ID A0A1I8IYU5_9PLAT Unreviewed; 491 AA.
AC A0A1I8IYU5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0032020-snap-gene-0.3-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0032020-snap-gene-0.3-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A1I8IYU5; -.
DR WBParaSite; maker-uti_cns_0032020-snap-gene-0.3-mRNA-1; maker-uti_cns_0032020-snap-gene-0.3-mRNA-1; maker-uti_cns_0032020-snap-gene-0.3.
DR Proteomes; UP000095280; Unplaced.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
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:SF104; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 144..481
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 53720 MW; 285A2DF538346E8E CRC64;
AIAPPSGPPA NTAPAASQVA PAAALAAGPS SSASPASTSG LKRVASQPNL AKQRSKPDSD
KASATSAASA ASATPAPPAP TPGPSSGVSS ESSSVKQAQA QVPPRVANGG GSSVAAVVRP
FSSFDAHTLN RMAPEYGSVP HGLTGLRNLG NTCYLNSTVQ CLSNTPVLAS YFLQGTFREH
VNKSNPLGHQ GDVAEQFSVV VQALWAGRYA CVSPYDFKHT IGRHAEAFAG NEQQDSQEFL
LFLLDGLHED LNRARRRRPP PELEDKESLP DVERAKRAWA RHCLINESIM VELFQGQFKS
TLVCEQCHYK SITFDAFMYL SLPVVSDTSC RLSDCLQAFL KPERLSGSSR WFCPRCRRDQ
SAVKKIDIWR LPPYLLIHFK RFSCDRLSSR GRKLNTLVDY PISNLDMSAY HSSEARPKHS
LVYNLYGVSN HFGSMECGHY TAFCRNSNLN RWFKFDDETV TEMRSGEIRS VSNYILFYSR
LANTFQVSSS L
//
