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Database: UniProt
Entry: W9K704_FUSOX
LinkDB: W9K704_FUSOX
Original site: W9K704_FUSOX 
ID   W9K704_FUSOX            Unreviewed;       727 AA.
AC   W9K704;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Ubiquitin thiolesterase {ECO:0000313|EMBL:EWZ38519.1};
GN   ORFNames=FOZG_10101 {ECO:0000313|EMBL:EWZ38519.1};
OS   Fusarium oxysporum Fo47.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660027 {ECO:0000313|EMBL:EWZ38519.1};
RN   [1] {ECO:0000313|EMBL:EWZ38519.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo47 {ECO:0000313|EMBL:EWZ38519.1};
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., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum Fo47.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EWZ38519.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Fo47 {ECO:0000313|EMBL:EWZ38519.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum Fo47.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   EMBL; JH717901; EWZ38519.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9K704; -.
DR   VEuPathDB; FungiDB:FOZG_10101; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProt.
DR   CDD; cd02658; Peptidase_C19B; 1.
DR   CDD; cd14385; UBA1_spUBP14_like; 1.
DR   CDD; cd14386; UBA2_UBP5; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR041432; UBP13_Znf-UBP_var.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF664; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 2.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR016308-3};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          1..107
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          150..259
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          301..727
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          578..619
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          640..680
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          680..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ   SEQUENCE   727 AA;  80125 MW;  D09F758BC1B0CCED CRC64;
     MACQHLDLIG LTPPNPSQSV YREDCTQCFD SIDDPAGLDV CLQCFNGGCA GDRNHNRLHY
     ALTQHPLALN IRRTRKIVER DEPPTKMSKL AIAAETEEDR YDTALTVKCL DCNTELDRTH
     PKLAPMVDGI LKANTFSRKE EVKAWEQELT SCEHILTLQQ APAKKIEQND LSHCYACDLP
     ENLWLCIECG NLGCGRKQMG GVDGNSHALA HANESGHGVA VKLGSITPEG TADIYCYKCD
     DERVDDNLGE HLNHWGIVLA ERQKTEKSLT EMQIEQNLKW DFSMTTEDGK ELKPLFGPGL
     TGLKNLGNSC YLASIIQCLF DMPSFQDRYF RPNDDLPIVP EPAADIETQL RKTADGLLSG
     RYSKPDAGVA GEGITHQKGL APAMLKHLIG RGHEEFSTMR QQDALEFLQH LFKLITRSPH
     PDGKDPTQPF RFVLEQRLQC LGCHKVRYSS NEQDNIFIDV PLEKLPREEG SEGPDAYKPV
     SLKECLDNFT GAEKVELTCS ACGSKDGFTK RSLFKTFPDT LVVNARKMTV VNWVPIKVDV
     PVLVPDEPFN LDEYLSRGLQ PGEEQLPDEP EVKAPAFEPD AAALAQLEAM GFPRNRCERA
     LHATGNSDAN AAMEWLFGHM EDPDIDAPLD LGAQSGDANT ADPEKIEMLG AMGFGAPQAK
     KALKETGGDV ERAVEWLFSH PDDQGTFDDD APAEAAAPKE PAGSADLPAT FQLRSIVCHK
     GTSIHAG
//
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