ID   CREB_ASPFU              Reviewed;         775 AA.
AC   Q4WQI1;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 3.
DT   27-MAR-2024, entry version 85.
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=AFUA_4G12910;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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=EAL89503.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000005; EAL89503.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_751541.2; XM_746448.2.
DR   AlphaFoldDB; Q4WQI1; -.
DR   SMR; Q4WQI1; -.
DR   STRING; 330879.Q4WQI1; -.
DR   GeneID; 3509101; -.
DR   KEGG; afm:AFUA_4G12910; -.
DR   VEuPathDB; FungiDB:Afu4g12910; -.
DR   eggNOG; KOG1864; Eukaryota.
DR   HOGENOM; CLU_008279_0_2_1; -.
DR   InParanoid; Q4WQI1; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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; 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..775
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT                   /id="PRO_0000395680"
FT   DOMAIN          55..468
FT                   /note="USP"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          586..653
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        253..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..579
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..761
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   775 AA;  87513 MW;  035E52A005B5368A CRC64;
     MGSFLRSFRH NGGSTAPSVG AVPAKKEPQP PPMTPLEKRL LDMGPIREDG SDKFYGMENY
     GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLEAALA KSLRYPNPNA QLEAEAQAEK
     QKAANAQRPG MPPNPQQKPE DKDSPEYKKK MALQTLPLLE TQNNASSYGM SESLFTSLKD
     IFESVVGSQS RIGIIRPQQF LEVLRRDHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK
     QPPIEKSLPA PETADSVDQS SSTGSKTPNT TRWVHELFEG LLTSETQCLT CEKVSQRDEV
     FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI KRLPRILALH
     LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR LYELYAVVVH IGGGPYHGHY
     VAIIKTEDRG WLLFDDEMVE PVDKNYVKNF FGDKPGLACA YVLFYQETTL EAVLKEQEQE
     NMDSNLAATD ANDTILKQNG FPQSPLAHVH SASQIPSHED NLRPNGLRRA PTAPQLSTHH
     EHGDPESAPF SPLSPLSPLS PLSPLSQTPP VPPVPERVTT VATPPKNDAL AKKERAREEK
     ERKAAEKERE KAEKLRRKEQ EARMKENQRR EEAELKAALE MSKASKAEED RRLSHENGKE
     KQGGSLSRLK RGSKSLSHRL GKDKETRSVS SDLPPVPIPE HSTLSQTGPT SEQQQQQQQQ
     QSPPNHDQPP NSPQLGKPTI REDEQVNHKD SKHERTGHGK WRSFSLRKKS FSILS
//