ID   G0W955_NAUDC            Unreviewed;       329 AA.
AC   G0W955;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN   Name=NDAI0C06570 {ECO:0000313|EMBL:CCD24316.1};
GN   OrderedLocusNames=NDAI_0C06570 {ECO:0000313|EMBL:CCD24316.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD24316.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD24316.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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:0000256|RuleBase:RU367104}.
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:0000256|ARBA:ARBA00000707,
CC         ECO:0000256|RuleBase:RU367104};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367104}.
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DR   EMBL; HE580269; CCD24316.1; -; Genomic_DNA.
DR   RefSeq; XP_003669559.1; XM_003669511.1.
DR   AlphaFoldDB; G0W955; -.
DR   STRING; 1071378.G0W955; -.
DR   MEROPS; C85.006; -.
DR   GeneID; 11496729; -.
DR   KEGG; ndi:NDAI_0C06570; -.
DR   eggNOG; KOG3288; Eukaryota.
DR   HOGENOM; CLU_049327_0_0_1; -.
DR   OMA; TRCILVY; -.
DR   OrthoDB; 5486835at2759; -.
DR   Proteomes; UP000000689; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd22745; OTU_OTU1; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
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   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW   Hydrolase {ECO:0000256|RuleBase:RU367104};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW   ECO:0000256|RuleBase:RU367104};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU367104}.
FT   DOMAIN          131..252
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
SQ   SEQUENCE   329 AA;  37275 MW;  0787C669DFDAC407 CRC64;
     MRLKISGIPG NPDKVITIEN GSNLSQLIGV IKESVNGNSA EFESGLNGIR IGYPPQRIDI
     NDDNLNKPVE ELGLKSGERV TLIIEGGAVR NNDSQASNVS NNNKNAQLQS SRKLKDTQMY
     IDTYDRGRKI LQVHKVPDDN SCLFHSISYC MYNDISLSDE LRQLCSRVIT QDKTTYNDAI
     LGRPNREYCD WILRKDSWGG GIELAILSKE LDMGIYVLDM DAIKFEKFND EQYDKFFIIL
     FNGVHYDSIE LIDEMTKEKL TIFDKRDELG DLVLKNILKI AQRLKSKGYA FNTQKAKIIC
     NICKMKFVGE RDIGRHAEST GHTDFGQST
//