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Database: UniProt
Entry: W9I182_FUSOX
LinkDB: W9I182_FUSOX
Original site: W9I182_FUSOX 
ID   W9I182_FUSOX            Unreviewed;       248 AA.
AC   W9I182;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN   ORFNames=FOYG_09595 {ECO:0000313|EMBL:EWY88367.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY88367.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY88367.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:RU361215};
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|RuleBase:RU361215}.
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DR   EMBL; JH717844; EWY88367.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9I182; -.
DR   OrthoDB; 179179at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR   Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF17; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW   Protease {ECO:0000256|RuleBase:RU361215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW   Thiol protease {ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU361215}.
FT   DOMAIN          17..217
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
SQ   SEQUENCE   248 AA;  27079 MW;  ABBD5B9AA1C59591 CRC64;
     MSTTPGVSFR KDGTKTFIPL ENNPEVFTKL IHNLGVSEKL GFYDVYSIDE PELLAMIPRP
     VHALVFITPA PMWARVREND PGSKELSYDG SGPDEPVVWY KQTIGHACGL IALLHSVSNG
     TAKSFINANS ILDKILKETQ DLKPLQRANH LYNSIELEKA HMAAAVTGDT IAPASEEPSG
     YHFISFVKGQ DGHLYDLEGG WGGPVDCGTL DDESNDINAS FTPGFLLYDG YFLRACPGAS
     TDLIEFSL
//
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