ID   OTU5B_XENLA             Reviewed;         518 AA.
AC   Q640H3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=OTU domain-containing protein 5-B;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme A;
DE            Short=DUBA;
GN   Name=otud5-b;
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=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-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}.
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}.
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DR   EMBL; BC082654; AAH82654.1; -; mRNA.
DR   RefSeq; NP_001088023.1; NM_001094554.1.
DR   AlphaFoldDB; Q640H3; -.
DR   SMR; Q640H3; -.
DR   MEROPS; C85.001; -.
DR   GeneID; 494714; -.
DR   KEGG; xla:494714; -.
DR   CTD; 494714; -.
DR   Xenbase; XB-GENE-6255335; otud5.L.
DR   OrthoDB; 1448656at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 494714; Expressed in internal ear and 19 other tissues.
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:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR   InterPro; IPR031084; OTU5.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419:SF4; PTHR12419:SF4; 1.
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..518
FT                   /note="OTU domain-containing protein 5-B"
FT                   /id="PRO_0000278228"
FT   DOMAIN          171..294
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          1..147
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          391..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..97
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"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   518 AA;  56209 MW;  2099AB07C6C93EC1 CRC64;
     MTILPKKKPP PSSDPEGNGE RSGSGAPDSH SRSGARPRSS PPPRWAYPGN PSSAAERHTQ
     QVSPPPGSAT SGGAGPLGDG APASSSSSSS SSCNGAGAGG CCSGPGHSKR RRQVLSAGPG
     ATGNCPDTDD GAGNNSEDEY ETAAQTQHLD PDTAQQQEHW FEKALCEKKG FIIKQMKEDG
     ACLFRAVADQ VYGDQDMHEV VRKHCMDYLM KNADYFSNYV TEDFTTYINR KRKNNCHGNH
     IEMQAMAEMY NRPVEVYQYG TEPINTFHGI QQNEDEPIRV SYHRNIHYNS VVNPNKATIG
     VGLGLPSFKP GHAEQSLMKS AIRTSEESWI EQQMLEDKKR ATDWEATNEA IEEQVARESY
     LQWLRDQEKQ ARQPRKASAT CSSATAAACS GLEEWSGRSP RQRSTAGSPE QPDVHAELCM
     KPPSPGAALT LGKPPSPCAP GPSNQMSAGA DRATSPLVSL YPALECRAIM QHMSPTAFGL
     KDWDDDEILA SVLAASQQEY LDTMKKSTLR RESSPDHS