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Database: UniProt
Entry: A0A0W0FU63_9AGAR
LinkDB: A0A0W0FU63_9AGAR
Original site: A0A0W0FU63_9AGAR 
ID   A0A0W0FU63_9AGAR        Unreviewed;      1126 AA.
AC   A0A0W0FU63;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=WG66_7596 {ECO:0000313|EMBL:KTB39895.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB39895.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB39895.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB39895.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-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   -!- 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:KTB39895.1}.
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DR   EMBL; LATX01001627; KTB39895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0FU63; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   Proteomes; UP000054988; 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; cd03775; MATH_Ubp21p; 1.
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; 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:UP000054988};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          69..201
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          227..546
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   1126 AA;  129541 MW;  72400ECB7E1F4CF1 CRC64;
     MEENRAQDLR KSGAGFSRSL RIMNDNMEAL DEKANGGPSM EAEEAVSVRN HEAFAAKHMP
     DLGHDIKDLQ VFTWRLEHWK KLEKKITSPE FECGGHKWRI LLFPFGNSNA PPNDTVSVYL
     DYAEPKKAPE GWHACAQFAL VISNPHDPTI YTVSHAHHRF IAEECDWGFT RFSELRKLFT
     PQENHARPTI ENEAADISVF VRVLEDPTGV LWHNFVNYDS KKETGFVGLK NQGATCYMNS
     MLQSLYCTRY FRKAVYQIPT EDDHPTESVA LALQRLFYHL QTSDQPVGTT ELTKSFGWKS
     LDAFFQHDVQ EFNRVLMDKL ESKMKGTKAE GAIAKLFVGK MKSYIKCVNV EYESSRIEEF
     NDIQLNVKGL KNLYESFKDY VAVETLDGEN KYQAEGFGLQ DAKKGIIFES FPPVLHLQLK
     RFEYDIQRDA MVKINDRHEF PFEIDLSEFL DTNADRSKPW VYKLAGVLVH SGDLHGGHYF
     ALIKPDRETR WLKFDDDRVT PVTDKEVLEE NYGGEVLNGL PATLQRNQVR AMKRFTNAYM
     LVYIRESAMD EVLAPFTEED TPPHLKRRLD EERLQIEAKK KEREEQHLFL TAKVITDETF
     AQHEGFDLAT FDEKNWPPSE LPSFRVLKTE TYSTFKNRVA QHFKIPDNQV RLWVLVNRQN
     KTVRPDTHIP ENEPTLTVEL IRNNMAARQN DLRLYLDVIP DPTKPDPPQQ SIMIFLKHFD
     TSKQTLFGAG KVYMLRTSKV ADLVPIINER MRWAPGTALK LYEEIKPGMI ELMKPKLSFA
     QSEIQDGDVI CFQVDLPERE IHDLESQGLY SNPMQYYDFL QNRVMIIFRP KNEEPDHDHP
     EFSLVLSKKQ NYDTMSMKVG DSLRHDPIKL RFTTTNAQNG TPKNVLKRSL NQSIAEIMAP
     YYTTSAVILY EKLDVSIVEL ETKRQLKVIW TGIHNKEEGS YPFLLPKTSS VHDLAENLAK
     KVTLAPGGTG KIRIFEISRD GKTQKEFTGS EMIGNIPDPV ELYAEEIPRE ELEADDSDKV
     IGVFHFSKDL SRTHGVPFKF VVKRGEKFTE TKKRLQARIG VSDKDLAKYR FAIIQVSTFK
     QPSYIEDDDT IYEHQFAPED VLGLDHVDKS GKARTGSGEK AIVIRG
//
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