ID B8PGW6_POSPM Unreviewed; 991 AA.
AC B8PGW6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EED79896.1};
GN ORFNames=POSPLDRAFT_98495 {ECO:0000313|EMBL:EED79896.1};
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:EED79896.1, 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).
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DR EMBL; EQ966362; EED79896.1; -; Genomic_DNA.
DR RefSeq; XP_002474922.1; XM_002474877.1.
DR AlphaFoldDB; B8PGW6; -.
DR KEGG; ppl:POSPLDRAFT_98495; -.
DR HOGENOM; CLU_002329_0_0_1; -.
DR InParanoid; B8PGW6; -.
DR OMA; EFNMIYR; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT BINDING 390
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 991 AA; 108774 MW; 5C642ABF9A75F3A1 CRC64;
MVNLNPVLNP LKNTIDFVAE SDAPVDQDGG HPLPPLLARK ITDVEQEAIR GPGFTPADLP
AYINAVKTLN GPGLDDRKFL LEKVLTLMAR APDDSAFAAT LQKFAIDILY KDLPHPPSGY
LALPSGAPPA ASPITKGVKY AYRSADGSDY HVLIPTLGMA GTPYARSVPS TTRIPPQYLP
DPGLVFDTLL KREKFVEHPG GISSLFFAFA DLVIHSIFNT NTRDWTINDA SSYLDLSPLY
GSSQAQVDSV RRKDGTGRLY EDVFADPRLL FMPPASCALL VLFCRNHNYV AERILAINEL
GSYRAPSTLG AQERAAQDEE LFQRARLVNS ALFMQVILGD YVGAILGLTR DGLAWRLDPL
AAMRELNHAF SPQGEGNVVA VEFNLMYRWH ATSSVSDTQW IENLFGELFP GKSWSDISVN
DFRTAIIKYV MGTPQDVKEW SFDNLKRGPD GRYDDVELAN ILQSATEAPA SAFGARGTPE
VLRVIEILGI MQARSWGTCS LNEFRSFMGL KPYSTFAEWN PDPKIYAGLQ AEETKVPMPG
AGLCPGYTIS RAILADAVCL TRGDRFLTVD LTPFNLTTWG YQDCQYKKDD GSIGGILSKL
LFRTLPNQYP ADSAYAFFPF MVPKTMKGHV AADAVNKYSW DRPALAAPVT SLLGPSVSAP
VSEYEKRLKA ILGGVVPDRA AVRQVLFSDA SIQQWAQSFQ EITQQLLKTK SVDHVDSKAK
YVNIVRDVIN VLPVVWISNF IVGLPLKTET NPHGVYREHD LLTKWSDIGN YVFLDQSPEG
QFALRGKCTE TAKDVTGFVK GHCAELSGHS LSGFADSVVD YVTGGNEHER SFIKSLLAGR
HGSHDALAAG VIAEVVATAP LYSRILAEVV DYYLDDGKRA RLVSVLTGES VNRDEKLLAL
IREALPTGDV QKLDAARSVD FGLLDHRFLA KTAFTVLRTI FSLKDLKRAP GSSGSLNRFA
DDTNGELRPV YLTSQGSVTP WPVSMLVQYN L
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