ID   CALYP_DROAN             Reviewed;         470 AA.
AC   B3MIV9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-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=GF12763;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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; CH902619; EDV36019.1; -; Genomic_DNA.
DR   RefSeq; XP_001959197.2; XM_001959161.2.
DR   AlphaFoldDB; B3MIV9; -.
DR   SMR; B3MIV9; -.
DR   STRING; 7217.FBpp0115955; -.
DR   MEROPS; C12.A09; -.
DR   EnsemblMetazoa; FBtr0117463; FBpp0115955; FBgn0089797.
DR   GeneID; 6495610; -.
DR   KEGG; dan:6495610; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_2_1_1; -.
DR   InParanoid; B3MIV9; -.
DR   OMA; IAINEQH; -.
DR   OrthoDB; 1363547at2759; -.
DR   PhylomeDB; B3MIV9; -.
DR   Proteomes; UP000007801; 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: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..470
FT                   /note="Ubiquitin carboxyl-terminal hydrolase calypso"
FT                   /id="PRO_0000395826"
FT   REGION          305..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..470
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            226
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   470 AA;  51537 MW;  001BABA110687CE3 CRC64;
     MNMTGGGAGP QAGPNSSCNI PNSSLLATAP VAATMPIAQL ADGWLELESD PGLFTLLLED
     FGCHDVQVEE VYDLQKPIES PYGFIFLFRW IEERRARRKI VETTAEIFVK DEEAISSIFF
     AQQVVPNSCA THALLSVLLN CNENNLQLGD TLSRLKAHTK GMSPENKGLA IGNTPELACA
     HNSHAMPQAR RRLERTGAGV SSCRFTGEAF HFVSFVPING QLFELDGLKP YPMNHGGWED
     HEDWTDKFRR VMTERLGIAT GEQDIRFNLM AVVPDRRIAI THKLKMLRTN QAIVSGTLQK
     LLKADEQGEG GNGDPQRPDT PSTLLEPSAF TARDLQSLLK NLDTEIAINE QHLADENDRR
     HKFKVDASRR THNYDKFICT FLSMLAHQGV LGELVSQHLL PSKKISGQSA ANRLNKQSNA
     TANAGATAAG AAGAAPKSQQ QQAAAAKNGK SPSKTPGRRR KGRNKCKKRK