ID B4F524_DROME Unreviewed; 340 AA.
AC B4F524;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 Name=CG1950 {ECO:0000313|EMBL:CAQ53272.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAQ53272.1};
RN [1] {ECO:0000313|EMBL:CAQ53272.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZBMEL384 {ECO:0000313|EMBL:CAQ53272.1};
RX PubMed=18477586; DOI=10.1093/molbev/msn111;
RA Baines J.F., Sawyer S.A., Hartl D.L., Parsch J.;
RT "Effects of X-linkage and sex-biased gene expression on the rate of
RT adaptive protein evolution in Drosophila.";
RL Mol. Biol. Evol. 25:1639-1650(2008).
CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic component of the PR-
CC DUB complex, a complex that specifically mediates deubiquitination of
CC histone H2A monoubiquitinated at 'Lys-118' (H2AK118ub1). Does not
CC deubiquitinate monoubiquitinated histone H2B. Required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development. The PR-DUB complex has weak or no activity toward 'Lys-
CC 48'- and 'Lys-63'-linked polyubiquitin chains.
CC {ECO:0000256|ARBA:ARBA00025087}.
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}.
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DR EMBL; AM998910; CAQ53272.1; -; Genomic_DNA.
DR AlphaFoldDB; B4F524; -.
DR MEROPS; C12.A04; -.
DR HOGENOM; CLU_018316_0_1_1; -.
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; 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 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 25..224
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 269..314
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT SITE 193
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ SEQUENCE 340 AA; 39329 MW; 314C900A850E52B7 CRC64;
MDTENPGAAT VEELTTKEAI AANNWCLIES DPGVFTEMIS GFGCTGPEVE EIWSIKADAF
RHLEPIHGLI FLFKWLDDKP AGRVVTDRSD IFFARQVIPN ACATQALLCL LLNLQHEDID
LGQTLTDLRN LCQDLDPECR GHRLANEEKI RKVHNSFARP ELFVVEESTD FIEDDCYHFV
GFMPIKGKLF ELDGMHEGPI ELADIDQQQN WLDVVRPINE ARMERYSVGE IHFNLMALVS
DRQRCYERKI QMLVNLPSQL SHADRQAEIA NLRSHVRHEK EKKRRYRKEN IRRRHNYLPF
IVELLKQLGE TGQLMAICDK AKDRSYLCKP SKDTRDQQPQ
//
