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}.
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; 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
//