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Database: UniProt
Entry: B8NZT9_POSPM
LinkDB: B8NZT9_POSPM
Original site: B8NZT9_POSPM 
ID   B8NZT9_POSPM            Unreviewed;       283 AA.
AC   B8NZT9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EED85839.1};
GN   ORFNames=POSPLDRAFT_100197 {ECO:0000313|EMBL:EED85839.1};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN   [1] {ECO:0000313|EMBL:EED85839.1, ECO:0000313|Proteomes:UP000001743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA   Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA   Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA   Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA   Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA   Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA   Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA   Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA   Brettin T., Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT   placenta supports unique mechanisms of lignocellulose conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; EQ966234; EED85839.1; -; Genomic_DNA.
DR   RefSeq; XP_002468906.1; XM_002468861.1.
DR   AlphaFoldDB; B8NZT9; -.
DR   KEGG; ppl:POSPLDRAFT_100197; -.
DR   HOGENOM; CLU_983935_0_0_1; -.
DR   InParanoid; B8NZT9; -.
DR   OrthoDB; 5538464at2759; -.
DR   Proteomes; UP000001743; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 2.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        207..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   283 AA;  30039 MW;  6037EBD269D45EDA CRC64;
     MTSIQPGAAE SIQAIAGLGS SAPSVLVRIP ATGPCADGSA SWQIKYVLDA GARGVLVPLV
     CTAAQAASVV AAARFPQKRI LLYPLEGVAR CRIIHARAMR VEVNEVVGCP VAWGRVSACR
     GGGWWCNIIW GGGAIVSAGR EAAGRLDVFE EERESVGVVE QYGVFIGSYD LSLAYGYPPP
     LPDPHPDVEV MIQDILRKAR AEGKKSSVVF FLLMLCAFLQ VFRCLGLRYR ATGLEAQPAS
     TGRIRHGYPQ IYVTSDSGAM TQALAQSLAV AAGQAPSDKR FGY
//
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