CREB_ASPCL
ID CREB_ASPCL Reviewed; 760 AA.
AC A1CIL1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 67.
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=ACLA_051880;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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=EAW10716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS027054; EAW10716.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001272142.1; XM_001272141.1.
DR AlphaFoldDB; A1CIL1; -.
DR SMR; A1CIL1; -.
DR STRING; 5057.CADACLAP00004413; -.
DR EnsemblFungi; EAW10716; EAW10716; ACLA_051880.
DR GeneID; 4703625; -.
DR KEGG; act:ACLA_051880; -.
DR eggNOG; KOG1864; Eukaryota.
DR OrthoDB; 378361at2759; -.
DR Proteomes; UP000006701; 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; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..760
FT /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT /id="PRO_0000395677"
FT DOMAIN 55..469
FT /note="USP"
FT REGION 1..28
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 520..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 575..635
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..746
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 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 760 AA; 85580 MW; 6C4CD500504810F8 CRC64;
MGSFLRSFRN NAGSTTPSVG AVPAKKEVPI PPMTPLEKRL LDMGSIRGDG SDKFYGMENY
GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLEAALA KSLRYPNPNA HLEAEAQAEK
QRAANAQRPG MPPAQPQKPE DKDSPDYKKK MALQTLPLLE AQNNATSYGM SESLFTSLKD
IFESVVGSQS RIGIVRPQQF LDVLRRDHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK
QPAAIEKSLP APDHAETVDQ SASSGSKTPN TTRWVHELFE GTLTSETQCL TCEKVSQRDE
IFLDLSVDLE QHSSVTSCLR KFSAEEMLCE RNKFHCDNCG GLQEAEKRMK IKRLPRILAL
HLKRFKYTED LQRLQKLFHR VVYPYHLRLF NTTDDAEDPD RLYELYAVVV HIGGGPYHGH
YVAIIKTEDR GWLLFDDELV EPVDKNYVRN FFGDKPGLAC AYVLFYQETT LEAVMKEQEQ
ENMESNLSAT DTNEAALKPN GSSPSHLAHV HSASYIPSLE EHNRPNGLKR APTAPQLSTH
HEHGDPESGA FSPVTATPPV PPIPEHLSAA PIPPKSDVQG KKERAREEKE RKAAEKEREK
AEKLRRKEQE ARAKENQRRE EAELKAALEA SKASKAQEDR RQSPDHGKDK LGGGLSRLKR
GSKSFSQRLG KDKETRSVSS LEAPPLPIPG HPISRDGPIP EQHQQQPDPK DDPFQDSHHP
NKPMMKEDEQ ANHKDPKHER TGHGKWRSFS LRKKSFSILS
