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Database: UniProt
Entry: X0BXY9_FUSOX
LinkDB: X0BXY9_FUSOX
Original site: X0BXY9_FUSOX 
ID   X0BXY9_FUSOX            Unreviewed;       354 AA.
AC   X0BXY9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000313|EMBL:EXK83768.1};
GN   ORFNames=FOQG_11929 {ECO:0000313|EMBL:EXK83768.1};
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:EXK83768.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK83768.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK83768.1,
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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DR   EMBL; JH658399; EXK83768.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0BXY9; -.
DR   HOGENOM; CLU_033446_1_1_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01517; PAP_phosphatase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   PANTHER; PTHR43200:SF2; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE; 1.
DR   PANTHER; PTHR43200; PHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663}.
SQ   SEQUENCE   354 AA;  38050 MW;  19A6A4E87E57D2F2 CRC64;
     MTPFARELHI AQLAVLRASI LTKSVQSRVH EISKDDDSPV TIADFAAQAL LIIALRDAFP
     SDKFLGEEDS AALRADEALC SKVFELVSSV ADTIDPNTGI PLPKPSSVAE MLSLIELGGR
     GTGGDEGRFW VMDPVDGTAT FLRGQQYAVA LSLIEQGREV IGVLGYPNIS TGMTQISEEN
     IDKSGMGIML TAVRGQGSMA RTMTPSGLKD AFPLSIMKTH SNNNNNNNNL HIVDCALSDV
     SRHDVIAELA DEFKAKFPNI EVWSSHVRYA ALIVGGGNAQ FWVPASSASK MHIWDHAGAQ
     LIFTELGGKV TDLDGKAMDF GAGRDLNRNR GLVVAQGEMH DALLAAMNRI IEGY
//
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