ID   A0A0A1U0G2_ENTIV        Unreviewed;       308 AA.
AC   A0A0A1U0G2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=EIN_096240 {ECO:0000313|EMBL:ELP87367.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP87367.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP87367.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP87367.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) 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|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   ---------------------------------------------------------------------------
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; KB206860; ELP87367.1; -; Genomic_DNA.
DR   RefSeq; XP_004254138.1; XM_004254090.1.
DR   AlphaFoldDB; A0A0A1U0G2; -.
DR   EnsemblProtists; ELP87367; ELP87367; EIN_096240.
DR   GeneID; 14886303; -.
DR   KEGG; eiv:EIN_096240; -.
DR   VEuPathDB; AmoebaDB:EIN_096240; -.
DR   OrthoDB; 276003at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
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   Gene3D; 1.20.58.860; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000014680};
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          6..206
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
FT   DOMAIN          252..294
FT                   /note="Peptidase C12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18031"
FT   ACT_SITE        91
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   ACT_SITE        168
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   SITE            183
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ   SEQUENCE   308 AA;  35031 MW;  ED40A73057F58A4A CRC64;
     MSTFNWNTIE SDPGIFTEMV EKLGCPNIQF KELYSLDDIE TLDRIKPIEG IVLLFEYDKR
     ALTYFQSEFC GIDTKEYPDL FFAKQVVNNA CATQAILSVL LNLKTIDVGS TLQQFKESAM
     KLSPYDRGVA IGKSDIIRKT HNEFAQPSQA LQERISNKFS GVTGKAHHFI GIIPYNGILL
     MLDGLSEDPI VIGGAEDDWV TTGVKPFFEG LCKALSGSLD FTILAVVHNQ VNKYKELYER
     AVEEKSDMAT TYKSMFEEEI QKRKKEREEN TRRKHDYMPL ALHVLLLMGK YGKLEQQVTR
     AEEEAQKS
//