ID   OTUBL_CAEBR             Reviewed;         288 AA.
AC   A8XDJ2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Ubiquitin thioesterase otubain-like {ECO:0000250|UniProtKB:Q9XVR6};
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96DC9};
DE   AltName: Full=Deubiquitinating enzyme otubain-like {ECO:0000250|UniProtKB:Q9XVR6};
DE   AltName: Full=Ubiquitin-specific-processing protease otubain-like {ECO:0000250|UniProtKB:Q9XVR6};
GN   Name=otub-1 {ECO:0000312|EMBL:CAP30711.1}; ORFNames=CBG11576;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP30711.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC       and plays an important regulatory role at the level of protein turnover
CC       by preventing degradation. Specifically cleaves 'Lys-48'-linked
CC       polyubiquitin (By similarity). {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; Evidence={ECO:0000250|UniProtKB:Q96DC9};
CC   -!- SIMILARITY: Belongs to the peptidase C65 family. {ECO:0000255}.
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DR   EMBL; HE600985; CAP30711.1; -; Genomic_DNA.
DR   RefSeq; XP_002637711.1; XM_002637665.1.
DR   AlphaFoldDB; A8XDJ2; -.
DR   SMR; A8XDJ2; -.
DR   STRING; 6238.CBG11576; -.
DR   MEROPS; C65.A01; -.
DR   EnsemblMetazoa; CBG11576.1; CBG11576.1; WBGene00032679.
DR   GeneID; 8579707; -.
DR   KEGG; cbr:CBG_11576; -.
DR   CTD; 8579707; -.
DR   WormBase; CBG11576; CBP17228; WBGene00032679; Cbr-otub-1.
DR   eggNOG; KOG3991; Eukaryota.
DR   HOGENOM; CLU_014832_3_0_1; -.
DR   InParanoid; A8XDJ2; -.
DR   OMA; VRVRYMD; -.
DR   OrthoDB; 1257066at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; IBA:GO_Central.
DR   Gene3D; 1.20.1300.20; -; 1.
DR   Gene3D; 3.30.200.60; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR016615; Otubain.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR019400; Peptidase_C65_otubain.
DR   InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR   InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR   PANTHER; PTHR12931; PTHR12931; 1.
DR   Pfam; PF10275; Peptidase_C65; 1.
DR   PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..288
FT                   /note="Ubiquitin thioesterase otubain-like"
FT                   /id="PRO_0000394766"
FT   DOMAIN          76..275
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   288 AA;  32949 MW;  C82E79D93EE5DA87 CRC64;
     MVNDTSENQP TTAGIVTTTE DELILQDQQM KRIEDEQKAS PLVGEKMPCA TLVSLYDQET
     APAFFEKANE LAKVYSHIRF IRGDGNCFIR AIQVGLVEIL LNDKERLVKF IASCKEWTER
     LVKLGFPDWT CTDFCEFFIE FIEKVRDGIH QKEDVFRIFN DDNTANYLLM FFRLITSGYL
     KEHAAEYEPF LDEGMSLAQY CETEIEAMWK ESDHLGIIAL VRALNIRIRI EYMDRNAAPN
     GGTHHNLPDG HDNATFTPDI TLLYRPGHYD LIYKAPAETS KPALPPVA