ID A0A2H3TNT1_FUSOX Unreviewed; 1460 AA.
AC A0A2H3TNT1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=FRV6_07646 {ECO:0000313|EMBL:SCO83433.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO83433.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) 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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; FMJY01000004; SCO83433.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10013859; -.
DR VEuPathDB; FungiDB:FOC4_g10011469; -.
DR VEuPathDB; FungiDB:FOIG_12166; -.
DR VEuPathDB; FungiDB:FOMG_05168; -.
DR VEuPathDB; FungiDB:FOXG_01907; -.
DR VEuPathDB; FungiDB:FOZG_05339; -.
DR VEuPathDB; FungiDB:HZS61_009819; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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:0000313|EMBL:SCO83433.1}.
FT DOMAIN 82..202
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 429..1228
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..998
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 162192 MW; A7F56B04994E3C95 CRC64;
MNGDADLPQR SSSPLKRRAS SMDPENDADR TRDVDMGTSQ ANESIEGASQ LAPESLPRDM
SVEAPEPTAN SATDAFPAQP IPSLQEQIKI IETLLKAYQE AQVKEGDKAY LVSNTWVQKA
LSLRGGSKDS KEGDSTSDLL GPVDNSDIIE EVVTEPTGKE YIRLKQGTNE NEFTLFPEDA
WKMVVDWYGI KNGQEAIIRA AINTAEPGEE PVIQFEFHPP VFTVHRLWSE ISPLPIEQSL
KAKNPPPYKF VRSRKYHAQT FVKEIKTATG VPLDRKIRLF MVPQVQQVSG PSEPSRALTP
PDSPGRTHNG ASSTDTWSKL LLDNVSFSQV RDQRVKCKLE DKTIDPKFNG SSNLTMFDLV
TDQTLVIDEA IDSFWVSNYT GKTPPNGLAI PTRSGLASSN ASGRSSPAPG GPLTRGRTGK
KPGRSIGVVG LQNLGNTCYM NSALQCVRSV EELTKYFLTN EYLDEVNKTN LLGYNGKVAI
TYGNLLKEIY TEGRGSVTPR DFKNTIGRCR STFSGYGQQD SQEFLGFLLD ALQEDLSRVK
KKPYIEKPDS TDDMINNPEA IKEMADKVWD ITRLRDDSVI ADLFTGLYKS TLKCPECGKI
SITFDPFNNL TLPIPVEDVW MAKVKFLPLN DVPVMFEVEL PKHSAIEQLK QFLSARTGVP
VERLIGGEEY KDRFFKIYDN NLDVSEEIAK NDLATFHELD AVPTNWPHKA SKPRSMLDID
TPLEAPWNDP RYERIVVPVF HRIPSNYGRA RDGVAPPSFI CFTKEEASDI DLIRRKILEK
ISNFSTWSKL RNGPEENSDN ADGEVVASDA DSSGDSKVVA NSVEGEDDIV DVHMKDTSEA
LPHQPQILKR FNKSRPKFIG PDSFLEPELQ NLFDLCYFTD KAYSGDVPTG WSNVDHHQLL
PKLSDRIPQP SPEDDDTASR DDESSTPSNE DASSNDESIK AETTQTRMVE ESSEEEVQEA
PRKFNGRPSK VKGRKLKGQK FNKKANKRRE RMQNKKHKAA SVKPQPQPPA VADGGPLIRL
GEGIVVDWNE DAWEKVFGGA AKILADEQGA PTFIDLEMLT DPALKIAQRR RHHRRTRGIS
LEECLDEFER AEVLSEQDMW YCPRCKEHRR ASKKFDLWKS PDILVAHLKR FSNSGWRRDK
LDVMVDFPIE GLDLTSRVIQ KEDGKDEIYD LIAVDDHYGG LGGGHYTAYA KNFVDGRWYN
YNDSSASPVS DPSTCITSAA YLLFYRRRSS TPLGGSRFGV ISEKYKNSEE NSEEEEEEGE
VGEGQRLGEG SSLNGLSSAG IGAAATRHLG GRGSDRITVT SLAGPDDEDE DLPPYDGANR
IESIHSTVED EGVDINGSYQ RLDNKSLNLV QGWNFEGLGD SGAEDSTGAD IGSDDVQLDS
SADERGLSQF DDHDTIMTGQ DPAEGESEPA APQTTILTDT QKSTWDRKDV IDVQTAAGSD
RDSNEVAEIH LENEKGIKAE
//
