ID   OTUD5_XENTR             Reviewed;         518 AA.
AC   Q6GL44;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=OTU domain-containing protein 5;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96G74};
DE   AltName: Full=Deubiquitinating enzyme A;
DE            Short=DUBA;
GN   Name=otud5;
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].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Deubiquitinating enzyme that may function as negative
CC       regulator of the innate immune system. Has peptidase activity towards
CC       'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave
CC       'Lys-11'-linked ubiquitin chains (in vitro) (By similarity).
CC       {ECO:0000250|UniProtKB:Q96G74}.
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;
CC   -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
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; BC074667; AAH74667.1; -; mRNA.
DR   RefSeq; NP_001004849.1; NM_001004849.1.
DR   AlphaFoldDB; Q6GL44; -.
DR   SMR; Q6GL44; -.
DR   MEROPS; C85.001; -.
DR   GeneID; 448134; -.
DR   KEGG; xtr:448134; -.
DR   AGR; Xenbase:XB-GENE-6455884; -.
DR   CTD; 55593; -.
DR   Xenbase; XB-GENE-6455884; otud5.
DR   eggNOG; KOG2605; Eukaryota.
DR   InParanoid; Q6GL44; -.
DR   OMA; DSHQHTH; -.
DR   OrthoDB; 691582at2759; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR   CDD; cd22752; OTU_OTUD5-like; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12419:SF4; OTU DOMAIN-CONTAINING PROTEIN 5; 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..518
FT                   /note="OTU domain-containing protein 5"
FT                   /id="PRO_0000278229"
FT   DOMAIN          171..294
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..182
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          231..241
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          282..287
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          371..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..69
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        182
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q96G74"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250|UniProtKB:Q96G74"
SQ   SEQUENCE   518 AA;  56332 MW;  69368C93932208F4 CRC64;
     MTILPKKKPP PPSDPEGNGE RSGSGGADSH SRSGARPRSS PPPRWAYPGN PAPPERHPAG
     TPRPQQASPP PCSGGSGGAG SGPLGEGALG PCCCCTGAGG CCSGPGHSKR RRQGVSAGPG
     APGSSPDRED GAGNNSEDEY ETAARTQAID PDTAEQQEHW FEKALQEKKG FIIKQMKEDG
     ACLFRAVADQ VYGDQDMHEV VRKHCMDYLM KNADYFSNYV TEDFTTYINR KRKNNCHGNH
     IEMQAMAEMY NRPVEVYQYG TEPINTFHGI QQNEDEPIRV SYHRNIHYNS VVNPNKATIG
     VGLGLPSFKP GFAEQSLMKS AIRTSEESWI EQQMLEDKKR ATDWEATNEA IEEQVARESY
     LQWLRDQEKQ ARQPRKASAT CSSATAAASS GLEEWSGRSP RQRSTAGSPE HPDLHAELCM
     KPPSPAATLM LGKPPSPCAP GPSNQTCAGA DRATSPLVSL YPALECRAIM QHMSPTAFGL
     KDWDDDEILA SVLAVSQQEY LDTIKKSTLR RDSSPDHS
//