ID   A0A2D3UV67_9PEZI        Unreviewed;      1178 AA.
AC   A0A2D3UV67;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-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};
GN   ORFNames=RCC_07446 {ECO:0000313|EMBL:CZT21582.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT21582.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT21582.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT21582.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; FJUY01000011; CZT21582.1; -; Genomic_DNA.
DR   STRING; 112498.A0A2D3UV67; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000225277; 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 7; 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, ECO:0000313|EMBL:CZT21582.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225277};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          77..208
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          234..558
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1178 AA;  134881 MW;  7B04F97187CE9E1A CRC64;
     MDNLGSDMLL DSDYDEKHLT PTEDDNDNVA IISPDDADSM VDDTDTASEA APPRADNWEA
     MRDRFLPIVP DYETADEQVH SWDITDWRSL PKRSHGPVFH CGGHPWRVLF FPAXNAAQES
     VSFYLEQGFG DDKPPDKWYA CAQFMLVLSN PNDPSIYIHH EANHRFTAEE GDWGFTRFAE
     KNRIFASKFD NFDRPLVEND CARVTAYVRV LKDPTGVLWH NFINYDSKTE TGMVGLRNQG
     ATCYLNSLLQ SLYLTGAFRK AVYQIPTETP QDREASSSAY ALQRLFYRLQ ADQVAVGTQE
     LTVSFGWESR QIFEQQDVQE LSRXLMEKLE ARMKGTEAEN ALPNMFVGKM KTYLRCINVE
     YESSRIEDFW DLQLNVSGCR SMDESFKNYV EVETLEGDNK YAAEGYGLQD AKKGVIFESF
     PNVLHLQLKR FEYDFQRDAM MKVNDRYEFP EIWDASPYLD DTADKSEPYI YHLHGVLVHS
     GDLNAGHYYA FLKPNKGGDF FRFDDDRVTR ATKREAIDDN FGGDYSATTG AKGGHNPYTR
     QWSTKRSNNA YMLVYIRESR LDEILLSEED VKPPAHLPTK IMEERALAER RRKEKEEAHL
     YMSVLVATEE NFKSYQGVDL VPWSSDDAED PATPTTHRML RSMTVAEFTH SIAQHLGKEA
     DLLRPWIMVN RQNGTVRPDQ PLSWQEMTLQ EAADKFSTRT SPFRVFMEET TRDDQGQPIW
     PPDDLPASPG SVQASQPHHP IILFLKHFDV DRQQLQGIGH VYMSPLDRAC DVAPRILDMM
     GWESGSVDLE LFEEIKQNXI EPMKPKNTLI NSEIQDGDIL VFQRHLDDAD AATLKQKNPT
     ACQSTPLFYD FLMNRLFVNF TPKNIPAPNL QFVKEGVEQF SLALSKKDTY DVLAHKVADY
     LSSXNANPVD PSHVRFSTTH AQSGKPKNPI KKTQGTTVNT ILFGSSGYGG YSYAPAHATD
     HLFYEVLDIS LSDLEQLKSI KIVWLTEGIT KEEPTEVLVP KQSQFSYVLD ALHKKLELPD
     EILDQIRFYE VHSSKVYKIL PLTHGVNALN EFMAVYAERT PEEELXINKE NGDRLLYCFH
     FEKEPSKPHA TPFIFLLKAG EIFKDTKERL SKRTGIKGKS FEKIRFAVIK NGQNYSKPVW
     VEDDDILSDK LGPDDHLGLE HPNKARNDWI KYQSLNIR
//