ID   D8QLS5_SCHCM            Unreviewed;      1111 AA.
AC   D8QLS5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=SCHCODRAFT_114799 {ECO:0000313|EMBL:EFI91160.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFI91160.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
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DR   EMBL; GL377319; EFI91160.1; -; Genomic_DNA.
DR   RefSeq; XP_003026063.1; XM_003026017.1.
DR   AlphaFoldDB; D8QLS5; -.
DR   GeneID; 9588895; -.
DR   KEGG; scm:SCHCO_02517480; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02517480; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_0_0_1; -.
DR   InParanoid; D8QLS5; -.
DR   OMA; EFNMIYR; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000007431; 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:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR036396; Cyt_P450_sf.
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; SSF48264; Cytochrome P450; 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:UP000007431}.
FT   BINDING         408
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"
FT   NON_TER         1111
FT                   /evidence="ECO:0000313|EMBL:EFI91160.1"
SQ   SEQUENCE   1111 AA;  123434 MW;  0EF0A67B2DC1D0F5 CRC64;
     MSIIQRLAGG ADFVLASTAP VDTDGGKPRP RYVVGQKLDE LVQYLKNPPA QLDSLVSISI
     PYILDAKLTK CSEPAYLDAV KHMHSGLDDR KLLPAQLEHL LTLMARLGSG NDFSSRVQEA
     VIDLLYKDLP HPPACYLSVL HQAGLNLNVP LANVNYAYRT ADGSYYNPLF PTLGMAGTPY
     ARSVPSANCT PLNNLPDAGL VFDTLLRRKE GTFKEHEGGM SSLFFAMADL IIHCIFDTDH
     KDITKNNTSS YLDLSILYGN SEEQLNGVRR HDGTGRLWDD VFADRRLLLM PPSTCALLVL
     FCRNHNHIAQ RILDINEKGK YRSVDSFSDD ARKAQDDEIF HRARLVNCGF FMQVILADYV
     GAILGLVRDG LPWRLDPLMT MRRESHEFSP QGEGNVVSIE FNLLYRWHAA LSAQDTKWTE
     GLFKSVFGQD VDFDKVTPTD FKRVVGRMFG QPQDPRTATF TDYAGQRLER HPEEGAATPD
     GAGRFADADL ARVLQDATSW RAGSYGARAI PAALRVIEVM GIEQSREWGT CSLNEFRHFM
     GLKKYDSFKD WNPDPVVHKQ AETLYKDINN LELHVGMQAE AIKTPGPGAG LCPGYTISRA
     ILGDAVALTR GDRFLTTEYT PNNLTRWGFK YSHVDPDDGS VGGILPRMLL ATLPDHYPSG
     SAYTHFPFLE PAYIRNEMRK RGDKNLDRYT WDRPAVPAPL TVISTWAEAV EVLDTQKARF
     VSSYPQRLKD VTGVDADSKL LARKTLLRLA PRLPAYFASK TMELINASPV TYVDADTKTV
     DIGRHVINLL PVHWISQQLA CIALKTESNP LGTEYESDVC DMFENVCRYV YLDNDTYNHF
     RLQTDARKAF EHLTSFTARK LRAMTGSRIS VSGITQTLSR FILKEDDSTP FLRALLEGSD
     GADADTLAAH LFAEVVPTAA HFSRIVMQVV DFFLGSDEEG DEKRQAREAI VALASQCTAE
     ADKQVMKYVD EALRLEPAVS GVYRTASAAA VVGNQRIEAG QRVYVALSAA KQDSSVFGAD
     TSTADFKRST PSSTRLGLPD SGLLIPQLFD RILPRVLGVI FGLKNLRRAP GQSGVMSSFT
     QTLHGAPEKL FFDFDGNVTP IPESLFVEYD F
//