ID   CREB_NEOFI              Reviewed;         761 AA.
AC   A1CW53;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   27-MAR-2024, entry version 73.
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=NFIA_103430;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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=EAW24855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027685; EAW24855.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001266752.1; XM_001266751.1.
DR   AlphaFoldDB; A1CW53; -.
DR   SMR; A1CW53; -.
DR   STRING; 331117.A1CW53; -.
DR   EnsemblFungi; EAW24855; EAW24855; NFIA_103430.
DR   GeneID; 4593253; -.
DR   KEGG; nfi:NFIA_103430; -.
DR   VEuPathDB; FungiDB:NFIA_103430; -.
DR   eggNOG; KOG1864; Eukaryota.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000006702; 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: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..761
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase creB"
FT                   /id="PRO_0000395685"
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          242..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          577..640
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..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..654
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..747
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   761 AA;  85840 MW;  1FD8CFA3FCDC6666 CRC64;
     MGSFLRSFRH NGGSTAPSVG AVPAKKEPQP PPMTPLEKRL LDMGPIREDG SDKFYGMENY
     GNTCYCNSIL QCLYYSVPFR EAVINYPTRT PIESLEAALA KSLRYPNPNA QLEAEAQAEK
     QKAANAQRPG MPPNPQQKPE DKDSPEYKKK MALQTLPLLE TQNNAASYGM SESLFTSLKD
     IFESVVGSQS RIGIIRPQQF LEVLRRDHEM FRTAMHQDAH EFLNLLLNEV VANVEAEASK
     QPLMEKSLPA 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
     EHGDPESTPF SPLSPLSPVP PVPPIPERVA TVATPPKNDA LAKREEKERK AAEKEKEKAE
     KLRRKEQGAR MKENQRREEA ELKAALEMSK ASKAEEDRRL STENGKEKQG GGLSRLKRGS
     KSLSHRLGKD KETRSVSSDL PPVPIPEHST LSQSGPTSEQ QQQQRQQSPP NHDQPPNSPQ
     PGKPTIREDE QVNHKDSKHE RTGHGKWRSF SLRKKSFSIL S
//