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 27-MAR-2024, entry version 55. 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 AGR; Xenbase:XB-GENE-17335325; -. DR CTD; 444600; -. DR Xenbase; XB-GENE-17335325; otud6b.L. DR OrthoDB; 242020at2759; -. DR Proteomes; UP000186698; Chromosome 6L. DR Bgee; 444600; Expressed in muscle tissue and 19 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_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 //