CREB_ASPFC
ID CREB_ASPFC Reviewed; 767 AA.
AC B0Y4P5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=AFUB_069810;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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}.
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DR EMBL; DS499598; EDP50644.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y4P5; -.
DR SMR; B0Y4P5; -.
DR EnsemblFungi; EDP50644; EDP50644; AFUB_069810.
DR HOGENOM; CLU_008279_0_2_1; -.
DR PhylomeDB; B0Y4P5; -.
DR Proteomes; UP000001699; 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..767
FT /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT /id="PRO_0000395678"
FT DOMAIN 49..462
FT /note="USP"
FT REGION 107..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 574..641
FT /evidence="ECO:0000255"
FT COMPBIAS 247..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 413
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 767 AA; 86762 MW; EFF2CE02A19E94D6 CRC64;
MFCLLLGSTA PSVGAVPAKK EPQPPPMTPL EKRLLDMGPI REDGSDKFYG MENYGNTCYC
NSILQCLYYS VPFREAVINY PTRTPIESLE AALAKSLRYP NPNAQLEAEA QAEKQKAANA
QRPGMPPNPQ QKPEDKDSPE YKKKMALQTL PLLETQNNAS SYGMSESLFT SLKDIFESVV
GSQSRIGIIR PQQFLEVLRR DHEMFRTAMH QDAHEFLNLL LNEVVANVEA EASKQPPIEK
SLPAPETADS VDQSSSTGSK TPNTTRWVHE LFEGLLTSET QCLTCEKVSQ RDEVFLDLSV
DLEQHSSVTS CLRKFSAEEM LCERNKFHCD NCGGLQEAEK RMKIKRLPRI LALHLKRFKY
TEDLQRLQKL FHRVVYPYHL RLFNTTDDAE DPDRLYELYA VVVHIGGGPY HGHYVAIIKT
EDRGWLLFDD EMVEPVDKNY VKNFFGDKPG LACAYVLFYQ ETTLEAVLKE QEQENMDSNL
AATDANDTIL KQNGFPQSPL AHVHSASQIP SHEDNLRPNG LRRAPTAPQL STHHEHGDPE
SAPFSPLSPL SPLSQTPPVP PVPERVTTVA TPPKNDALAK KERAREEKER KAAEKEREKA
EKLRRKEQEA RMKENQRREE AELKAALEMS KASKAEEDRR LSHENGKEKQ GGSLSRLKRG
SKSLSHRLGK DKETRSVSSD LPPVPIPEHS TLSQTGPTSE QQQQQQQQQQ QQQSPPNHDQ
PPNSPQLGKP TIREDEQVNH KDSKHERTGH GKWRSFSLRK KSFSILS
