ID A0A1J4JC37_9EUKA Unreviewed; 959 AA.
AC A0A1J4JC37;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=USP domain-containing protein {ECO:0000259|PROSITE:PS50235};
GN ORFNames=TRFO_37637 {ECO:0000313|EMBL:OHS96225.1};
OS Tritrichomonas foetus.
OC Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC Tritrichomonas.
OX NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHS96225.1, ECO:0000313|Proteomes:UP000179807};
RN [1] {ECO:0000313|Proteomes:UP000179807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA Tasca T., Bogo M.R., de Souza W.;
RL Submitted (OCT-2016) 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 -!- 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:OHS96225.1}.
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DR EMBL; MLAK01001191; OHS96225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4JC37; -.
DR VEuPathDB; TrichDB:TRFO_37637; -.
DR OrthoDB; 24284at2759; -.
DR Proteomes; UP000179807; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; 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; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000179807}.
FT DOMAIN 149..457
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 959 AA; 110076 MW; 26343E8F9A45EF10 CRC64;
MWPFYSRPKI PSNSPSFTFL VPPKTAGKPT FSETFSQSYS SFTAVYFYET QGLTIYLTYS
SSLCQYDDVR YLFDFVINDE KPFTTVSSFS LNRPFISIPI SSQNLQNSNK FGKKYDIHEK
INKNDFILSI KIRSHCLSNV CVCDNIPYVG IMNLGLTCYI AASLQYLASI TPFVSLIFRQ
KPEPNTTSYE LQRVFGQMKS STTPLSITTF VSSFGSNLRD LIFIEQDAHE FITMLFDRLD
TELGEEFCKK RKALFGVETM RIIQCTKIDI KSEIIEDSND IDLPVKGVHN LKRALDKIST
KEKMTGNSKW DTGDEKYGKQ DAVLYKKYKI LPPFLMFHLM RFTYNESNFE CEEVKSSFDC
PNEIDMSKYV IDNYTHETRY KMMGIVAHRG CLISGHYVAF ISPKVDNDRW FQFNDSTVSV
SSLNEARATF GGGKSAIMNL FGAHNDFVAY LVGYVRYDFI EENRKNLIAP VEIAPLLSNN
FSANILNLTK LSNQSETIHK QADDDVIDLD KTKSFSPKKP ILDTIYGKGE RIDWNEKDKT
IFELIGIPKN SNVKIYINYP KMNSLLGPID GNKSASDFAF KGFFIQFIVT DGSINEPVFV
YIENVLFSVD DTSTLFYKYN NDYLLVFEND FLTNDSPCVP SCSSITLISK NGITLNINEI
KLKVMANTSY QSIQVMLAEH LNQRNTQINL KQNLKILPSR VLIYSGNKFL PPNKYKNALL
LHKFYSLEYR ILVEPATINS MNFNVPLTLF LTDLNHVTTK KEEYWFSKDT LIQSLFQYIP
VFFNFPKNTK FLISIQNQGI ATTILGPSPT EICHSQFVNI NDAQNDFQNV RVDLIRGFFP
KKMAEFKEFI KQKKMLTIEV RTENLWNCSR TIGFFDVNKD STFLDIVNIV KIMDKMENIN
IKEISVKSEN YIFFGLLVQE NANVFDSLIK ASQQTQANPR SVLNHERPVI SIKLNPKSK
//