ID A0A0G2FAK8_9PEZI Unreviewed; 395 AA.
AC A0A0G2FAK8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=UCDDA912_g08824 {ECO:0000313|EMBL:KKY31221.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY31221.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY31221.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY31221.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY31221.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY31221.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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 -!- 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:KKY31221.1}.
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DR EMBL; LCUC01000405; KKY31221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FAK8; -.
DR STRING; 1214573.A0A0G2FAK8; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02257; Peptidase_C19; 1.
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; 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; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KKY31221.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..395
FT /note="ubiquitinyl hydrolase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005181977"
FT DOMAIN 1..394
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 137..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 43944 MW; D139841491865CCF CRC64;
MLTRMFSAQV LQLLLFCTPF YNFLDQVRKN VVHSFKLSSK TPLIDAMIGF ISDFRSINSA
DSPDQLQRKL KPEDHHHLGK AFAPNGVYKV VRELERFNTV KPGSQHDAPE FLMLLLNGLE
EECERMIRDS ATFASGSDQA SLDQHDVNGG ADASDDWTEV GQRQRLAVSQ RSGPAIIPNP
ISKIFSGQHR EVLRLSRKES VTYNAYQNLS LAIDDPSIKT VIDALKYFHR SEPITSKNSQ
GVEVNGTKQT LIETLPPILI MHLKRFYVNG GEAEKTWKVD GQEWLRFDDT IITRISGEAV
AEAGVEEANH KAAAATKHER ANDTSNNRFA AMGEDDAADN DGDWKQVGPG ANGAKKYSGG
VNGSSSGTST PKSKPIRDHK DHNKVAYLLF YQLWN
//
