ID A0A0R3W987_TAEAS Unreviewed; 588 AA.
AC A0A0R3W987;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme A {ECO:0000256|ARBA:ARBA00033460};
GN ORFNames=TASK_LOCUS6995 {ECO:0000313|EMBL:VDK37683.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000699401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000699401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK37683.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 -!- SIMILARITY: Belongs to the peptidase C85 family.
CC {ECO:0000256|ARBA:ARBA00010407}.
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DR EMBL; UYRS01018560; VDK37683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3W987; -.
DR STRING; 60517.A0A0R3W987; -.
DR WBParaSite; TASK_0000699401-mRNA-1; TASK_0000699401-mRNA-1; TASK_0000699401.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; Unassembled WGS sequence.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd22752; OTU_OTUD5-like; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12419:SF4; OTU DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000282613}.
FT DOMAIN 200..322
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 65004 MW; 99E911D554EECFCF CRC64;
MVVRRNSEEN SGKKSVQDSS SDTSEEDLDY LIDSVLGNLS VYSPKPQEMT IKNRKERSKH
ERSEKATNVE STASSQDESH PFGIRRHFSG NRGHASSRVR NRQSRGHSSV VRPNRFAFTQ
YATAADGRLS SASVNRHWSS PHEPTKNIPV RLVECSEVTD LGTGNNSEDE YGRMSENTSP
NSAKSEGNAL EQLLKEKKGW KVVRVHGDGA CLFRSVSHQV FGDEEKHDII RKQVVDYMCK
NREHFSQYVT EDFDHYLHRK RQPNCFGNHL EIQAISELYN RPVEIYYNNV VPINVFHAEY
SHDVPIRLGY YGRTHYNSII DPCKPSFGHG LGMPNYQPGL PEKDLVKQAI RESETSELEE
AMLRDKLAES ETKQLEDCIA EHVLRESLYE HVKARLDGQA AERQRMTSSQ SLSPRPRKSS
PPPPLSSHPA PSSTSASQVP CSSSYSSTLP SSSTSIKPSS SSAAIDVPGS ATTFTAAAAS
AATASASLSC DPAASDFAVL RHIPANMLDM SDDDVLAMVL EQSRSEYIEG LRAAYRGEDD
DFEDRGRPTA QSYFRQNLEP PQPPAASSKN DSGGGGCGSD DGDGDVRN
//
