ID A0A2L2TIG8_9HYPO Unreviewed; 618 AA.
AC A0A2L2TIG8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI40127.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) 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 ---------------------------------------------------------------------------
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; LN649232; CEI40127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2TIG8; -.
DR STRING; 56646.A0A2L2TIG8; -.
DR OrthoDB; 74526at2759; -.
DR Proteomes; UP000245910; Chromosome iiii.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02660; Peptidase_C19D; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000245910}.
FT DOMAIN 280..615
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 70926 MW; CD145EDA76AF547C CRC64;
MYLFRQSQPT SPSTEKDEQL SDFRPVPRDS DPRRIIKKHR YNRNRVTYWN YLPYDTIPAG
VVPLDKFRVV PLLELPFINL VLQELHILAQ VEPITKTQSP IMSARPTTPA SPKNVRVKSP
VPGLPMFGCE HIQLLLSKNQ EVMNSSITHY KLILRGIFDA TPIVPQTSTL DGRPVTSLTS
NYLCLQCPST VTEEERLRHG TKKQHRFYVD SRSGCLYCQI CDDYIWDPTL EELRVRKIGT
GSFSGRKRKH DELFTGSFKD DPRFISNNTN TASCRANGLR GIYNAGATCY QNVVLQSFLH
NPLLRNFYLS DGHQSSDCQV PHCLSCAMDD MFQDFYALET TNGYTAANIL SGFWISEKKA
FENLVTTKEQ DAHEFFQFLA EELHERNGDG KKPEIGSEHS CNCIMHQTFY GKMQTTTTCQ
NCSGQSNSIQ SFLDLSLGLE NVVQKKSKRT GQKKPTVSLQ DCLDEEYIKY DKCEYRCNNC
NGTQQAKRHT SIKRLPNVLS IQLKRFEYRH GRHDRAASKV DNEVKFPLQL NMMPYTNRVR
NHDSRESLEL ERSCTYDLLS VVVHVGELDT GHYTSYCRVG DQMKKWFKFN DHKVELASLS
DVLGAQAYLL FYIIRSLA
//
