ID   CALYP_DROVI             Reviewed;         462 AA.
AC   B4LQ24;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso;
DE            EC=3.4.19.12;
DE   AltName: Full=BAP1 homolog;
GN   Name=calypso; ORFNames=GJ20906;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
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; CH940648; EDW60347.1; -; Genomic_DNA.
DR   RefSeq; XP_002049154.1; XM_002049118.2.
DR   AlphaFoldDB; B4LQ24; -.
DR   SMR; B4LQ24; -.
DR   STRING; 7244.FBpp0235323; -.
DR   MEROPS; C12.A09; -.
DR   EnsemblMetazoa; FBtr0236831; FBpp0235323; FBgn0208042.
DR   GeneID; 6626878; -.
DR   KEGG; dvi:6626878; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_2_1_1; -.
DR   InParanoid; B4LQ24; -.
DR   OMA; IAINEQH; -.
DR   OrthoDB; 1363547at2759; -.
DR   PhylomeDB; B4LQ24; -.
DR   Proteomes; UP000008792; 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..462
FT                   /note="Ubiquitin carboxyl-terminal hydrolase calypso"
FT                   /id="PRO_0000395834"
FT   REGION          394..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..462
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   462 AA;  51378 MW;  8B4F7B38F50D8F2E CRC64;
     MNVAGGGTGT TAGSAGNNNT LPMAQLADGW LELESDPGLF TLLLEDFGCH DVQVEEVYDL
     QKPIESPYGF IFLFRWIEER RARRKIVETT AEIFVKDEEA ISSIFFAQQV VPNSCATHAL
     LSVLLNCNEN NLQLGETLSR LKAHTKGMSP ENKGLAIGNT PELACAHNSH AMPQARRRLE
     RTGAGVASCR FTGEAFHFVS FVPINGQLFE LDGLKPYPMN HGCWEEHEDW TDKFRRVMAE
     RLGIATGEQD IRFNLMAVVP DRRIAITHKL KMLRTNQAIV SGTLQKLLKA DEQGERDEQQ
     RPDTPNTLLE PSAFTARDLQ SLLKNLDTEI AINEQHLADE NDRRQMFKVD ASRRTHNYDK
     FICTFLTMLA HQGVLGELVS QHLLPSKKIS GQSAANRLNK QNSAAASTAN SSAGATAGGA
     KSQQQQQQQQ QPQQPQTPKN GKSPGKTPGR RRKGRNKCRK RK