ID A0A178DTI7_9PLEO Unreviewed; 1132 AA.
AC A0A178DTI7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=IQ07DRAFT_546259 {ECO:0000313|EMBL:OAL47000.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL47000.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL47000.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL47000.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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; KV441653; OAL47000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DTI7; -.
DR STRING; 765867.A0A178DTI7; -.
DR InParanoid; A0A178DTI7; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000077535; 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:OAL47000.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 64..194
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 220..542
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1132 AA; 130052 MW; CC769CAFA874615F CRC64;
MDQIGSDMLV DADYDEKHDV AIITPDTDDQ MDEADAEPEP RADEYEAFLN KHMPELPEHE
TEAQVYNTWE IREWRSLTRR EHGPLFECAG HPWRILFFPY GNNVDFASFY LEQGYEENQI
PQDWYACVQF MLVLWNPKDP SMYTTHTAHH RFTAEEGDWG FTRFAELRRL FSNSWDDRGR
PMVEDNAANV TAYLRVLKDP TGVLWHNFIN YDSKKETGMV GLKNQGATCY LNSLLQSLFF
TNAFRQAVYQ IPTAEESDRS NSAYALQRLF YLLQTSSNAV GTTDLTQSFG WDSKQIFEQQ
DVQELSRVLM DKLDEKMKGT EAEGALTKMF VGKMKTYISC INVDYESSRV EEFWDIQLNV
SGNKNLDDSF KDYVQVETMD GENKYFAEGF GLQDAKKGVI FESFPPVLHL QLKRFEYDFQ
RDAMMKVNDR YEFPETWDAA PYLSEGADRS ESWKYHLHGV LVHSGDLNAG HYYAFLKPTK
DGHYYKFDDD RVTRATLREA LEENFGGDYA QANGNAGQRN PYTRAWSSKR SMSAYMLVYI
RETRLADVLV EGKDVTPPAH LAERLAEERA AFEKRKKERE EAHLYMDVAV ASENNFRLYQ
GFDIVPWKGE TDLEASPKIY RILRATTMAD FAKTVGEDLG VDADMLRPWS MVNRQNGTVR
PDTALEFPDM TVEEAANKHG TKQAQFRLWI EKAEKRDENG VPLFGDRMLE LKSAQTNRPL
MIFLKHFDAK TQSLFGIGTF YAAVQDKVSD LSPTITKLLG WPSGTPIKLS EEIKQNMIEA
MKPKSTLAAS EIQDGDIITV QRVLSDKETS QITASGGYVD AKDFYDYLLN RISVEFVPRV
AEPTDLPTFT LTLSKKMAYD QFASKVAEHL KTDAGFLRFT TVSTTGKPKA TIKYNPSSTL
NTLLFPSPYN YSPATAQRPD AMYYEVLDMS LKELEQRKPI KVTWLPEGLN KEEEYTLMVP
KNAQVSDLLE ALQKKANISD EVMPKVRAYE AHMHKFHKSL PPDFQVISLY DYTQIYVAPF
PEDESTKKIL VFHFDKEPSK AHGIPFQFSL KEGEPFSETK QRLSDFTKIK GKQLDKIKFS
LLSKTQYSKP EYLDDEEILT GLIGTREDVV LGMDHTNKSR SFWGKSDSIF IR
//
