ID   Q0VA01_XENTR            Unreviewed;       469 AA.
AC   Q0VA01;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   Flags: Fragment;
GN   Name=otud7b {ECO:0000313|EMBL:AAI21326.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI21326.1};
RN   [1] {ECO:0000313|EMBL:AAI21326.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testes {ECO:0000313|EMBL:AAI21326.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) 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 C64 family.
CC       {ECO:0000256|ARBA:ARBA00005865}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC121325; AAI21326.1; -; mRNA.
DR   AlphaFoldDB; Q0VA01; -.
DR   MEROPS; C64.001; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd22772; OTU_OTUD7B; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   PANTHER; PTHR13367:SF8; OTU DOMAIN-CONTAINING PROTEIN 7B; 1.
DR   PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR   Pfam; PF02338; OTU; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   2: Evidence at transcript level;
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          147..329
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   REGION          25..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         469
FT                   /evidence="ECO:0000313|EMBL:AAI21326.1"
SQ   SEQUENCE   469 AA;  52183 MW;  27F68F540928F599 CRC64;
     MASKGKKWDV GAALNDYDQL RQTSAGGLGH SFSEGRNFKP PEVGRSVRPM LQRQDDVVQE
     KRLSRGISHA SSSIVSLARS HVSSNGSSEH PLETPVCTFQ LPDLTVYKDE FRNFIERDLI
     EQSMLVALEH AGRLNWWAQL DPTYPRLLPL ATTGDGNCLL HAASLGMWGF HDRDLMLRKS
     LYTLMEKGAE KEALKRRWRF HQTMQNKESG LVYTEEEWQK EWNDLIKLAS SEPRMHYGTN
     GGNCGGVESS EEPVYESLEE FHVFVLAHVL KRPVVVVADT MLRDSGGEAF APIPFGGIYL
     PLEVPPNKCH CSPLVLAYDQ AHFSALVSME QKEQTKEQAP FIPLTDSDHK LLPVHFAVDP
     GKDWEWGKND SDNVCLASVT LSLEAKLNLL HNYMSVTWLS LPCETQAPLA QPESPTASAG
     DDARSAAESG ESDKESVCSS SASNGGSKSG KEKDKEKDKS RKDKEKKKK
//