ID   OTU1_DICDI              Reviewed;         325 AA.
AC   Q55BI3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Ubiquitin thioesterase OTU1;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN   Name=yod1; ORFNames=DDB_G0271346;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(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.
CC       {ECO:0000250|UniProtKB:Q5VVQ6}.
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};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}.
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DR   EMBL; AAFI02000006; EAL71803.1; -; Genomic_DNA.
DR   RefSeq; XP_645629.1; XM_640537.1.
DR   AlphaFoldDB; Q55BI3; -.
DR   SMR; Q55BI3; -.
DR   STRING; 44689.Q55BI3; -.
DR   MEROPS; C85.007; -.
DR   PaxDb; 44689-DDB0266410; -.
DR   EnsemblProtists; EAL71803; EAL71803; DDB_G0271346.
DR   GeneID; 8617821; -.
DR   KEGG; ddi:DDB_G0271346; -.
DR   dictyBase; DDB_G0271346; yod1.
DR   eggNOG; KOG3288; Eukaryota.
DR   HOGENOM; CLU_049327_1_1_1; -.
DR   InParanoid; Q55BI3; -.
DR   OMA; TRCILVY; -.
DR   PhylomeDB; Q55BI3; -.
DR   Reactome; R-DDI-5689896; Ovarian tumor domain proteases.
DR   PRO; PR:Q55BI3; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   CDD; cd22793; OTU_plant_OTU1_2-like; 1.
DR   CDD; cd17059; Ubl_OTU1; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR048857; OTU1_Ubl.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR   PANTHER; PTHR13312:SF0; UBIQUITIN THIOESTERASE OTU1; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF21403; OTU1_UBXL; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..325
FT                   /note="Ubiquitin thioesterase OTU1"
FT                   /id="PRO_0000328367"
FT   DOMAIN          123..246
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ZN_FING         292..316
FT                   /note="C2H2-type"
FT   REGION          7..86
FT                   /note="UBX-like"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          128..134
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          185..195
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          235..239
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          265..270
FT                   /note="S2 site"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   325 AA;  36456 MW;  DFB2AB7B181E4BDD CRC64;
     MSLISIRIRS KTGVENIKLE SQLKLKELQN IIEEKTKIST DTQKILYGFP PKALDLSNQD
     AVISGFLANG DTITIENVSS ISSNPGVDSV TNDKVTSSTN SFDRNIKSQP FISQEEEEDG
     GYATRRVTDD DNSCLFSAVA YVLEDKNRLK GYSLRALIAQ NVKSDPFEYN EAVLGKSNEG
     YCNWIQNPKN WGGAIELSIL SNHYKVEIAA FDISTQLMYC YGEDRKYTER VYLIYDGIHY
     DALSICLTKN GPEDFDITRF SVDDKDSLAK MKVLIEKEFK AGKFTDTAKF SLICLNCNKT
     LKGEKEAAIH ASTTGHGNFT EYKKR
//