ID A0A1V6TJR9_9EURO Unreviewed; 882 AA.
AC A0A1V6TJR9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=PENSTE_c005G08352 {ECO:0000313|EMBL:OQE26406.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE26406.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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:OQE26406.1}.
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; MLKD01000005; OQE26406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TJR9; -.
DR STRING; 303698.A0A1V6TJR9; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000191285; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 426..797
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 97023 MW; D5E8A4B365939820 CRC64;
MNHHLPPMPH GQPPMPQGRR QQDFAYNSGH PNMRSPPYMA YPPHMNGMNG MNGMNGMNGM
NGMNGHMPPA YSPQQFSPWY PPYGHMQLPP RHFQSQPHYG PMIVSSYPPS QPMMTPNHVP
PHSLPMQPRT TTPLQPNMSP SVHAVPLQSD IQDHPALPVQ APQHYPAATP PPRWEPKTIP
EPEVTESELK IPFAAPVPWL SVPEVPFPQR LRTRRRSARP MISALEFPKK DGKHIIGEKK
VEDEVKPAEI AANVTSEPQT PTTSIHQSET NSTQPTTPSS TTKSQTQQTQ QTQQKSTKPA
PVVPVVPTIP GTPRRQANKD SSSVGSETPK STTADSEQDS SPATEASTKP TSPVRAAPKS
WADLVRTKAA AAAAAQAAAA SPVSAPASSE SATVAAPKSE SIGDVLSSLG EDVTQYSDKI
AFLEPRGLVN TGNMCYMNSV LQILVSCVPF YQFLEHVGRR AVHSFKSDVP LIDALIMFMR
EFRAIDAATS EEQLKMRLKP TELEQYGESF VPEFVYEMIR QLPRFRDMRR GHQQDAQEFL
GFLLEEMHEE CDRAAKHVSK TGAAQDSADG SSGDGWLEVG AKQKSAMTQS SGIIAVESPV
TRIFGGKLRS EFKVPGNKPS VTMEPYQPLQ LDIGAPDVHN ILDALRGLTK PENIQGDFNS
PRGPNVTATK QMFIETLPPV LILHLKRFQY DSVTGATQKI WKKVGYPLDL ELPREVFPAH
RRNAMNAHGG LPKYRLMGVI YHHGKNASGG HYTVDVRRQD GREWIRMDDT VLRRVRSEDV
AEAGGEEDPK VLAAALEQHS KQDKNTSANI FDHIDQDEME SADNDKGWSQ VNGTGSNGHA
SKKSVNGVAP TSGPSSGIRT PLGRYGSRDN KVAYLLFYQR MA
//
