CREB_ASPFN
ID CREB_ASPFN Reviewed; 755 AA.
AC B8NSV5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=AFLA_051480;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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}.
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DR EMBL; EQ963483; EED47094.1; -; Genomic_DNA.
DR RefSeq; XP_002383274.1; XM_002383233.1.
DR AlphaFoldDB; B8NSV5; -.
DR SMR; B8NSV5; -.
DR STRING; 5059.CADAFLAP00011139; -.
DR PRIDE; B8NSV5; -.
DR EnsemblFungi; EED47094; EED47094; AFLA_051480.
DR VEuPathDB; FungiDB:AFLA_051480; -.
DR eggNOG; KOG1864; Eukaryota.
DR HOGENOM; CLU_008279_0_2_1; -.
DR OMA; HRVVYPF; -.
DR Proteomes; UP000001875; 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: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; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..755
FT /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT /id="PRO_0000395679"
FT DOMAIN 55..468
FT /note="USP"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 581..630
FT /evidence="ECO:0000255"
FT COMPBIAS 253..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..740
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 755 AA; 85064 MW; FA0FB9C8256630C4 CRC64;
MGSFLRSLRR DVGPPTPSVG ATPAKKEPPV PPVTPLEKML QDMGAIREDG SDKFFGMENY
GNTCYCNSIL QCLYYSVPFR EAVVNYPTRT PIESLEAALA NTLRYQNFAA NLEAEALAEK
QKAANAQRPG APPNQPQKPE DKDSPEYKKK MALQTLPLLE TKNNATSYGM SESLFTSLKD
LFESVVASQS RIGIIRPQHF LDVLRREHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK
QPEPERSLPP AESADSTELS GSSGSKTPNT TRWVHELFEG TLTSETQCLT CEKVSQRDEV
FLDLSVDLEQ HSSVTSCLRK FSAEEMLCER NKFHCDNCGG LQEAEKRMKI KRLPRILALH
LKRFKYTEDL QRLQKLFHRV VYPYHLRLFN TTDDAEDPDR LYELYAVVVH IGGGPYHGHY
VAIIKTQDRG WLLFDDEMVE PVDKNYVRNF FGDRPGLACA YVLFYQETTL EAVMKEQEQE
NMDLNTSVAD INDSTLKQNG YPLSPGLAHV HSASQIPSPS EPARFSNLQR APTAPPLFPH
PEHADSESSP ADPSTTASAT PPVPPIPDIH SLPLSPKKSD SHFKKERAKE EKERKANEKE
KEKQRRRDQE ARIREQRRED AEIRAALEAS KASKAEEDRR HSPDDTKKSS HGLSRLKRGS
KSFSHRLGKD KENRVSSSSH SATPIAEHPP SRNGASESQQ QLPNGQSPGS HGLHTRHTGL
DEERDTLKDP KHDRSGHHGK WRSFSLKKKS FSILS
