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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//