ID A0A0D2DXW8_9EURO Unreviewed; 584 AA.
AC A0A0D2DXW8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=PV06_00150 {ECO:0000313|EMBL:KIW47455.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47455.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW47455.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47455.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KN847332; KIW47455.1; -; Genomic_DNA.
DR RefSeq; XP_016267671.1; XM_016400618.1.
DR AlphaFoldDB; A0A0D2DXW8; -.
DR STRING; 215243.A0A0D2DXW8; -.
DR GeneID; 27352224; -.
DR VEuPathDB; FungiDB:PV06_00150; -.
DR HOGENOM; CLU_017549_2_0_1; -.
DR OrthoDB; 160664at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02657; Peptidase_C19A; 1.
DR CDD; cd16104; Ubl_USP14_like; 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; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 4..78
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 109..574
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 389..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 65534 MW; E2E871CBE6F2CB55 CRC64;
MATIPIVIKH QGKKYNVDLD TASNGEMLKL QLFSLTGVEP QRQSILIKGG KLKDDTDLSK
LNAKPGQIFT MLGTASSEGS SLAAPVEKPR FLEDMTEAEA AAQEGATPAG LENLGNTCYL
NSTLQVLRSI PEMQDELKAY NPDHSDVRSN SDEMSRLGLG ATGASNDLTG QLRDLYSRMS
NTQRSLAPLM FWNALRVIYP QFAQRAKNGA GFAQQDAEEA WSQIIHQLRQ NLKITEKSSS
EENKAKKEVV FIDRYMAGAF HSSLAPPTEA AENEPVVEAD DVFLKLDCHI DQSINHLRDG
LLAGLTEEIE KNSPTLDRNA IYTKTSRVSR LPKYLTVHFV RFFWKKDVQK KAKILKKVTF
PEEMDAVEFC TDDLRKRLIP VRDKVRDIRK DEQDVERARK RQKLRHKQEE DRKHDEALKE
KEAAPIAKLR EQKDKKDSKE KEPEGGDMDV YKTDAEYEAE RAASIKQAKK ELYALINQQL
ADDAGANKSG LYELRGVITH QGASADSGHY TSYVKKAGKL VDDAQAPGGK RMEEDGKWWW
FNDDKVSEVD TERIMALSGG GESASALILL YKAIDLPTRD ELEQ
//
