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Database: UniProt
Entry: N1RJW3_FUSC4
LinkDB: N1RJW3_FUSC4
Original site: N1RJW3_FUSC4 
ID   N1RJW3_FUSC4            Unreviewed;       514 AA.
AC   N1RJW3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=FOC4_g10003408 {ECO:0000313|EMBL:EMT66873.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT66873.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
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:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
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; KB726963; EMT66873.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1RJW3; -.
DR   STRING; 1229665.N1RJW3; -.
DR   HOGENOM; CLU_008279_11_2_1; -.
DR   Proteomes; UP000016929; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   CDD; cd02660; Peptidase_C19D; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EMT66873.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016929}.
FT   DOMAIN          179..511
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   514 AA;  58712 MW;  D3D92BA791BBF5D3 CRC64;
     MSGRPTTPAS PKNIKVKSPV PGSPMFGCEH VQLLLSKNQE VMNSSITHYK LILRNIFDAT
     PIVPQTSTQE GRPVTTLTSN YLCLQCPMTV SEEDRLKHGT KKQHRFYVDS RSGCLYCQMC
     DDFVWDPTLE ELRVRKIGTG SFSGRKRKHN ELFSDSMKDD PRYITNNTTT ASCRANGLRG
     IYNAGATCYQ NVVLQSFLHN PLLRNFYLSD GHQSNDCQVP HCLSCAMDDM FQDFYALENT
     NGYTAANILS GFWISEKKAF ENLVTTKEQD AHEFFQFLAE ELHERNGDGK KPEIGSEHSC
     NCIMHQTFYG KMQTTTTCQN CSGQSNSIQS FLDLSLGLEN VVQKKSKRTG QKKPSLTLQD
     CLDEEYIKYD KCEYRCNNCN GTQQAKRHTS IKRLPNVLSI QLKRFEYRHG RHDRAASKVD
     NEVKFPLQLN MLPYTNRVRN HESRESLELE RSCTYDLLSV VVHVGEIDTG HYTSYCRVGD
     QWFKFNDHKV ELASLSDVLG AQAYLLFYII RSLA
//
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