ID X0DBY8_FUSOX Unreviewed; 1477 AA.
AC X0DBY8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=FOQG_00710 {ECO:0000313|EMBL:EXL00630.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXL00630.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXL00630.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXL00630.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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; JH658362; EXL00630.1; -; Genomic_DNA.
DR Proteomes; UP000030663; 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 Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT DOMAIN 82..202
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 429..1245
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..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1477
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..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1015
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1477 AA; 163868 MW; 420D4B96916E7899 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 VKSRKYHAQT 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
PRVGLSISLS NSPSAYTKQK FNGRPSKVKG RKLKGQKFNK KANKRRERMQ NKKHKAASVK
PQPQPPAVAD GGPLIRLGEG IVVDWNEDAW EKVFGGAAKI LADEQGAPTF IDLETLTDPA
LKIAQRRRHH RRTRGISLEE CLDEFERAEV LSEQDMWYCP RCKEHRRASK KFDLWKSPDI
LVAHLKRFSN SGWRRDKLDV MVDFPIEGLD LTSRVIQKED GKDEIYDLIA VDDHYGGLGG
GHYTAYAKNF VDGRWYNYND SSASPVSDPS TCITSAAYLL FYRRRSSTPL GGSRFGVISE
KYKNSEENSE EEEEEGEVGE GQRLGEGSSL NGLSSAGIGA AATRHLGGRG SDRITVTSLA
GPDDEDEDLP PYDGANRIES IHSTVEDEGV DINGSYQRLD NKSLNLVQGW NFEGLGDSGA
EDSTGADIGS DDVQLDSSAD ERGLSQFDDH DTIMTGQDPA EGESEPAAPQ TTILTDTQKS
TWDRKDVIDV QTAAGSDRDS NEVAEIHLEN EKGIKAE
//
