ID A0A125YIA0_TOXGV Unreviewed; 347 AA.
AC A0A125YIA0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=TGVEG_271070 {ECO:0000313|EMBL:ESS36165.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS36165.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC and may therefore play an important regulatory role at the level of
CC protein turnover by preventing degradation.
CC {ECO:0000256|RuleBase:RU367104}.
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:RU367104};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367104}.
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:ESS36165.1}.
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DR EMBL; AAYL02000012; ESS36165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A125YIA0; -.
DR EnsemblProtists; ESS36165; ESS36165; TGVEG_271070.
DR VEuPathDB; ToxoDB:TGVEG_271070; -.
DR OMA; CVKAREV; -.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd22744; OTU; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR PANTHER; PTHR13312:SF0; UBIQUITIN THIOESTERASE OTU1; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW Hydrolase {ECO:0000256|RuleBase:RU367104};
KW Protease {ECO:0000313|EMBL:ESS36165.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW Thiol protease {ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT DOMAIN 143..344
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 264..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 38259 MW; D9A879C4F5B5C9CD CRC64;
MAGVPEPRIL CDTMRYLVTV LAIFFFQKCA ALQPHLPPQS LRLFVGHALM PQMFQWQPET
YGWKSSPRKT VRGPHKQNRV FFSGSSSEFD TLQMVRQYSS RDYVSNAVLR RLSRSSQGDT
DLDESDNSLL PGCLEVRDMP YCVKAREVPG DGACLFVSVA ASLWWNAFET HADLNDPAFV
DMVGSLRQLA VDTLQDTNAT PLALEGDEVL SRRTLVTMAA ADYNMTPAAY CERMRLPGTW
GGGPEIVAMS HALRRVIVVY EKHSPSMQSG DSQSGSAFDT HPHRLSRPPA TDSPSDSGQN
PIKLKVVACL GFPENVAEEP LHILFTSSAG DGQAADHFLP LFPVVSQ
//
