ID   C1LIU0_SCHJA            Unreviewed;       933 AA.
AC   C1LIU0;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   Name=H34C03.2 {ECO:0000313|EMBL:CAX74618.1};
OS   Schistosoma japonicum (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6182 {ECO:0000313|EMBL:CAX74618.1};
RN   [1] {ECO:0000313|EMBL:CAX74618.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Anhui {ECO:0000313|EMBL:CAX74618.1};
RX   DOI=10.1038/nature08140;
RA   Liu F., Zhou Y., Wang Z.Q., Lu G., Zheng H., Brindley P.J., McManus D.P.,
RA   Blair D., Zhang Q.H., Zhong Y., Wang S., Han Z.G., Chen Z.;
RT   "The Schistosoma japonicum genome reveals features of host-parasite
RT   interplay.";
RL   Nature 460:345-351(2009).
RN   [2] {ECO:0000313|EMBL:CAX74618.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Anhui {ECO:0000313|EMBL:CAX74618.1};
RA   Gang L.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00000707,
CC         ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; FN318890; CAX74618.1; -; mRNA.
DR   AlphaFoldDB; C1LIU0; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:CAX74618.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          26..135
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          276..865
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          607..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  105932 MW;  6F71E68966BAACDC CRC64;
     MQPSSAFLRK LQAGMVSEYE NCRNADILAS QKAKVEELMK VEMVKGDLWY ILSLNWWAKW
     EVFVDLVSKS GIVDETSEEY PGKVDNSDIL CDGKLKENLL LENDITLVPK DVWKLFVDFY
     GCVHTETSLF ERRAIQAPKS AEIEIYPPHY SFYLNSPNSN PTLLTEGTYC KFQTIRELKL
     LVAQHLKMAP GLTLHLLIHN EQNEFEELED EDATIEEANL EREKVIYVQL EPKNGIRSEI
     YVDNSRAKSI DSVKSRPELQ MVSLHGSNPP LVPGVCGLNN LGNTCFMNSA LQCMSNVPAL
     TSYFLSGKWK SELNIRNPLG SQGRIAIAYA DLIKQLWSGT RAYAVPREFK IEIARIARQF
     SGYAQHDTHE LLVFLLDGLH EDLNRIHSKP YIEVKDSDGR PDIEVANEAW QYYKSRNDSI
     IVDLFHGQLK STVICPTCQR KSVTFDPFAS LILPIQEVYK YLVRVYVWPW VPNKSQLLLL
     ELTVQTIPCA QNIIEALEQE RTPHPGCQYY IPNKSVDRSR YTPLIVYELT EGFPIPVLWT
     NDNIGQSTNL PIYISLPIND NVTGMTITIS EDLLINYIIS RLYAIGINGE ITEFSVGEEL
     KLEDENDSAA SHSVNSFHSS SQPDTSPTAS VGIVDQSKQA DENSTDNLTS LLKGRLCLRD
     IRGHDWLAGS ENGLISLPCS EAYSIILNCQ GLEIRRKLND IRSHIQQHPV TRLNQTLQLS
     DCFERFTDVE QLGSRDLWYC NRCKAEKPAT KKFDLWKLPD VLVVQLKRFR SHLRFHDKID
     TLLEFPLTGL NLTSRVLEKK PDEKFIYDLV AVSNHMGYLG GGHYTAFALN AQTNLWYFFD
     DSSTRECDPS KIVTSSAYVL VYVRRKVGSM LMYNANNSND EEQEDSSSET DENGLLNGDL
     SLNYVSKACM QNGCTDNTNS SSNLQDQDLM DIE
//