ID   OTU1_DROPS              Reviewed;         358 AA.
AC   Q29FC9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Ubiquitin thioesterase OTU1;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN   ORFNames=GA18292;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC       and may therefore play an important regulatory role at the level of
CC       protein turnover by preventing degradation. {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:Q5VVQ6};
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DR   EMBL; CH379067; EAL31326.1; -; Genomic_DNA.
DR   RefSeq; XP_001354273.1; XM_001354237.3.
DR   AlphaFoldDB; Q29FC9; -.
DR   SMR; Q29FC9; -.
DR   STRING; 7237.FBpp0278050; -.
DR   MEROPS; C85.007; -.
DR   EnsemblMetazoa; FBtr0279612; FBpp0278050; FBgn0078297.
DR   GeneID; 4814165; -.
DR   KEGG; dpo:Dpse_GA18292; -.
DR   eggNOG; KOG3288; Eukaryota.
DR   HOGENOM; CLU_049327_1_1_1; -.
DR   InParanoid; Q29FC9; -.
DR   OMA; NEEYCDW; -.
DR   PhylomeDB; Q29FC9; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0078297; Expressed in adult organism and 3 other tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   InterPro; IPR039138; OTU1_2_3.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13312; PTHR13312; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..358
FT                   /note="Ubiquitin thioesterase OTU1"
FT                   /id="PRO_0000282363"
FT   DOMAIN          5..87
FT                   /note="Ubiquitin-like"
FT   DOMAIN          161..285
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ZN_FING         328..352
FT                   /note="C2H2-type"
FT   REGION          8..94
FT                   /note="UBX-like"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          83..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..172
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          224..234
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          274..278
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          301..306
FT                   /note="S2 site"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        172
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        352
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   358 AA;  39210 MW;  87FCB64C93082855 CRC64;
     MTGSFSVKLK SKKGQFIVKD LNQNTTLGEL KTRIAQATAI QELQLHVLVG YPPKPLDLSE
     NRENQNLKTV GINSGETLIV EEKAGAAGPT STPLASGSGS STMEDDEALA RRLQAEEDAE
     HLRQVSSGGS IETGALNIVQ SLEPVISPEE SGPNGNFNGI LLKKVVPADN SCLFTSIRFV
     LNGKVDNEGS EMMRHIIAQE VSADTQQYND AVLGKSNSDY CAWIQKADSW GGAIEVSILS
     NYYGIEIDVV DIQNAIINRF GEDKNFGLRV FLLFDGIHYD PLYMETQQNS VPATIFPVEE
     MGVYQQAEQI ANEAKSSRQF TNVDKFTLRC MDCDVMLVGQ GQAQEHAKKT GHENFEEI