ID   CALYP_DROMO             Reviewed;         461 AA.
AC   B4KT51;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso;
DE            EC=3.4.19.12;
DE   AltName: Full=BAP1 homolog;
GN   Name=calypso; ORFNames=GI18963;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22;
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; CH933808; EDW09571.1; -; Genomic_DNA.
DR   RefSeq; XP_002005636.1; XM_002005600.2.
DR   AlphaFoldDB; B4KT51; -.
DR   SMR; B4KT51; -.
DR   STRING; 7230.FBpp0168180; -.
DR   MEROPS; C12.A09; -.
DR   EnsemblMetazoa; FBtr0169688; FBpp0168180; FBgn0141702.
DR   GeneID; 6579754; -.
DR   KEGG; dmo:Dmoj_GI18963; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_2_1_1; -.
DR   InParanoid; B4KT51; -.
DR   OMA; IAINEQH; -.
DR   OrthoDB; 1363547at2759; -.
DR   PhylomeDB; B4KT51; -.
DR   Proteomes; UP000009192; 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..461
FT                   /note="Ubiquitin carboxyl-terminal hydrolase calypso"
FT                   /id="PRO_0000395829"
FT   REGION          392..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..461
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            212
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  51195 MW;  12F6203BE0B33A9A CRC64;
     MNVAAGGTSA AAGSASNNNA LPMAQLADGW LELESDPGLF TLLLEDFGCH DVQVEEVYDL
     QKPIESPYGF IFLFRWIEER RARRKIVETT AEIFVKDEEA ISSIFFAQQV VPNSCATHAL
     LSVLLNCNEN NLQLGETLSR LKAHTKGMSP ENKGLAIGNT PELACAHNSH AMPQARRRLE
     RTGAGVASCR FTGEAFHFVS FVPINGQLFE LDGLKPYPMN HGCWEEHEDW TDKFRRVMAD
     RLGIATGEQD IRFNLMAVVP DRRIAITHKL KMLRTNQAIV SGTLQKLLKA DEQGDDQQRP
     DTPNTLLEPS AFTARDLQSL LKNLDTEIAI NEQHLADEND RRQMFKVDAS RRTHNYDKFI
     CTFLSMLAHQ GVLGELVSQH LLPTKKISGQ SAANRLSKQS SAATANTANS AANATAGKSQ
     PQQQQQQQQQ QPQSQAAKNG KSPGKTPGRR RKGRNKCRKR K