ID A0A2L2T2V9_9HYPO Unreviewed; 623 AA.
AC A0A2L2T2V9;
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=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI64028.1, 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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; LN649229; CEI64028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2T2V9; -.
DR STRING; 56646.A0A2L2T2V9; -.
DR OrthoDB; 1204714at2759; -.
DR Proteomes; UP000245910; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02662; Peptidase_C19F; 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:SF945; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 11; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000245910};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..619
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 191..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 68763 MW; 24BB1B6F3A45FFCC CRC64;
MHDKNTSVVS YAAGASLAAA ALIYVFAPNF SIDHDATSSK KKTIVGLRNQ ANDCFINSVL
QALAGLGELR VYLIRETHRR HIEDPAVYAR LVQPEGKEIP QWKLQGLQEG LVTQGLKEML
DALNERPIYK KSISPFPFVK VLEAAFKQRI SRQQQDAQEF LQIVAERLKD EYHCGQRARL
HVRRRGLFPT NSATNIDKTA EDQANGNGSD ESSQEQQPTT NGDSNSAIEP SEETEISQVD
GQLPLEIEEG FPMEGKYESH LKCLTCNYKT KPREETFCTI TLAVPQVSGT TLNACFDGIF
KSETIDDFKC EMCRLLQTKA DLEAEMAKST SESFKAQAQE NIDRLQHTID TDPENPPEDL
DLGDSRYAPK RKIAKTTRMS IFPKILAIHL SRSIYDVGQM TQKNSAKVVF PEQLPLGGLM
DQKKYKLLGL VTHRGGHNSG HYEAFRRQNV PAPFSNPNTF QPSEAFSKTP TPMGTPVLGG
GPTHSPAIST PDLLSGSSGN SSTPSLDSLP PPPRSVPADL RGSASLPAIG KPKDPETSSL
RSVAASTKSA ISKLTSPKQT NSSSTTPKLV PSNVSKRSKK RKATSDKWWR VNDEKVKEAK
TSEVLGMQRE VYLLFYELDK EDA
//
