ID A0A2K0WLQ7_GIBNY Unreviewed; 858 AA.
AC A0A2K0WLQ7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=FNYG_03522 {ECO:0000313|EMBL:PNP83200.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP83200.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP83200.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP83200.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-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 -!- 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:PNP83200.1}.
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DR EMBL; MTQA01000054; PNP83200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0WLQ7; -.
DR STRING; 42673.A0A2K0WLQ7; -.
DR OrthoDB; 1353379at2759; -.
DR Proteomes; UP000236664; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02670; Peptidase_C19N; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000236664}.
FT DOMAIN 136..606
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..841
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 96195 MW; 1B0D111DA305F3D1 CRC64;
MKEFPRKFLS KREKNGRRSK SATPAPVVPT VPDSTSSKNK PRPLSAGAFM ALFKNDSAKQ
GAKAEADKEK DTAQIEDILR RLDELNITNV TADHVTDIMG TKFADHDPKK TVEFIDMEQK
AAAGIITPYD PSVDMVGAEN RGNVTCYLDA LLFSMFAKID AFECMLKNDF PEEDNRNKLV
NLLRMWVNML RTGKLVHTDM TKLIQDALAD CGWSDARMLE QQDTSEAFAF ITETLQLPLL
SLQVDLFHQG KKDKDDHKVV YERLLNLAVP PDPEEKGLKL EDCLEEYFNA QVDVKRDSED
GKKLGVEEKS RSEAPTLKHR DTIRIITEER GEASTPTSPL VNTPSEITPT SEKGVSLLLA
DPNVKDGNTP DDEEEGEVTT VEIVKNKPSM RTRSTSVIQR VVLDEDGRPS TPDNVTMLQK
AMRKGSTVVK AVTIPAWQFF RLIPWHALSS SEPRNNTEVA LNFEQRPVVG ICLKRYAMTE
SGQPKRHNTF IDIPDSLRLP HFMLADEPKA EEDMNVLNTD YKLVLQSVIC HRGDSLQSGH
YVSFARVAPK LLKDNRRHNF DPPPDYEEAQ WVKFDDLQIE NRVSYVEDIR SALKEEMPYL
LFYQIMPMVE VSPPSVDETE TEPPSYNDSK ISIELPPTPS QSNRLGSLEG GYFDSTPTLE
NSQLLSSKPP SIRLSMEGER PRRSEDIDRN PGSLAGDSRR PSAVWTDSTI HTPNSHSPAV
TPNEESTASR LSRAASRFTL VNRSRPSSQN GENRISFSMS RLGGLMRPSK EPLAEPKDEP
NGIGMSSANS TGVLTAEISK ESRESKDAVD GTEQLAEPEP EQHHHRHHGH KHGHKRVKSK
DKVKNKSGDQ PERECTVM
//
