ID   CREB_ASPOR              Reviewed;         754 AA.
AC   Q2UUG8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   03-AUG-2022, entry version 68.
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=AO090009000320;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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=BAE54797.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007150; BAE54797.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2UUG8; -.
DR   SMR; Q2UUG8; -.
DR   STRING; 510516.Q2UUG8; -.
DR   Proteomes; UP000006564; Chromosome 1.
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..754
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT                   /id="PRO_0000395682"
FT   DOMAIN          54..467
FT                   /note="USP"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          580..629
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        252..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        63
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        418
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   754 AA;  84965 MW;  5C2FE319F4111992 CRC64;
     MGSFLRSLRR DGPPTPSVGA TPAKKEPPVP PVTPLEKMLQ DMGAIREDGS DKFFGMENYG
     NTCYCNSILQ CLYYSVPFRE AVVNYPTRTP IESLEAALAN TLRYQNFAAN LEAEALAEKQ
     KAANAQRPGA PPNQPQKPED KDSPEYKKKM ALQTLPLLET KNNATSYGMS ESLFTSLKDL
     FESVVASQSR IGIIRPQHFL DVLRREHEMF RTAMHQDAHE FLNLLLNEVV ANVEAEASKQ
     PEPERSLPPA ESADSTELSG SSGSKTPNTT RWVHELFEGT LTSETQCLTC EKVSQRDEVF
     LDLSVDLEQH SSVTSCLRKF SAEEMLCERN KFHCDNCGGL QEAEKRMKIK RLPRILALHL
     KRFKYTEDLQ RLQKLFHRVV YPYHLRLFNT TDDAEDPDRL YELYAVVVHI GGGPYHGHYV
     AIIKTQDRGW LLFDDEMVEP VDKNYVRNFF GDRPGLACAY VLFYQETTLE AVMKEQEQEN
     MDLNTSVADI NDSTLKQNGY PLSPGLAHVH SASQIPSPSE PARFSNLQRA PTAPPLFPHP
     EHADSESSPA DPSTTASATP PVPPIPDIHS LPLSPKKSDS HFKKERAKEE KERKANEKEK
     EKQRRRDQEA RIREQRREDA EIRAALEASK ASKAEEDRRH SPDDTKKSSH GLSRLKRGSK
     SFSHRLGKDK ENRVSSSSHS ATPIAEHPPS RNGASESQQQ LPNGQSPGSH GLHTRHTGLD
     EERDTLKDPK HDRSGHHGKW RSFSLKKKSF SILS