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Database: UniProt
Entry: A0A317SEH9_9PEZI
LinkDB: A0A317SEH9_9PEZI
Original site: A0A317SEH9_9PEZI 
ID   A0A317SEH9_9PEZI        Unreviewed;      1140 AA.
AC   A0A317SEH9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=C7212DRAFT_285793 {ECO:0000313|EMBL:PWW72755.1};
OS   Tuber magnatum (white Piedmont truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW72755.1, ECO:0000313|Proteomes:UP000246991};
RN   [1] {ECO:0000313|EMBL:PWW72755.1, ECO:0000313|Proteomes:UP000246991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=091103-1 {ECO:0000313|EMBL:PWW72755.1};
RA   Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT   "Genomes of Pezizomycetes fungi and the evolution of truffles.";
RL   Submitted (MAR-2018) 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   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWW72755.1}.
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DR   EMBL; PYWC01000094; PWW72755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317SEH9; -.
DR   STRING; 42249.A0A317SEH9; -.
DR   Proteomes; UP000246991; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR024729; USP7_ICP0-binding_dom.
DR   InterPro; IPR029346; USP_C.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE K02C4.3-RELATED; 1.
DR   Pfam; PF00917; MATH; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF14533; USP7_C2; 1.
DR   Pfam; PF12436; USP7_ICP0_bdg; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246991};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          73..201
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          227..547
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   1140 AA;  131526 MW;  9B0A88CA71DCA2D0 CRC64;
     MGVIQEQPDD QAMVIDGLDQ DNGKTQDVTI ISPQQSIDSG SADDKDSIVL ADDHEAMKKI
     LLPDIPDLET EDETTYTWKI ENWRKMERRS RGPVFHCGGA PWRVLFFPQG NNCDFTSFYL
     EQGFDEKPPE NWYKCVQFGL VLWNPNDPSV HVTHQAHHRF TVDEGDWGFT KFYELRLLMS
     PTKERARPLV EDESANLTAY VRVVKDPTGV LWHNFLNYDS KKETGYVGLK NQGATCYLNS
     LLQSLYFTNS FRKAVYQIPT ENEPLSNSAL TLQRLFYLLQ TSNEAVGTYE LTRSFGWETQ
     DIFAQQDVQE LNRILMESLE QKMKGTQAEN SLAKLFVGKT KTYIKCINVD YTSERIEDFW
     DIQLNVRGFK NLDESFKDYI AVETMDGENK YFAEGHGLQD AKKGVIFESF PEVLHLHLKR
     FEYDLNTYAM QKVNDHYEFP EEFDAAPYLS EDADQSEPYT YALHGVLVHS GDLNAGHYYA
     FLRPEKDGRF LKFDDDRVTK ATLRETMDEN FGGDYGPATN GLPRNPQARA ISVKRSMNAY
     MLVYLRKNKI DEILPAVTEE DTPPHLQKKL DEERATRELR KRERDEQHLY LNVKVITESQ
     FKAHQGFDLT SWDDKDQPEE AQPRHYRVLK ASLVKDLVEK VAADICVDPC NVRLWIMVNR
     QNKTVRPDQP LTIPEMSIED ASNKHNNKSS DFRLWAEVAT ENKPGKNLEP WAQARDSNSA
     WIVVFLKRYD PGSQTLRGVG HLYMRKNDKV AELIPAILTE MNWPRDTPLK LYEEIKPQMI
     EPMKPKQTFN QAEIQDGDII CFQKSYTEKE AQALFRESLI PDAKDFYDLL VNRIVIKFHP
     KSSHIAEGKV FDLTLNKKMT YDQLAEKVGD FLDAPPTHLR FTTINAATGG ARSTIKRNPN
     ATLHQMLTTT YYSNTTISPN SLYYEVLELS LTELETMKTL KLFWLPEGIV KEELVEILVP
     KNGQVQDVAA ILQKKLELDD ETASKLRFYE SHLGRFYKEL EPAFNVAGIQ DYMNLLAERR
     PNEELEMEEG DRFINAFHYH KEPSKAHAFG IPFRFVVKQG EIFEKTKERL QLRTGIKGKP
     FEKIKFAVVR KSNVPKPIYL SDEDILADVA SETDDVLGLD HIDKNSRTWG RSGGPEIRIR
//
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