ID   CALYP_CULQU             Reviewed;         470 AA.
AC   B0W2R4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso;
DE            EC=3.4.19.12;
DE   AltName: Full=BAP1 homolog;
GN   Name=calypso; ORFNames=CPIJ001439;
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB;
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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) (By
CC       similarity). {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. {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; DS231828; EDS29817.1; -; Genomic_DNA.
DR   RefSeq; XP_001842998.1; XM_001842946.1.
DR   AlphaFoldDB; B0W2R4; -.
DR   SMR; B0W2R4; -.
DR   STRING; 7176.CPIJ001439-PA; -.
DR   MEROPS; C12.A09; -.
DR   GeneID; 6032393; -.
DR   KEGG; cqu:CpipJ_CPIJ001439; -.
DR   VEuPathDB; VectorBase:CPIJ001439; -.
DR   VEuPathDB; VectorBase:CQUJHB016383; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_2_1_1; -.
DR   InParanoid; B0W2R4; -.
DR   OMA; IAINEQH; -.
DR   OrthoDB; 1363547at2759; -.
DR   PhylomeDB; B0W2R4; -.
DR   Proteomes; UP000002320; Partially assembled 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_0000395825"
FT   REGION          423..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..470
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        98
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            192
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   470 AA;  53180 MW;  D894D640FC6CCBE8 CRC64;
     MPVDINRLTD GWLELESDPG LFTLLLEDFG VKGVQVEEIY DLQKTIEGPV FGFIFLFRWI
     EERRARRKIV ETTTEMYVKD EEAVNSIFFA HQVVPNSCAT HALLSVLLNC SDIDLGTTLS
     RLKVHTKGMC PDNKGWAIGN TPELACAHNS HAMPQARRRM DRNSGVSTGR FTGEAFHFVS
     FCPINGHLFE LDGLKPFPMD HGPWGEKEDW TDKFRRVMSD RLGISTDRRI AITHKLKMLR
     TNQTIVSAAL EKLLKSKQLE SRSQAEIRET VDKIKKEEQE STVKLSSEYS QLLEMHEKDE
     PAVAMSKELE SLVSLNSSSD SVEIIGETEI KKENPPPSPP PAFIGAGTFS PKDLLSLLKN
     LESEINITEQ HLCDENEKRA MFKVDDCRRT HNYDEFICTF LSMLAYQGEL GDLVTQHLVT
     SRKPSLGGVQ NSGSRGVVRN YNKKSTTNGS SPKTPSSKRR RGRTKYRKRK