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Database: UniProt
Entry: A0A1V6TIL9_9EURO
LinkDB: A0A1V6TIL9_9EURO
Original site: A0A1V6TIL9_9EURO 
ID   A0A1V6TIL9_9EURO        Unreviewed;       526 AA.
AC   A0A1V6TIL9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=3-phytase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSTE_c006G02271 {ECO:0000313|EMBL:OQE25413.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE25413.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE25413.1}.
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DR   EMBL; MLKD01000006; OQE25413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TIL9; -.
DR   STRING; 303698.A0A1V6TIL9; -.
DR   OrthoDB; 2721627at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
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   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..526
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012438440"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   ACT_SITE        380
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   DISULFID        68..434
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        286..299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   526 AA;  58223 MW;  7F310FD073A146D0 CRC64;
     MKGFIGTAAT LVAVANVATA TATSSASASA PTGTDYASGF DMTKSWANLS PYKDAKSFGL
     PKGVPQGCEL SQVHVLHRHA ERYPTDYPLD GAGMEDFASK LTNYSKAHQG KDVASGPLKF
     LNDWEYVIGS DILMETGAAT EATSGAHFWI KYGRLLYRPD RDNVAAWNES LNVWPNGTSR
     PKPVFRTTSQ DRILESARWW LSGFFGNSGA NSSYDQYDLV IIPETSPFNN TLASYESCPG
     DMTEGDNAAE TFIARYTKDA RTRLSQFFPK DFNLTAMDVL AMQNLCVYEY TSLAGSSFCS
     LFTEQEWKDF AYNIDIQYYG DYAYGSPTGR AQGIGYVLEL AARLQHKLIT TSDTSINYTY
     DNNEAQFPFD QPFYMDMSHD DIILSVINAL SLDHFRFGPH GLPSDLPHAP SQRNFSLSEM
     TPFGARLMSE IWSCPANTSF EELDPVLYTN PTLKTEDTTN YIRFVLNGAP LPTKGLPGCE
     DAKNGFCPVD RFLHGVPTLK KKAQYQHACF GKYPTGHQVS DGVPRS
//
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