ID A0A3A2ZUY9_9EURO Unreviewed; 1121 AA.
AC A0A3A2ZUY9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PHISCL_02461 {ECO:0000313|EMBL:RJE25187.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE25187.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) 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:RJE25187.1}.
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DR EMBL; MVGC01000055; RJE25187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A2ZUY9; -.
DR STRING; 2070753.A0A3A2ZUY9; -.
DR Proteomes; UP000266188; 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, ECO:0000313|EMBL:RJE25187.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000266188};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 65..194
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 220..543
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 129655 MW; 7EE14652488E84C3 CRC64;
MDNVTDSDML VDEYEQYQNN DRTDVVVVSR SGSEEEPEPE PLADDHAAMM SRVLPKDPEL
ETEEETYHTW HIQDWRKLKR KEHGPIFKCG GFPWRILFFP YGNHVEHASF YLEHAWEDEP
PKDWYACVQF ALVLWNVNDP SIYVSHVAVH RFNADEGDWG FTRFCELRKL FSVQWEGRGA
TLVQNDEANV TAYVRVVKDP TGVLWHSFQN YDSKKMTGMV GLRNQGATCY LNSLLQSLYF
TNAFRKAVYQ IPTEAEASRD NSAWTLQRLF YNLQTSETPV STTELTASFG WESRQIFEQQ
DVQELSRKLM ERLEEKMKGT AAEKALPDLF VGKTKTYISC INVNYESSRI EEFWDIQLNV
RGNKTLDDSF RDYIQVETLE GENKYDAGQP YGLQDAKKGE IFESFPPVLH LHLKRFEYDI
NRDAMMKLND RHAFPMEFDA TPYLSNDADK SESWVYQLHG VLVHSGDLNA GHYYAFLKPT
KDGFWYRFDD DRVTRATEKE VLDENYGGEY ELSNGTPGVR QPYTRGLSTK RSMNAYMLVY
IRKTRLDDVL LPITKDEIPA HIEKRLAEDR AEFARRKKER EEAHLYINVG ILSDESFRSH
HGFDLTSQDL PAGDPALPSV YRTLRAQKLS EFAEQIAEEK GLKAEQIRFW VMVNRQNKTT
RPDQVIKDPE STTVEDAYNR FGTKGNAFRI WMEVAEPSAD GTITWPDTNN SVLIFLKHFD
AAAQTLTGVG ATYVRRNQKV SELAPTILDK MNWPAGTEFM LFEEIKHNMI EVMKSKQTFQ
QSEIQDGDII TFQKVVKESE LPETALYQDA RQYYDYLLNQ MSVTFAPIRG GESDGFTLTL
SRKMTYDQFS KKVGEHLNVD PTHLRFAPVM ASTGKPKQFL KRSPQTLFQI LGSQYGNYGY
TLHRSDALYY EVLETSLSDY ESKKLLKPTW LPEGISKEQV VEILVPRNGT ISDLLAVFTK
KANLDEEAAQ NLRVYEAHSG KIYKELGEDF NIAGLNEYVS LYIEKMPDEE VNMDEGERTI
NAFNFDRETT KPHGVPFKFV IKPGEIFKET KERLSKRTGI KGKQFEKIKF AVVPRSLYAS
PRYLEDDDIL SDIVNDDDLL GLDHVNKNRN FWNRSESFFI R
//
