ID   OTU6B_XENLA             Reviewed;         294 AA.
AC   Q6GM06;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Deubiquitinase OTUD6B {ECO:0000305};
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q8N6M0};
GN   Name=otud6b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Deubiquitinating enzyme that may play a role in the
CC       ubiquitin-dependent regulation of different cellular processes.
CC       {ECO:0000250|UniProtKB:Q8N6M0}.
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:0000250|UniProtKB:Q8N6M0};
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; BC074286; AAH74286.1; -; mRNA.
DR   RefSeq; NP_001086171.1; NM_001092702.1.
DR   AlphaFoldDB; Q6GM06; -.
DR   SMR; Q6GM06; -.
DR   DNASU; 444600; -.
DR   GeneID; 444600; -.
DR   KEGG; xla:444600; -.
DR   CTD; 444600; -.
DR   Xenbase; XB-GENE-17335325; otud6b.L.
DR   OrthoDB; 1541668at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 444600; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..294
FT                   /note="Deubiquitinase OTUD6B"
FT                   /id="PRO_0000076283"
FT   DOMAIN          150..287
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          85..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..161
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          222..232
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          270..280
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        100..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        161
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6M0"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  33432 MW;  48293B8CD6D4E7F0 CRC64;
     MDVAEENSEE ALLIKQQRKE KKEVQAKIQC MKNSVPKNDK KRRKQMTEDI AKLEAEVEAR
     HKEELEALAQ KPTEPTQVSS ITNGVTSLDL GSEEPVQQPR VSKAQKRREK KAAQEKERDD
     RIAEAEIANL SGARHLESQK LAQILAEREL QIRQIPSDGH CMYRAIEHQL NEQGNSLTVA
     NLRSQTADYM QKRAEDFLPF LTNSSTGDMY TQEEFQKYCT DIVNTPAWGG QLELRALSHI
     LKTPIEVIQA ESLPIVIGEE YSNKPITLVY MRHAYGLGEH YNSVEQLDTS TENS