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Database: UniProt
Entry: A0A094GW21_9PEZI
LinkDB: A0A094GW21_9PEZI
Original site: A0A094GW21_9PEZI 
ID   A0A094GW21_9PEZI        Unreviewed;       481 AA.
AC   A0A094GW21;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN   ORFNames=V501_06857 {ECO:0000313|EMBL:KFZ07007.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ07007.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ07007.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFZ07007.1}.
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DR   EMBL; JPKD01002063; KFZ07007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094GW21; -.
DR   STRING; 1420914.A0A094GW21; -.
DR   HOGENOM; CLU_023111_1_0_1; -.
DR   Proteomes; UP000029315; 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; PTHR11567:SF142; -; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..481
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001898143"
FT   TRANSMEM        432..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   481 AA;  50833 MW;  582D28AA369C7E6B CRC64;
     MVTTQLLLIS LLSLVVQAQE TVLGAYIVHR HGDRTPKEFP PAGLTDLGYA QIYGAGAFYR
     ARYLEDSSRN KIYGISQNVV KLSQLTVQAP VDTVLQNSAQ GWLQGLYPPV GTSAATQMLA
     NGTSVSAPMN GYQLIPVNTV SSARSSSANP EDTTWLQGSS GCNNAITSSN SYFISDDYTS
     TLASTKDFYA SLLPVVKTTF SSSDDTYKNA YAIYDYIHVS KIHNSTIPSG DLLTDNVLHQ
     LQTRANQHEF NLAYNSSEPV RAIAGSTLAA EIVQQLNATI TSKSASSLAV QFGAYNSFLS
     FFGLAQLPSV SDDFTGIVDY ASAMVFELVT SATVTESSYP STDRISVRFL FTNGSAAYNP
     LTEYPLFGQP ATSLPWNTFV SSMNKFAISD KASWCSACGD TTGACAATST STDSSNSSAA
     GSGSGGISKA TAGVIGAMVT LAVLLGLATL VLLFGGLRVV SKKRLAGAHT DREAVSPVSK
     E
//
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