ID E9B1G2_LEIMU Unreviewed; 456 AA.
AC E9B1G2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=LMXM_30_0140 {ECO:0000313|EMBL:CBZ29068.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ29068.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|EMBL:CBZ29068.1, ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ29068.1,
RC ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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|RuleBase:RU366025}.
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DR EMBL; FR799583; CBZ29068.1; -; Genomic_DNA.
DR RefSeq; XP_003877533.1; XM_003877484.1.
DR AlphaFoldDB; E9B1G2; -.
DR GeneID; 13451746; -.
DR KEGG; lmi:LMXM_30_0140; -.
DR VEuPathDB; TriTrypDB:LmxM.30.0140; -.
DR OMA; FKSDAEY; -.
DR OrthoDB; 160664at2759; -.
DR PhylomeDB; E9B1G2; -.
DR Proteomes; UP000007259; Chromosome 30.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 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:CBZ29068.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 1..71
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 104..445
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 343..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 50718 MW; 2BCDAFB931A9A252 CRC64;
MAEIKVKWGK ENLTMEVDLG STVGAFKEAL KAKTGVPVEK QKLMGLKPAM NKDDATLSAA
GLVSGKTVML IGSAESTATV PMVQATVVEA NETGGYTATA TTSNGLKNIA NTCYLNSALQ
MMRSIPEIRE VLEAYRGDNA LLQQLRAVLQ LLESTKDAVM PLQFWTTLVQ TNPTFGERNE
HGGFMQQDSQ EVLNMLLQAV NSVLPEKYAH LFEGKLHQTL TCVDDPADKG KESDVPFTML
TCNITGEVQT LEAGLEHAFD EHFTAPCEAL QKDAAQFTRV SKLTEAPEYV FVHMVRFSWR
GDIQKKAKIL KPITFPFTLD TTIISTEALK AAQKPVREVV RERRDKELER RRRPRTEKSS
PVDKSEEEKV PLILKNESGY YDLCGVISHK GRSADGGHYV YWGKKADTWL VYDDEHVAAV
SEEDVKRLRG VGEAHIAYVL LYRSRDPVTR TPVIPL
//
