ID A0A1V6PRR4_9EURO Unreviewed; 831 AA.
AC A0A1V6PRR4;
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=PENANT_c045G08321 {ECO:0000313|EMBL:OQD79719.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD79719.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
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:OQD79719.1}.
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DR EMBL; MDYN01000045; OQD79719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PRR4; -.
DR STRING; 416450.A0A1V6PRR4; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000191672; 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:UP000191672};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 379..751
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92348 MW; 5192E334D117A171 CRC64;
MQHGQPMPPQ RRQQDFPYNT VPPNMRSSPY MGYHPHMNGH MPQSYAPQPY PQWYPPYGHI
QQMPQRPYQP HPYSPMIVSS YPHSQPVMVP THLPPHSMSM QQRIPTPLQP TMSPSIQIPS
LQPEMHEHPA VLPQPVPVYP VASPSPRWEP KSSLPPKPDF TAPLPWLSVP EQPFPPRIPR
RRRKGRAMQY SLELPDKDAQ KGIETNNLEE TKLSSSIQVP SEPQTPTTTF QQSDTDSTQP
TTPSSTARSQ APSKSSKPAT APVVPVVPNV PATPRRHTKG SSSVTSGTPK STAATTVETE
ADTAPVTDTK KSSPVPAANK RWADLVRSKP SAKPAGTSAP APATTNGVPQ KSESLADVLV
TLGEDVTQYS DKIAFLEPRG LVNTGNMCYM NSVLQILVSC TPFFQFLDHL GRRATHSFHS
DLPLIDAMIM FMKEFRVIDA ATSEEQLRLR LKPTELEQYG EAFIPEFVYE MVRQLPRFRD
MRRGHQQDAQ EFLGFLLEEM HEECARASKY TSIKTQESDD SGADEWLEVG HKQKAAVTQL
SGSIAAESPV TRIFGGKLRS EFKVPGNKTS VTLEPYQPLQ LDIGAHDVHN ILDALKGLTK
PESIQGDFNS SRGPNVTATK QIFIETLPPV LILHLKRFQY DSITGATQKI WKKVGYPLDL
ELPREVFPAH QRNAMAAQGG PPKYRLMGVI YHHGKNASGG HYTVDVRRQE GLEWIRMDDT
IIRRVRSEDV AEAGGEEDPK VLAAALEQHK QNKTPNGNIF DHIDQDDMDS ADSDKGWSQV
NGNGINGHAS KKSVNGVTPS PGQSSGVRTP IGRFGSRDNK VAYLLFYQRM D
//
