSQRDEV
     FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI KRLPRILALH
     LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR LYELYAVVVH IGGGPYHGHY
     VAIIKTQDRG WLLFDDEMVE PVDKNYVRNF FGDKPGLACA YVLFYQETTL EAVLREQEQE
     NMDPALATTE TNDSLKQNGF AQSPALGLVH SASQIPSHDE PHRLNSLKRA PTAPSLPTHY
     EHTDTNSAPS IPKPAMAPPV PPIPETHSMP LSPKKSDLQS RKERAKEEKE RKAAEKERER
     QRRKEQEATR KEQEARAREN QRREDAELKA ALEASRASKA DEDRRNQEGQ KDRDPGRSGH
     GLSRLKRGSK SFSHRLSKDK DTRVPSSSNP GVPDPNSPPL NNTVVTSEHQ EQEQQPPSDQ
     QPGASRLSKK HNLNDEERDA NKDPKQDKPG HGKWRSFSLR KKSLGILS
//