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 27-MAR-2024, entry version 92. 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}; 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; AJ720738; CAG32397.1; -; mRNA. DR RefSeq; NP_001006347.1; NM_001006347.1. DR AlphaFoldDB; Q5ZIP6; -. DR SMR; Q5ZIP6; -. DR STRING; 9031.ENSGALP00000058469; -. DR MEROPS; C85.008; -. DR PaxDb; 9031-ENSGALP00000025612; -. DR Ensembl; ENSGALT00000061824; ENSGALP00000058469; ENSGALG00000041337. DR Ensembl; ENSGALT00010026542.1; ENSGALP00010015119.1; ENSGALG00010011086.1. DR Ensembl; ENSGALT00015005715; ENSGALP00015003487; ENSGALG00015002560. 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; PIILVYM; -. DR OrthoDB; 242020at2759; -. 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 cell types or 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 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..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 //