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Database: UniProt
Entry: A0A0N4U0Z2_DRAME
LinkDB: A0A0N4U0Z2_DRAME
Original site: A0A0N4U0Z2_DRAME 
ID   A0A0N4U0Z2_DRAME        Unreviewed;       228 AA.
AC   A0A0N4U0Z2;
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=DME_LOCUS4600 {ECO:0000313|EMBL:VDN54627.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000024001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000024001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN54627.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UYYG01001150; VDN54627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4U0Z2; -.
DR   STRING; 318479.A0A0N4U0Z2; -.
DR   WBParaSite; DME_0000024001-mRNA-1; DME_0000024001-mRNA-1; DME_0000024001.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; 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; cd09616; Peptidase_C12_UCH_L1_L3; 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:SF48; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00140; UCH_1; 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:UP000274756};
KW   Thiol protease {ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU361215}.
FT   DOMAIN          90..106
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|PROSITE:PS00140"
SQ   SEQUENCE   228 AA;  25586 MW;  BD18C58FA5BF1335 CRC64;
     MTPSLKWIPL ESNPDVISNL MLKFGVEKDV ICVDVYGFDK ELLDMLPKPC YALILCFPEC
     QKVKEMMAAV YDDHVKSNGS IPENVFFMKQ KISNACGTFA LIHALANNKN KIDLGNGPFK
     KWLEKADRLE ADLRSDSLQE NAELAEAHEV CAVSGETNSE VEEVEHHFIS YVNCDGILYE
     MDSSRDFPRA CGPTNEENFL QDAGKVCKEL MLMMDSISFS ALAIVRKC
//
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