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Database: UniProt
Entry: K1W9B7_TRIAC
LinkDB: K1W9B7_TRIAC
Original site: K1W9B7_TRIAC 
ID   K1W9B7_TRIAC            Unreviewed;       660 AA.
AC   K1W9B7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Phytase {ECO:0000313|EMBL:EKC98203.1};
GN   ORFNames=A1Q2_07535 {ECO:0000313|EMBL:EKC98203.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98203.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKC98203.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98203.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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:EKC98203.1}.
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DR   EMBL; AMBO01000395; EKC98203.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1W9B7; -.
DR   STRING; 1220162.K1W9B7; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_020880_2_2_1; -.
DR   InParanoid; K1W9B7; -.
DR   OMA; DVYTMQQ; -.
DR   OrthoDB; 2721627at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF42; 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   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        56..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..584
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  74380 MW;  9833A59766493691 CRC64;
     MVYHDKPDEL AGEEFELPHD HDDNAPLLPR YEGPSSSSLP AHPKYTRSGP RRRRPFLWIC
     ILLAILIPSA GFAACYYERK GGKALRYDGL PDKAKEWLDK VWGPHTGSAE NDDFPAEAAL
     VVTAPALPEY TGVSPIVPPQ NSKFKDFSII KHWGNLSPYH SVKSHGLPSS SQIVPKGCEL
     EQMHWLQRHG ARYPTTNPNG PAGLATRLKA AKFKASGKLK FLNDWDYKLG AELLTPFGRS
     QLYNLGVSAR IKYGFLLDRM NGTKPVFRTE SQDRMLRSAQ NFAAGFFGIP DEDQYNLLVM
     IEAPGFNCSL APYHSCPNDN KLYPNVNAKL ATWDFIYLKD ARKRLQKMVK GYDITIQDAR
     DMTVALGHSA FCELFTEKEW RGYEYRSSIY WWYAASFGSP VARAEGLGYL QELTARLSET
     PITEFNSSIN STYHTETRFP LGYPLYADFT HDTTFAQLLP TMNLTTFAKA GPPPLDHIPD
     NWPFIAAKFS PFATNMQVQV LSCPARTEKD ADFDTNMFED LLGNLKEWWP FGKHGYALKE
     KRMNVVKPAG PLNWPSASSA APEPTPTEEP EEEQPEPEDE EDEEVPTGER KRFVRLILND
     AAVPLTGIRG CKKDRDGLCE FDAFVSSMRE LIAGVDFAYD CNADYDITEE VTNGQPNRRH
//
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