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Database: UniProt
Entry: A0A0G2G6M2_9EURO
LinkDB: A0A0G2G6M2_9EURO
Original site: A0A0G2G6M2_9EURO 
ID   A0A0G2G6M2_9EURO        Unreviewed;       545 AA.
AC   A0A0G2G6M2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   AltName: Full=Carbon catabolite repression protein B {ECO:0000256|ARBA:ARBA00041962};
DE   AltName: Full=Deubiquitinating enzyme creB {ECO:0000256|ARBA:ARBA00042958};
DE   AltName: Full=Ubiquitin thioesterase creB {ECO:0000256|ARBA:ARBA00041772};
DE   AltName: Full=Ubiquitin-hydrolyzing enzyme creB {ECO:0000256|ARBA:ARBA00041870};
DE   AltName: Full=Ubiquitin-specific-processing protease creB {ECO:0000256|ARBA:ARBA00042086};
GN   ORFNames=UCRPC4_g04528 {ECO:0000313|EMBL:KKY19368.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY19368.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY19368.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY19368.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY19368.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY19368.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00037075}.
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; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC   -!- SUBUNIT: Interacts with creA, creC and qutD.
CC       {ECO:0000256|ARBA:ARBA00038752}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKY19368.1}.
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DR   EMBL; LCWF01000108; KKY19368.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2G6M2; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000053317; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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:SF733; RE52890P; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KKY19368.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317}.
FT   DOMAIN          1..311
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          39..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..443
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  61019 MW;  4E4B758AEE4E494F CRC64;
     MENFGNTCYC NSILQCLYYS APFRENVLNF PKRSTAESVN AAAAKATPRI PSPPPPNLSP
     GKKSPNPSAR NPGAPVTNPN QKPDEKDSAD YKKKQALFVG PVLNMSYGNA SGYGMQDSLF
     TSLKDIFEAV VVSQSRIGVR DEAFLDLSVD LDQHSSVTSC LRRFSEEEML CERNKFHCDN
     CGGLQEAEKR MKIKRLPKIL ALHLKRFKYT EDLQRLQKLF HKVVYPYHLR LFNTTDDAED
     PDRLYELYAV VVHIGGGPYH GHYVSIIKTE DRGWLLFDDE LVEPVDKSYV RNFFGDRPGL
     ACAYVLFYQE TTLEAVQKEQ EKEESWHGYD DPVSLGAHPH VNGDLQRIKS SPMPQTHDID
     PMEAALGNLD QVMTSPGTYR PDNYFQSAPQ LSHSVTSPGQ SKKEKAKEEK DKKAAEKERE
     KNEKQARKEA EIRQREALKK QEADLKAALA ASKVSKAEED RRVTSEAPSK ENATGGLSRF
     KRGSKSISTK LGSVVRSDKT SATASSEGSQ STHASETLEK DKKLSFGNRR KKSFVFGRST
     MDGDG
//
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