ID E6ZTX7_SPORE Unreviewed; 761 AA.
AC E6ZTX7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=sr10393 {ECO:0000313|EMBL:CBQ70684.1};
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:CBQ70684.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ70684.1, 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:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ311441; CBQ70684.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZTX7; -.
DR EnsemblFungi; CBQ70684; CBQ70684; sr10393.
DR VEuPathDB; FungiDB:sr10393; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_340693_0_0_1; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000008867; Chromosome 2.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02661; Peptidase_C19E; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:CBQ70684.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 198..508
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 82552 MW; 3661B9905FA44AAF CRC64;
MAEVVRRPSS QADSGSGSRS YSQSPQKSNG LRRSDSFSSQ TNKSSSSPNG HHPHKKSSSI
SSLPNSPSKQ ERRKLAKEIL SAGGDQLRDT LKQRGMLHAL LADPVKFIKS SQKQGQDYTT
LGLTPVNDLN FAAAQKRKQE QKQHALLLHT DSPTLNGNGA LPTEAPSSPT KNGKAKSRDL
YPYKVSLRFP GKVRGVATGL ANYGNTCYMN SVMQSLIHTP PLAFALLTQD LDALHGELGG
KPNATFDAVT AMHAFTRASL MGSKPTNAPK EFNRNLKAFA KPLRQGRQED AHEYLRFLLE
ALQQSCLARA SKSLKPDDPI RRTTFVQKMF GGKLRSRVTC HSCGHNSDTF DPFMDLSLEV
RKGITSLTDA FRAFVAKDHL TGSEKYKCDK CKRKVDATKQ FTIEAAPPAL TVHLKRFTAF
GGKVSRQINF DESLNIAPYL SVNRGPARYK LYAVVHHYGS GPNSGHYVAS VRSPSGKWTR
MDDSLVSEMG RSGPLNDQSA YILFYMKEKD EALDKAIAAA TSVKSPMVKA SPASPASQLV
GDKKRKAVSE SESDSDSVGG DDAADADGFD DDAAYRAILK RRKAAAAKNT GEEESDSDSP
PPRTPGQKLD QMLSSKPKSS ASFYGARSNP FTLPTSSSID EELGTAIDRD EYESLVGPVS
TAATSVSSPS RRDAPDDPEA DSDEDSFVAM SKKEKRKQKK AAQLVHAAKT SRGIPASPYA
SALTGGYSGA SAREQKKEKS KRDKEKALGG FAARMKPRPK F
//
