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Database: UniProt
Entry: W6QAP2_PENRF
LinkDB: W6QAP2_PENRF
Original site: W6QAP2_PENRF 
ID   W6QAP2_PENRF            Unreviewed;       352 AA.
AC   W6QAP2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Inositol monophosphatase {ECO:0000313|EMBL:CDM26782.1};
GN   ORFNames=PROQFM164_S01g000591 {ECO:0000313|EMBL:CDM26782.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM26782.1};
RN   [1] {ECO:0000313|EMBL:CDM26782.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM26782.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
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; HG792015; CDM26782.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QAP2; -.
DR   STRING; 1365484.W6QAP2; -.
DR   OMA; AGCHGMV; -.
DR   OrthoDB; 5486961at2759; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}.
SQ   SEQUENCE   352 AA;  37256 MW;  10F3DDF533DB6C2C CRC64;
     MTSMPYAKEL QLASLAVQRA AILTKELLSA VDKGALDKSD SSPVTIADFA AQASIIAAIH
     NVFPDDDIVG EEDATALRSN PDLLARTWDL ATSIHLNDPE SEALLHTPRT TSELLDLIDL
     GAKGACTPTS RTWTLDPVDG TATFIRGEQY AVCLSLVENG IQRIGVLGCP NLLESGLVAE
     DRVDRDGLGQ MISAVVGQGA TIRPMGPGAL LPARPLEHVP QVGASGVRFI DTRAAKTQDL
     EAHARVAAHL GCPWPNPVDL WSAQMRYIAI AVQGGCNAFV KVPLSADYRS KIWDHAGGML
     IVQELGCLVT DLEGKPVDCS LGRTLAGCHG MVVGPASVHG RILEAVREAR GL
//
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