ID A0A178B2S8_9PLEO Unreviewed; 733 AA.
AC A0A178B2S8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thermostable phytase {ECO:0000313|EMBL:OAL04516.1};
GN ORFNames=IQ06DRAFT_323584 {ECO:0000313|EMBL:OAL04516.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL04516.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL04516.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL04516.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KV441707; OAL04516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178B2S8; -.
DR STRING; 765868.A0A178B2S8; -.
DR InParanoid; A0A178B2S8; -.
DR OrthoDB; 2142659at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0016158; F:3-phytase activity; IEA:InterPro.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003431; BP_Phytase.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR PANTHER; PTHR14949:SF50; 3-PHYTASE; 1.
DR PANTHER; PTHR14949; EGF-LIKE-DOMAIN, MULTIPLE 7, 8; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF02333; Phytase; 1.
DR SUPFAM; SSF50956; Thermostable phytase (3-phytase); 2.
DR PROSITE; PS51662; BP_PHYTASE; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..733
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008082486"
FT DOMAIN 11..313
FT /note="BPP"
FT /evidence="ECO:0000259|PROSITE:PS51662"
FT DOMAIN 362..394
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 388..727
FT /note="BPP"
FT /evidence="ECO:0000259|PROSITE:PS51662"
FT DISULFID 366..376
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 384..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 733 AA; 77878 MW; 036939A9C60D5CDF CRC64;
MSTLVNCLLW ASTFIAAASA QTANVTLVPA AVGFDGHPDN TEFVYGRSPV LVANDGSAAD
GGFRNFAVSN SATFKQITHQ KTSRSKIAVP VHDVGGRDVI INVPAPDSLI RVFDAQTGKK
IDSNDKKQLG DWSTACVWRS QKSGESYVFL FGKKMVVQFI VSSDKKDVEI LEVQTFPVPI
EGEACTVFAN GQVFFSAEDQ PLYSFQATET IAAPSIRTVI EKIEVQGLAT YHSNGSDYLF
VAHDEVIDVY DKDVKQKGNI GLSGIADLSI EGGLSIFQSS FDGHPAGVFA FAFENDDDAG
VAVGSLASAL APLGIKANTG YSPKAKICNK CEDVVSKKCS ENGFSASGGC QCFAGFTGKD
CSKTTCKNDC SGHGKCDGPN VCKCKNGWTG PDCSFVAVKA KYETEANGGD GDDPAVWIHA
TRPDQSKVIT TTKSADGEGF GVFDLQGKLL QHLTAKEPNN VDIIYNVTVG SRRTDLAIAA
CRGDNTMCFA EVNSTGLLSN IPGGTQPLPE DYEPYGSCNY HSRKSGKDYL FVNNKEAQYL
QFELGSTANG TLTTKLVRQF QGGSGGQVEG CVGDDEAGYI FLGEEPLGIW RYDAEPTGSN
TGVQIAKVGD ASGLQADVEG ITLVPAKKGS GGYIMASSQG ISAYKVYERA PPHKYVSTFT
IVENEKKGID HVSNTDGITA VGNRLNNDFP YGLFVTHDDA NELAEGGTGK TASFKMASLV
DVLGEERARG LGY
//