ID   A0A0M3HP75_ASCLU        Unreviewed;       652 AA.
AC   A0A0M3HP75;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000364301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0000364301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C64 family.
CC       {ECO:0000256|ARBA:ARBA00005865}.
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DR   AlphaFoldDB; A0A0M3HP75; -.
DR   WBParaSite; ALUE_0000364301-mRNA-1; ALUE_0000364301-mRNA-1; ALUE_0000364301.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd22768; OTU_OTUD7; 1.
DR   CDD; cd14273; UBA_TAP-C_like; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   PANTHER; PTHR13367:SF27; OTU DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR   Pfam; PF02338; OTU; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          144..328
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   REGION          53..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..638
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  73673 MW;  0F96E81BFFF739EB CRC64;
     MHDDNVDVHV QAVEKFVAIT QTTPSFARGF LEDDGWDVAA SVQRFNIWNK KDEEPQSISP
     STSDGKVEEG NNENNYGGEG KWSWDVAKRF EMPSCAFVLP NLSELAPEFR RFLEEDLIET
     TILKKLENSG HLNWWCCNGG GQRLWPLSTT GDGNCLLHAA SLGLWGVHDR HLMLRKTLHE
     MITQGSRRHT LYRRWRFAES KANQESGLTL SDDEWQKEWQ ILLDSAAATP RKTTQRNELS
     TETENQDSEQ VYASLETIHV FALAHVLKRS IIGTLVSDTV LRNAMGEELA PIPFGGIYLP
     LECPPEQCSR SPLVLCYDSA HFSAVVTMRP TSNSTLLPII PIVDKERNLL PVHFSVDPGP
     DFTWWKDAED DEIASRIELT EADRLSLICE YLDISKIEVR RGSHRRSTLT RPGQNDDTNK
     SMTLACGGDL AKKHLSSGII FEIAQHIRNK FRSSARRKNT RKRCIDAVTV ADLRYSNLIL
     AAHLDNCVHE YMEHMVDSYM YYARQRFEQA KRTPASVARQ RNRISRSFST SSLLIKCINV
     HCEKVASQST NFLCADCYEY QRQLMASFGT RPGRLRSLRS GTTADRGDED DSEKKRSTGR
     SIKSSTMPSL GSSSADNGAG DHKHISEETP RRTVHTVAVH DAQHPFESIT TK
//