ID A0A1Z5TL71_HORWE Unreviewed; 627 AA.
AC A0A1Z5TL71;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=BTJ68_03365 {ECO:0000313|EMBL:OTA36715.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA36715.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA36715.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA36715.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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:OTA36715.1}.
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DR EMBL; MUNK01000028; OTA36715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TL71; -.
DR STRING; 1157616.A0A1Z5TL71; -.
DR VEuPathDB; FungiDB:BTJ68_03365; -.
DR InParanoid; A0A1Z5TL71; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000194280; 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:UP000194280};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 68976 MW; 3EC84EC0C62DB143 CRC64;
MRGRIMQDSP DCSSEHGGHT KGIEHPAKHD EEKHGDLSTK LRPAPESVSG SGVSTLFRQR
PLFAGQVVLF TIIVVQAVML YRSLALASAC GIVDAGALRK QAASSGSSSS DIPQYYQTSP
ELFPGPTPTG EPAFLAQTNP APFPSTTYIP PSPLETQVPI QGNENDGNIF HMMGQLSHYF
PNPDGFGVDE YPLPENATIK QLNMLSRHGA RYPTTGSGAP MLAEKITNYT TGVLGDVEFT
GPLSFLNKWQ YKLGAEILVP VGKQELFDSG TLHQYMYGHL YPNNGSKIIA RSTTQDRMTK
TAEYFLAGFF GLDWPSNATL VLAIEGSDST WNNSLAGYDN CPNSNKPVNA GGNNATMEWY
NIYLADATES LRPHAPGFNW TVTDTYNAQS MCAYETVALG YSTFCDLFTF EEWQGYEYSI
DLYFAGSYGF QSPTGRAVGI GYVQEILARL QHHVIDHPVA QINLTLDNNT ATFPLDQTLN
FDFSHDTNIM AILTAFGFTQ FAPFLPPDHI PARHHRNLIV SYMEPFAARL DMEILSTPSP
LDGRRTHGPK YLDGPPTTYI HFLLNQRTLP LGESFPACGD RDDGWCELTT FLEVQEESLA
KANYEFACFG EYEAVPYGTI MDGAPLG
//
