ID   CALYP_DROPE             Reviewed;         475 AA.
AC   B4GAM2;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso;
DE            EC=3.4.19.12;
DE   AltName: Full=BAP1 homolog;
GN   Name=calypso; ORFNames=GL10684;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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 (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- SUBUNIT: Component of the PR-DUB complex, at least composed of calypso
CC       and Asx. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to PcG
CC       response elements (PREs). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH479181; EDW31974.1; -; Genomic_DNA.
DR   RefSeq; XP_002016084.1; XM_002016048.1.
DR   AlphaFoldDB; B4GAM2; -.
DR   SMR; B4GAM2; -.
DR   STRING; 7234.FBpp0174791; -.
DR   MEROPS; C12.A09; -.
DR   EnsemblMetazoa; FBtr0176299; FBpp0174791; FBgn0148294.
DR   GeneID; 6590516; -.
DR   KEGG; dpe:6590516; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_2_1_1; -.
DR   OMA; IAINEQH; -.
DR   PhylomeDB; B4GAM2; -.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0035517; C:PR-DUB complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR   GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR   GO; GO:0007385; P:specification of segmental identity, abdomen; IEA:EnsemblMetazoa.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.532.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   InterPro; IPR041507; UCH_C.
DR   PANTHER; PTHR10589; PTHR10589; 2.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Hydrolase; Nucleus; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..475
FT                   /note="Ubiquitin carboxyl-terminal hydrolase calypso"
FT                   /id="PRO_0000395830"
FT   REGION          411..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..475
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            227
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   475 AA;  52100 MW;  02746ECD4125FDD8 CRC64;
     MNVAAGGPGT ASASTTAANS IFNNSLLASA TGATTMPMAQ LADGWLELES DPGLFTLLLE
     DFGCHDVQVE EVYDLQKPIE SPYGFIFLFR WIEERRARRK IVETTAEIFV KDEEAISSIF
     FAQQVVPNSC ATHALLSVLL NCNENNLQLG DTLSRLKVHT KGMSPENKGL AIGNTPELAC
     AHNSHAIPQA RRRLERTGAG VASCRFTGEA FHFVSFVPIS GQLFELDGLK PYPMNHGGWE
     DHEDWTDKFR RVMAERLGIA TGEQDIRFNL MAVVPDRRIA ITHKLKMLRT NQAIVSGTLQ
     KLLKADEQGE SGNGDQQRPD TPTTLLEPSA FTAKDLQLLL KNLDTEIAIN EQNLADENDR
     RHMFKVDASR RTHNYDKFIC TFLSMLAHQG VLGELVSQHL LPSKKVSGQS AANRISKQNS
     AASSAGANAG AAAGVTPKSQ QQQQQPQTAA SKNGKSPGKT PGRRRKGRNK CRKRK