ID A0A2H3IJ65_9EURO Unreviewed; 754 AA.
AC A0A2H3IJ65;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PENO1_085040 {ECO:0000313|EMBL:PCG93155.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG93155.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG93155.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG93155.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(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 -!- 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:PCG93155.1}.
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DR EMBL; NPFK01000329; PCG93155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IJ65; -.
DR STRING; 290292.A0A2H3IJ65; -.
DR OrthoDB; 1353379at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PCG93155.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 116..542
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 85009 MW; BEDF929E090974F3 CRC64;
MSGIQRFLTK RGERHRRPAK QEKEPPIPGV RSYLRGLVIK SETVPSNDTS DGQKVKALEQ
RLASIGILDL NSAQIQGALS SPYAQGDMEK AFDLLMVIED SIEGILQDYN PDVKLVGAVN
RQGVTCYLDA LLFAMFARLD FFEAILYRPF TDNNDPRRRL VILLRLWVNM LRSGRLITTD
ITEHLQEALS ECGWPEAAKL CQQDASEAFT FVTEKLELPL LTLKMDIYHT GKEDVADDHK
FINERLLEVA IPPEHEDGTA ITLEECLEAY FNNKIEVKRY LERRGTINSV RSFDSSTKAG
TVHVETVEVG SSAPSPIGTS SPKIEYPLAE KFSVSSMLSR RSSIVQERFV PDKGSHDDLV
HPGRKRKGSY RKEVMMPAWQ FFSLIPWYTD NAPMNDAQVA AHFSSKRPIL GMCLKRYSVL
PNGNAIRLNT FIDIPTEIGL PHFIQDDRLD ENGPLYGNFK LSLQSVVCHR GNSVDSGHYI
SLVRGSNIKL PSTSYSADTN LTVENSDLWM RFDDLAADRV TRVSIEEALK EESPYLLFYQ
IVPIDDSFTE ENLSDKRASF ISGSEDLHDD QEKEIFLSAV SLDSTGRDPS SARLSFDLSS
LRPTLDNTET DTGPNVPDRT MTDIKDSAQN NTSLRDAFTA RRSLSIPRRR KESQSRSRSR
GGDQSGEKRL SAFSRFTSRM SKEKSIENPP TNADEHDGQA DTEDGTVPSI SYDEIEIKEQ
ERGRDATINQ NKGKQRRKQS TNKKERPDRE CLVM
//
