ID W9IEW9_FUSOX Unreviewed; 774 AA.
AC W9IEW9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=FOYG_08806 {ECO:0000313|EMBL:EWY91855.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY91855.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY91855.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
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 FOSC 3-a.";
RL Submitted (JUN-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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; JH717843; EWY91855.1; -; Genomic_DNA.
DR AlphaFoldDB; W9IEW9; -.
DR HOGENOM; CLU_009884_1_0_1; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 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; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR016308-3}; Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025};
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..774
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 ACT_SITE 310
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 728
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
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 774 AA; 85839 MW; 0260D88BDA2EF67D CRC64;
MACQHLDLIG LTPPNPSQSV YREDCTQCFD SIDDPAGLDV CLQCFNGGCA GDRNHNRLHY
ALTQHPLALN IRRTRKIVER DEPPTKMSKL AIAAETEEDR YDTALTVKCL DCNTELDRTH
PKLAPMVDGI LKANTFSRKE EVKAWEQELT SCEHILMLQQ APAKKIEQND LSHCYACDLA
ENLWLCIECG NLGCGRKQMG GVDGNSHALA HANESGHGVA VKLGSITPEG TADIYCYKCD
DERVDDNLGE HLNHWGIVLA ERQKTEKSLT EMQIEQNLKW DFSMTTEDGK ELKPLFGPGL
TGLKNLGNSC YLASIIQCLF DMPSFQDRYF RPNDDLPIVP EPAADIETQL RKTADGLLSG
RYSKPDADVA GEGITHQKGL APAMLKHLIG RGHEEFSTMR QQDALEFLQH LFKLITRSPH
PHGKDPTQPF 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 PDDQGIFDDD APAEAAAPKE PAGSADLPAT FQLRSIVCHK
GTSIHAGHYV AFIRKALGDA NVPTWVLFND EKVVEAHDVD EMRKFAYVYF FKRV
//
