ID   OTU6B_XENTR             Reviewed;         294 AA.
AC   Q5M8L0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Deubiquitinase OTUD6B {ECO:0000305};
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q8N6M0};
GN   Name=otud6b;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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};
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DR   EMBL; BC087978; AAH87978.1; -; mRNA.
DR   RefSeq; NP_001011269.1; NM_001011269.1.
DR   AlphaFoldDB; Q5M8L0; -.
DR   SMR; Q5M8L0; -.
DR   STRING; 8364.ENSXETP00000054791; -.
DR   MEROPS; C85.008; -.
DR   PaxDb; 8364-ENSXETP00000031929; -.
DR   DNASU; 496720; -.
DR   GeneID; 496720; -.
DR   KEGG; xtr:496720; -.
DR   AGR; Xenbase:XB-GENE-985119; -.
DR   CTD; 51633; -.
DR   Xenbase; XB-GENE-985119; otud6b.
DR   eggNOG; KOG2606; Eukaryota.
DR   HOGENOM; CLU_034963_0_0_1; -.
DR   InParanoid; Q5M8L0; -.
DR   OMA; PIILVYM; -.
DR   OrthoDB; 242020at2759; -.
DR   PhylomeDB; Q5M8L0; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Bgee; ENSXETG00000014596; Expressed in ovary and 12 other cell types or tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd22761; OTU_OTUD6; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR049772; OTU_OTUD6.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419:SF10; DEUBIQUITINASE OTUD6B; 1.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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_0000076284"
FT   DOMAIN          150..287
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..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        8..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..101
FT                   /note="Polar 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;  33367 MW;  646F5246455D08D6 CRC64;
     MDEAEGNSEE SGLIKQHRKE KRDLQAKIQS MKNSVPKNDK KRRKQLTEDI AKLEADLDVR
     HKEELEAFAQ KQPEPTQVSG ITNGVTSLDL GNEAPVQQPR QSKAQKRREK KAAQEKERDE
     RIAEAEIANL SGARHLESQK LARILAEREL QIRQIPSDGH CMYRAIEHQL RERGNDLTVA
     NLRSQTADYM QNHAEDFLPF LTNSSTGDMY TQEEFLKYCT DIVNTPAWGG QLELRALSHI
     LKTAIEVIQA ESSPIVIGEE YSSKAITLVY MRHAYGLGEH YNSVELLDTS TENS
//