ID A0A0V0RU25_9BILA Unreviewed; 692 AA.
AC A0A0V0RU25;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=usp33 {ECO:0000313|EMBL:KRX17717.1};
GN ORFNames=T07_3602 {ECO:0000313|EMBL:KRX17717.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX17717.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX17717.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX17717.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX17717.1}.
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DR EMBL; JYDL01000083; KRX17717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RU25; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF86; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR PROSITE; PS51283; DUSP; 2.
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:KRX17717.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 23..461
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 463..560
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 584..691
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
SQ SEQUENCE 692 AA; 78939 MW; 7F6219F552061418 CRC64;
MLSKIGLPVS VLTHTDEPNF GLKGIQNVGN TCYLNAAVQA LSNCPPLTEY MRHCSLPCSS
SPDGNRRNKL ASEFQKLIDA LWDDEYENML SPIFFVDAVL ACNPHFRLFQ QQDTQEFLRF
LLNELHDQLK RPVYKWEHRL LKTRNHHEML KNNTHGYDSD SSMSSCSSFV SCVSAGSDNL
DCEKNGISSD TDDASSYNST AELMEGSDNF VAEEEVLNKE FLLRKPVRYN SIISDIFSGQ
LVTSITCLRC KSVSHNKEIF QDISLSIPSL EQLVLMQNAS INGNEYVSPS SIANQSWLSW
LTLRFKEYIS RMDLTLSDCL KLFFSPEDLR GDDMYRCDRC KSLQPGVKIC RLLKTPQILC
IHIKRFRHEA SSSFKLTNRI GFPLEGLDLS DFVQGRSSDL HTYNLVAVIS HSGNADGGHY
VSYCMNHSNY RWYLFDDETV TAVDPCTVEN VEAYVLFYEK TSNTIGFVRE QASALFENSH
LLSPVETSFY YISMEWVIRL STFAEPGPVN NYSFLCRHGL VNVKKLSSRH NYCLKLSPSL
WNYLRVKFGG GPVCRHLKHC IICSAYQEAF ESRRKHELSK FYRYQNDDEY FISKSIADEN
HDFASSSRLI CTKWLRRWKA FVFGETDELP GPIDNSCMVP VPLRNGSAKT ISIEVSDLLP
NLCFCCINND TWRDLISIYG GGPEICCQNK EL
//
