ID   OTU6B_CHICK             Reviewed;         302 AA.
AC   Q5ZIP6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Deubiquitinase OTUD6B {ECO:0000305};
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q8N6M0};
GN   Name=OTUD6B; ORFNames=RCJMB04_24h18;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720738; CAG32397.1; -; mRNA.
DR   RefSeq; NP_001006347.1; NM_001006347.1.
DR   AlphaFoldDB; Q5ZIP6; -.
DR   SMR; Q5ZIP6; -.
DR   STRING; 9031.ENSGALP00000025612; -.
DR   MEROPS; C85.008; -.
DR   PaxDb; Q5ZIP6; -.
DR   Ensembl; ENSGALT00000061824; ENSGALP00000058469; ENSGALG00000041337.
DR   GeneID; 420222; -.
DR   KEGG; gga:420222; -.
DR   CTD; 139562; -.
DR   VEuPathDB; HostDB:geneid_420222; -.
DR   eggNOG; KOG2606; Eukaryota.
DR   GeneTree; ENSGT00390000012840; -.
DR   HOGENOM; CLU_034963_0_0_1; -.
DR   InParanoid; Q5ZIP6; -.
DR   OMA; TYHRHMY; -.
DR   OrthoDB; 1541668at2759; -.
DR   PhylomeDB; Q5ZIP6; -.
DR   TreeFam; TF315010; -.
DR   PRO; PR:Q5ZIP6; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000041337; Expressed in muscle tissue and 14 other tissues.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IEA:Ensembl.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0043248; P:proteasome assembly; IEA:Ensembl.
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..302
FT                   /note="Deubiquitinase OTUD6B"
FT                   /id="PRO_0000076281"
FT   DOMAIN          156..293
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..167
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          228..238
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          276..286
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        167
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N6M0"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  34542 MW;  D23A118D9F4A6A13 CRC64;
     MEGSEDEEAE AGGPLQQLVK RQRREKRELQ AKIQGMKNAV PKNDKKRRKQ LAEEVAKLEA
     ELEQKHKEEL KQLKEAMPEQ NKIDSIADGV ANFELEGREQ QIQHPRISKA QKRREKKAAL
     EKEREERIAE AEIENLTGAR HLESQKLASL LAARHLEIKQ IPSDGHCMYR AIEDQLKDHH
     NSWTVATLRN QTAKYIHSHF DDFLPFLTNP NTGDMYSKEE FEKYCDDIAN TAAWGGQLEL
     RALSHILQTP IEVVQMDSPS IIVGEEYSGK PIILVYMRHA YGLGEHYNSV KLLTDATTEN
     GS