ID D0A5E6_TRYB9 Unreviewed; 236 AA.
AC D0A5E6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN ORFNames=TbgDal_XI120 {ECO:0000313|EMBL:CBH16897.1};
OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH16897.1, ECO:0000313|Proteomes:UP000002316};
RN [1] {ECO:0000313|Proteomes:UP000002316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA Barry J.D., Berriman M., Hertz-Fowler C.;
RT "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT chronic human african trypanosomiasis.";
RL PLoS Negl. Trop. Dis. 4:E658-E658(2010).
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:RU361215};
CC -!- SIMILARITY: Belongs to the peptidase C12 family.
CC {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|RuleBase:RU361215}.
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DR EMBL; FN554974; CBH16897.1; -; Genomic_DNA.
DR RefSeq; XP_011779161.1; XM_011780859.1.
DR AlphaFoldDB; D0A5E6; -.
DR GeneID; 23866354; -.
DR KEGG; tbg:TbgDal_XI120; -.
DR VEuPathDB; TriTrypDB:Tbg972.11.120; -.
DR OrthoDB; 179179at2759; -.
DR Proteomes; UP000002316; Chromosome 11.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF17; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW Protease {ECO:0000256|RuleBase:RU361215};
KW Thiol protease {ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU361215}.
FT DOMAIN 5..217
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
SQ SEQUENCE 236 AA; 25926 MW; 2DF8D8850114A5F5 CRC64;
MTKTWLPLES NPDVLNEYLK SLGLTNPKVA FNDVFGLDAE LLAMVPRPIY AMILLYPLSD
GMESGDAAAC LKQKSEIEQF MTTNKFFYSK QTISNACGTM AVLHAVLNNT DVVGDMLEGS
PIATLLWSTK DKSPEENAKL IESDSLLDEA HALASASGVT DNQPLDADID LHFTCFVKIG
DRCVELDGRK PHPLLHGHCV DEESFVKSCV DAIKEKMGRD PQSPRFNIIA LCESCE
//
