ID   A0A1X0PA66_9TRYP        Unreviewed;       884 AA.
AC   A0A1X0PA66;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   29-MAY-2024, entry version 22.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=TM35_000016930 {ECO:0000313|EMBL:ORC93816.1};
OS   Trypanosoma theileri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC93816.1, ECO:0000313|Proteomes:UP000192257};
RN   [1] {ECO:0000313|EMBL:ORC93816.1, ECO:0000313|Proteomes:UP000192257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edinburgh {ECO:0000313|EMBL:ORC93816.1};
RA   Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA   Matthews J., Matthews K., Carrington M.;
RT   "An alternative strategy for trypanosome survival in the mammalian
RT   bloodstream revealed through genome and transcriptome analysis of the
RT   ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL   Submitted (MAR-2017) 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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORC93816.1}.
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DR   EMBL; NBCO01000001; ORC93816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0PA66; -.
DR   STRING; 67003.A0A1X0PA66; -.
DR   VEuPathDB; TriTrypDB:TM35_000016930; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000192257; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:TreeGrafter.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:ORC93816.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192257};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          20..332
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   884 AA;  101798 MW;  604F6824888CFD92 CRC64;
     MLRNTYCFSY EEREKPPPYS GLVNQGSTCY LNAVIQVLYH LPAFRYSIYS IEEPEKHSIT
     LALRNIFSQL NCSYSFISTK DLTDAFGWED KEAYIQQDVH EMMQKLFQIL ERVCKNTPQE
     NFIRDLFYGE ITYITRTVDG VDHTTYHKEG FYDIELSVKD KNSIYDSLDQ WIQPERMENV
     SLEIEKGKPS SVHVVERKQF FSRLPPVLLV HPNRVCFSTE TCEVLMLENK WTFSNSLNLE
     SYIFSEGGDN VKDVKNLGTK YELRSVIIHQ GGAHSGHYLS YVHIGEEWIC FNDNSVSRVN
     EKIVMQAAYG GKRGYLSGFS NERASLLMYV NKKKSDEILK EKPIPKHLKD VAENINELNK
     RKWDEAYTKK EYYYLKDGER LIHVLDGYAN RGLKSSLFSS LCTSSIQDLY NTIAAEINQT
     ADKFRIWVYP EIPIMKSGCG ILKDITSIKF FFFVESLPKP KEEIEALSKD YFFAPVRLVY
     EDTLRFYGIV HSREELKELM MENKEKMKCF MCTFPPTVYE VSVDEVLIGS NLILCPESVS
     NKSLLYILQR LLYNEVHLFL LENKNANSWK PFGSFQLDNN TSYEDLQKEA FRLLSLAGLH
     LPPSPEYIGF HSQISSDSAV PSLSIAPPIS DNGCTSTLGS ILAHQNEMGC LYVQILPLPL
     SLLDVLRVVI FNVGGGFRPL VFIEKKNYTL GELFRITLDQ YGSYLSPELV QRITRSLQEN
     IPALRLLSYE EMLHLNVQVN NEERIPLTPG YYIIDVLVEV KEGFSLIDVL FCSRRKKEDY
     FGFPTNIPIS NTYEETGEEI ARRVADKIKA TEEVADITLW IVAIREQKGF YHTIGSKDSL
     KSVIKRISSE VECFVIDRPR SFSLDGVENS HQKSEQSIVI RETS
//