ID A0A093YJ25_9PEZI Unreviewed; 1185 AA.
AC A0A093YJ25;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=O988_04127 {ECO:0000313|EMBL:KFX98909.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX98909.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX98909.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX98909.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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|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:KFX98909.1}.
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DR EMBL; JPJR01000732; KFX98909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YJ25; -.
DR STRING; 1391699.A0A093YJ25; -.
DR HOGENOM; CLU_003532_2_1_1; -.
DR Proteomes; UP000029329; 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; 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:UP000029329};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 75..205
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 231..551
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 822..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 135919 MW; 2728A285D77A697F CRC64;
MDQALDGETL SPTGMQVDGD EYVVEPQEGE PDDVAIINTD DDGGLAAPLP TADNYEAMKS
VVLPRLVEDP EILADAVHTW HIENWTELSR KEHGPVFEAG GNPWRVLMFP SGNNVEHCSF
YLEQGFEEGK VPDDWYCCAQ FSLVLWNPND PSLYTSHTAH HRFTKDEGDW GFTRFVELRK
LFNVEWDSSG RPLVENEAAN MTAYVRVVKD ETGVLWHTFN NYDSKKETGY VGLKNQGATC
YLNSLLQSLY FTNAFRKAVY QIPTEDEENL ANSAYTLQRL FYQLQTSPTA VSTNELTKSF
GWETRHIFEQ QDVQELSRKL MERMEEKMKG TEAENVLPRL FCMKVKTYIS CINVDYESSR
VEDFWDIQLN VIGNKDIEES FKDYIGVEKM DGENQYFAGE VFKLQDANKG VIFQSFPEVL
HLQLKRFEYD MERDATMKTN DRYEFPETFD ASPYLAEDAD KSEPYIYQLH SVLVHSGDLN
AGHYYAFIKP TKDGCFYRCD DDKVIRATMR EVLEDNFGGE VDYVNGQTKP AFQKPPVIRQ
NSAYMLVYIR RSRLDQVLLP VTKDDTPSHL QKKLDEENAL REARRKEREE QHLYLNARVM
TDRTFREHSS TDLTTFDASE KEPGCAKNFR VLRSSTVKDL AARVGADIGQ DPRRIRFWFM
VNRQNKTVRP DQPITDVNQT VEQAHQKLSG TKTQEIRLWA EEAEEVDSTG EPIWPGLSAQ
QTNGSLKSDS ILLFLKWFDI DNQALKCIGH VYIGKERKVE DLVPLILQKM GWPEKLPSGD
RTQLKLYEEI KPQMIDPMKG KQTLKAAELQ DGDIICFQRV SGAKSEHDKE PKNNRNLASL
SSSTDLSNNA SRSPSNSVAP RASDFIEDAQ LFYDYLLYRK IVHFLPYSKT AVDRQYALDI
ELSSKYTYDQ IAAKVGEKIN VDPTHLRFHT VNATTGAPKA PVKRSLNHTL QNILTPPYTT
FGNNNQRVDE LYFEVLEMSL SELDTKKSLR VIWLSEGITK DETFDILVPK SGNVTDLISG
LIKKAKLDDE ETAGPIRVYG IHNNKIYKEM NPEYSVASIS EYITLVAERI PEEDVDVDPA
HFIQAFHFQG EPNKPHGIPF KFSIRRDEKF SETRKRLEKR TGIKGKNFEK IKFAVVKRSS
YSKPTYLEDD DLLWDVATND DDLLGLDHID RTRLARNGAV DLFLK
//
