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Database: UniProt
Entry: N4TRV1_FUSC1
LinkDB: N4TRV1_FUSC1
Original site: N4TRV1_FUSC1 
ID   N4TRV1_FUSC1            Unreviewed;      1056 AA.
AC   N4TRV1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=FOC1_g10006909 {ECO:0000313|EMBL:ENH65524.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH65524.1, ECO:0000313|Proteomes:UP000016928};
RN   [1] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
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};
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DR   EMBL; KB730492; ENH65524.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4TRV1; -.
DR   STRING; 1229664.N4TRV1; -.
DR   VEuPathDB; FungiDB:FOC1_g10006909; -.
DR   HOGENOM; CLU_005922_0_0_1; -.
DR   OMA; PFVHTYE; -.
DR   Proteomes; UP000016928; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ENH65524.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016928}.
FT   DOMAIN          382..510
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          679..1053
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1056 AA;  118237 MW;  8258BF37643D4C06 CRC64;
     MASLGHSRAS SVATAGSHSL GSPGAFNHGS IPGGNRGGES PSKAPIPHID DVLAARNLDR
     NVSVRKLLES AEASFKQAEI AREFRRPAIA LNEYIRASII AVQFITNHPE YHDLKTSHGD
     FVKAHNNLLT KISQQDHIYA KIKADIIADN KRSGVQPRTV RPNSSQGGSR PHTPSKSTAE
     RPISPSKHRF DGHDTNGSPA RAKPAIQPKP QSLHGNAIKP GAQRASINGV QDLATRFANL
     RGPQPSPGQD PRIKTHQITL PKPMGPRDMP PPRPPKVGID TSVPTLPKMP DAIYSPARGS
     ISGEVTRPPS STPRSMYRTA STVSIPGTPT GSSQSQTDYF VPTQSYSNNS IPPVPPSNLN
     GSVKIPEGDA ISPEELYQAM KAKGGILIID IRMRDDFNEG HIMSSSTICI EPSILLRDNL
     SADEISESLI LSPNQEQSLF EQRHTYDLVV FYDQDSEEIP EHPRNSDDLV IISLHRALVH
     FNFMKELKNT PKILKGGLDA WVDLMGPASL GSTTSTTNKT VHLERNRSRL SAIERRRSKY
     IAKPLKPDEV KVWQETLKND DDMQTASSPN FTRTTEDFLR RFPPVSLEQE SMTSPEEKPR
     NRPVYGLSHK VDLYTDLPSP PTRPAPALPR RSYSGLTEGR DENELYGNNN AVVPARPSRA
     PTMKAVEHQS TGDSAKFYTG LNNPNNWCYA NSTLQSLLAS PEFGRELANS EWVSKYKAPM
     KDDEKIEQPQ LMIRIISNLF HWMSSGKFQV MMAQTLMNYS HHVCTQSRSI EQFGGSQQQD
     AQEFMSFVIT HLHDETNTRR DRKGTAAQPD TKHQSLVKAA VQYWQNHLEY NRSIVDRYWR
     GLELSTVECF ECHTRTYQFN PIDVVPVTVG MGRGMTLEQV LDQYTSGNII NDFHCDHCRH
     PTRAQQSLSF ARFPSLLCVV FRRFHYQHDS SDLRKSTAPI TWDFNDTDFT RYFLPPGSRE
     SSSGFDPMDP AFTGPFRYEA YAVIVHTGSR TDNGHYLAYV RDSTSHDPYA WFCCNDSRVT
     KVRIGSGDRD DVQEEVFKSG RDRVPYLVFF RRKGMR
//
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