ID E6ZY30_SPORE Unreviewed; 241 AA.
AC E6ZY30;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN ORFNames=sr10633 {ECO:0000313|EMBL:CBQ72137.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72137.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ72137.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311452; CBQ72137.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZY30; -.
DR MEROPS; C12.002; -.
DR EnsemblFungi; CBQ72137; CBQ72137; sr10633.
DR VEuPathDB; FungiDB:sr10633; -.
DR eggNOG; KOG1415; Eukaryota.
DR HOGENOM; CLU_054406_0_2_1; -.
DR OrthoDB; 179179at2759; -.
DR Proteomes; UP000008867; Chromosome 3.
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.
DR PROSITE; PS00140; UCH_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW Protease {ECO:0000256|RuleBase:RU361215};
KW Thiol protease {ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU361215}.
FT DOMAIN 91..107
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|PROSITE:PS00140"
SQ SEQUENCE 241 AA; 26187 MW; F1D8BCD8D675C741 CRC64;
MTESRMMWVP LESNPELFTT WCSSMGMDTS KFAFHDIYGT DPDLLAMVPQ PVSAVLLLFP
ITESVEKLRA SENASAQPPP SDSNDILWFK QTIGNACGTI GLLHALANSS AASAIKPGSP
LDTLFTKARS TQDPDERASI LYNSKELQTV HEATASQGQS QAPDDLDNVL LHFVCYVRSK
DGELVELDGS GGRKGPLNRG KKVATQEELL PVAVEYVKDN YMALNPDEVN FNLIALGPSL
D
//