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Database: UniProt
Entry: A0A423WUN9_9PEZI
LinkDB: A0A423WUN9_9PEZI
Original site: A0A423WUN9_9PEZI 
ID   A0A423WUN9_9PEZI        Unreviewed;       547 AA.
AC   A0A423WUN9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN   ORFNames=VMCG_04082 {ECO:0000313|EMBL:ROW06952.1};
OS   Valsa malicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW06952.1, ECO:0000313|Proteomes:UP000283895};
RN   [1] {ECO:0000313|EMBL:ROW06952.1, ECO:0000313|Proteomes:UP000283895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-1 {ECO:0000313|EMBL:ROW06952.1,
RC   ECO:0000313|Proteomes:UP000283895};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) 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:ROW06952.1}.
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DR   EMBL; LKEA01000009; ROW06952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WUN9; -.
DR   STRING; 356882.A0A423WUN9; -.
DR   Proteomes; UP000283895; Unassembled WGS sequence.
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:SF55; PHOSPHATASE, PUTATIVE-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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283895};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..547
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019053525"
SQ   SEQUENCE   547 AA;  59006 MW;  E4A6112842612C52 CRC64;
     MHSVRLVLIA LLTDIAGASP ITDSPAAGSI TSDIFPPAST SVNTDLFPGE PVVGYPGTII
     TGIEPAAAQT ASAYPYNNGP ANEFPLVAPV PHGESSSSSF DIKKYWGNLS PWYSVSSADY
     GLPDASPLIS DGCNIVQVHV LYRHGARYPT SGAAPATFAQ KIVNATKTGF SATGELSFLA
     DWTYKLGAEF LTPFGRSQNF LLGLEYRQLY GSLLNNFTEQ GAIPVFRTES QDRMVKTANN
     FAAGFFGVPE YLDEVNIEIL VETSGLNNSG APYETCTNSN VASKGSIGST VATAFANNAF
     NTTLSRLNSQ VTGITFTPTD AVAMLQLCSY ETVALGYSVF CDLFSQEDYL NYEYYYDLSF
     YYNNGPGSPV SAAQGKGYLQ EFVARFTGTY PTAESALNAT FDNNTTYFPL NQSIYADATH
     EVVVLDTLTA FNLTALFDGE PLSVTGNTHQ NSFVASKTVP FATHFTVQVL ECPAYQPTKQ
     IRFIVNDAVV PVNGTYSGCE YNADGLCSFD NVVSVLQQRL DEIDYEYDCF ANYTAKAGVD
     YNGRAPK
//
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