ID S3C446_OPHP1 Unreviewed; 674 AA.
AC S3C446;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=F503_01052 {ECO:0000313|EMBL:EPE08269.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE08269.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE08269.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE08269.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KE148149; EPE08269.1; -; Genomic_DNA.
DR AlphaFoldDB; S3C446; -.
DR STRING; 1262450.S3C446; -.
DR VEuPathDB; FungiDB:F503_01052; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_2_1_1; -.
DR OMA; LHSYMYG; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR20963:SF43; PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01240)-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 72853 MW; 4747B9D6B91DAA2D CRC64;
MADRKGAVTK SGSQPVAVAD AAEEVELQRR KETSSDSKKA SFADDRSNAY DDDEDGNADE
TRGFLAAGNS TRIYPGTASP STNAPGFAPA STSGSADAPK WLSKKMARVV AVSFMTCLAV
CIGFKLVADN TGLVLSLDHP KAGQDGSSSG SKDMSGGGGA GDDCACATAT VTVPLHFQTS
PQLWAGPTAT GRPAFMAQTV TIDPSATYVA NQPLQTNIVV EGELGDEPSI FRHMGYLSPY
NPSPGFGVQE YALPPGAVIS QLQMLSRHGS RYPTLGTNVQ TLGNKMAKVK GKFKASGALA
FLEDWEYKMG YEILVPKGRQ ELYDSGVLHA YMYADLYNPN SKIIVRTTTQ DRMLKSAENF
LAGFFGLEWT NNATIEVIIE RAGANNSLAG YMNCPNSLKD TAGSTASAIW VQNYLRNATA
RFQSKIEGIE WTIDDTYAAQ NLCPYETAAF GFSRFCSLFT HEEWVGFGYS IDLGFAGNSG
FQSSTGRAVG IGYQQEVVAR LRNHTLGYSG SQINVTLDNN TDTFPLNQSL YLDFSHDTNI
VSILTAFGFK QFSQLLKPTE YPGPHNFTVA HVVPFGARLD IEIIDAPKPV AADRSGYDEA
GKETRYIHFI LNQRTVPLGA SFPECDASRV DGWCELETFL RIQEDMPARA KYDEACHGPF
TPQPYGLIND GAPM
//
