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}.
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; 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
//