ID Q6BVL0_DEBHA Unreviewed; 335 AA.
AC Q6BVL0;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN OrderedLocusNames=DEHA2C01804g {ECO:0000313|EMBL:CAG85795.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG85795.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG85795.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382135; CAG85795.2; -; Genomic_DNA.
DR RefSeq; XP_457759.2; XM_457759.1.
DR AlphaFoldDB; Q6BVL0; -.
DR STRING; 284592.Q6BVL0; -.
DR MEROPS; C85.006; -.
DR GeneID; 2900331; -.
DR KEGG; dha:DEHA2C01804g; -.
DR VEuPathDB; FungiDB:DEHA2C01804g; -.
DR eggNOG; KOG3288; Eukaryota.
DR HOGENOM; CLU_049327_0_0_1; -.
DR InParanoid; Q6BVL0; -.
DR OMA; IRKESSW; -.
DR OrthoDB; 5486835at2759; -.
DR Proteomes; UP000000599; Chromosome C.
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 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.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW Hydrolase {ECO:0000256|RuleBase:RU367104};
KW Protease {ECO:0000256|RuleBase:RU367104};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Thiol protease {ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT DOMAIN 122..252
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 80..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 37475 MW; 3484427BF9EC18B8 CRC64;
MKVKIKSRAG ASVISCTSNQ VSLNTLVHEI KTALKGSISD DAVVTLKNGF PPKAIDMSRL
EAPLSELGIK NGDQLILEDE NESSSTDMQE SNPTQVSSGS HTKTKSDPNI PSIYIESLDK
HLILRNIPDD NSCMFNSISY GLFGYDSFDR DGISPPSNLR SIISSTIQDN QDTYNEVVLG
RTVDKYCQWI LKKDSWGGAI ELGILAEWFK VRINCLDIES GKFIRFENEA NKPDNFIILI
YSGIHYDILS LNVNLSTSSQ DKQTDTCVWP INSKIEELVL EYSLKLCHYL QTQNYSTNTT
TFRIRCLDCY KILVGEMGAS KHANETGHYN FGEVK
//
