ID A0A0M9VSU9_9HYPO Unreviewed; 513 AA.
AC A0A0M9VSU9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN ORFNames=ESCO_002614 {ECO:0000313|EMBL:KOS18083.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS18083.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS18083.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361215};
CC -!- SIMILARITY: Belongs to the peptidase C12 family.
CC {ECO:0000256|RuleBase:RU361215}.
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:KOS18083.1}.
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DR EMBL; LGSR01000022; KOS18083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9VSU9; -.
DR STRING; 150374.A0A0M9VSU9; -.
DR OrthoDB; 2714324at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW Protease {ECO:0000256|RuleBase:RU361215};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Thiol protease {ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU361215}.
FT DOMAIN 109..337
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 56411 MW; E318ED36A026CCB0 CRC64;
MASSQEQEPI AAVMSPGPRR STRVARLAAA TPAAAAASSA SPASNAQQAS GNSSRAASKE
ATPSSQGRRN PKRKASEAVG HADSRLPDEL LEEALRPLTA EDIRDWEGWV ELESEPAFFN
IILRDLGVKD VKAQEIFSID QASLDFLPRP VYGLIFLFQY GPGGDESEGD DDTGSLWFAN
QTTHNSCATV ALLNIVMNAG QVELGSELAA FKASTRDLGT ALRGHELSRN KFIRTIHNSF
TRRMDHLNAD LALEDEASSA ETAAAKRRAG RGRAKVLTTK GRKTPADEYG YHFIAYVPAD
GYVWELDGLK SKPRRIGVIE PQAAWTTIAR PRIEDRIIKY QGSELSFNLL ALCQSPLAMH
ARAIAQALAA LRRLEQQIAQ RPDLADPADP STDPSDEQES RRETHSFLSR SLDEQQLAEF
NLSGADVDSA PIPDCVPPEI SHLERSAVLG LRERLVVDAK SAMGEFRAER MSMEDDELRV
KGRRKDYGRS LHRWVRKLAE KNVLEEVIQH SCP
//
