ID   A0A0S7E052_9EURO        Unreviewed;       316 AA.
AC   A0A0S7E052;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
GN   ORFNames=ALT_001929 {ECO:0000313|EMBL:GIM42331.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM42331.1};
RN   [1] {ECO:0000313|EMBL:GIM42331.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM42331.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
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|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|PIRNR:PIRNR038120,
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:GIM42331.1}.
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DR   EMBL; BCLY01000016; GIM42331.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7E052; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_7886; -.
DR   OrthoDB; 276003at2759; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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   InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR   InterPro; IPR041507; UCH_C.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038120};
KW   Protease {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR038120,
KW   ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR038120}.
FT   DOMAIN          7..221
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
FT   DOMAIN          251..285
FT                   /note="Peptidase C12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18031"
FT   ACT_SITE        93
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   SITE            191
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ   SEQUENCE   316 AA;  35470 MW;  58B0D28EA16ADFB7 CRC64;
     MADGGGWSTI ESDEGVFTSL IENLGVKDVQ FEELISLDAD TIRSLSPVYG VIFLFKWIRE
     PPSTNTTQPL DGTYITSLPE NLFFAAQTIQ NACGTQAILS VILNQDSPAS TPYPINIGPE
     LRSFKDFTTG FPPDLRGEAL SNSETIRTAH NAFARASPFV DETVRTAQDE EADVYHFIAY
     TPVNGVLYEL DGLQPYPISH GECVAETFPE KVIAVLQRRI ARYPEGETRF NLMAVVRDLR
     VRARETGDVE LLEREARKRR AWAWENTLRR WNFVGFIGEM VKGVAGMKEK EGPGAYEAWV
     EKAKQETQKR LLSRRG
//