ID X0D0E0_FUSOX Unreviewed; 1066 AA.
AC X0D0E0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=FOQG_00261 {ECO:0000313|EMBL:EXK99881.1};
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:EXK99881.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK99881.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK99881.1,
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; EXK99881.1; -; Genomic_DNA.
DR AlphaFoldDB; X0D0E0; -.
DR HOGENOM; CLU_003532_0_1_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 1..109
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 135..456
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1066 AA; 124032 MW; 0AC440B454B68A1F CRC64;
MLTFHYYRRI LLFPHGNNID QCSIYLEHGF DADSVPDNWS CCVQFALVLW NPNDPSLYVH
HTAHHRFTKE EGDWGFTRFV EHRRMFNVPW EGSSRPLCEN DTANITAYLR LVEDETGVLW
HNFANYDSKK ETGYVGLKNQ GATCYLNSLM QSLYFTNKFR KAIYEIPTEA DPSMTNSAYT
LQRLFYQLQT SDQAVGTTEL TKSFGWDTRH IFEQQDVQEF SRKLMERMED KMKGTASENV
LPEMFSGKIK TYISCINVDY ESSRIEDFWD IQLNVSGNKH LLESFEDYVQ VEKMDGENQY
FAGDQYKLQD ANKGVIFNSF PDVLHLQLKR FEYDIQRDTM MKINDRYEFP EFFDAAPYLS
EDADKSVPWT YQLHSVLVHS GDLNAGHYYA FLKPEKDGWF YKYDDDKVTK ATMREVLEEN
FGGEYQTSNG YPRAPVQKKA PIMRQNSAYM LVYIRQSRID DILCPVTKDH IPLHLRQKFE
EETVQREARK KEQREAHLYM WAKVITDYSF QQYGGTDLCQ FDAKPEDPAA PKFYRVRRAM
TMEEFVAQVA SDMGEDPRRV RLWLMVNRQN KTVRPDQPIM DLRPTVDETF SRSAAHRDAS
LRVWAEVAEE VNADGEPIWP SYQSQPNGVI VKNDTILLLL KHFDIDAQTL RGVGHVYISK
DKKVEELLPM ILKKMGWGEK LPAEEKLLLW EEIKPTMIEP LKPKQSLKVA ELQDGDIICF
QRTKAGVEKR AGEKTSQETS NTSDHFEDAR EYYDFLENRR TVKFHPHPAR CDQAQYPPFD
LVLNTKITYD TLSERVGAYL DVKPTHIRFW TVNASTQNPK TPVRRGANPT LRQILSPMGS
TALNSTQRDD AFYFEVLEMS LTELDTKKSI KVNLLSEGIT KEDTYDLLVP KTGTIDDLVE
VLIRKAQIPS ETDGGRIRIY ETSSNRFYRE PLREHPVINL NEFAKIYAER VPQEELNADD
THFIHVFHFH NDVSRVHGVP FKFLVIEGES FADTKKRLEK RTGIKGKSFE KIKIAVVRRA
NYSKPQYLND DDVLSSFIQG EDDYLGLDHV DRTRTLRNGV GDLFLK
//
