ID   A8N8W9_COPC7            Unreviewed;      1066 AA.
AC   A8N8W9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Heme peroxidase {ECO:0000313|EMBL:EAU90460.2};
GN   ORFNames=CC1G_00844 {ECO:0000313|EMBL:EAU90460.2};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU90460.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU90460.2, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EAU90460.2}.
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DR   EMBL; AACS02000007; EAU90460.2; -; Genomic_DNA.
DR   RefSeq; XP_001831297.2; XM_001831245.2.
DR   AlphaFoldDB; A8N8W9; -.
DR   GeneID; 6007766; -.
DR   KEGG; cci:CC1G_00844; -.
DR   VEuPathDB; FungiDB:CC1G_00844; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_0_0_1; -.
DR   InParanoid; A8N8W9; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000001861; 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:UniProtKB-KW.
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; 2.
DR   PRINTS; PR00457; ANPEROXIDASE.
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:0000313|EMBL:EAU90460.2};
KW   Peroxidase {ECO:0000313|EMBL:EAU90460.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         398
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   1066 AA;  120099 MW;  80CAEC4E648141DD CRC64;
     MSSSKVKRMS TLFRKKEKEP STSNGVVTNG AEKKDEAASP TSPTSPLSPS QEAEGMKTMR
     NFRESVKKGS PFDFSTSSIA AVLDLIRNKE SIDDRKLFLE HALTFISRLE EGPLARTLKN
     KIIQLLYNDL THPASTSVSN QFAWRTADGS CNNVDIPDMG KAGTPYSRSV QQTVPLPKNQ
     MPDAGLLFDT LLRREKFVPH PGGLSSLMFA FATLVIHTVF RTSHRDWTIN ETSSYVDLAP
     LYGNNEDDQN RIRIRDGRGH LYPDVFAEDR LLLLPPAVCA LLVLFSRNHN YIATKLLEVN
     ERGTFVDPST LSMDDPKQKA KLMAQDEELF QTARLVNCGW FAMVVFSDYF SCILGLVRDG
     NSWSLTPFDE IRMEDHTLFE RGKGNSCSVE FNCLYRWHTT TSREDEKWTE GVFSQLFPGK
     PFEEVTIDDF KTTAHKLLTN RPPTTEWTFG GLKRQPDGRF RDEDLARIIQ DATECEAAAF
     GARGTPAVMR LNEIMGIEQS RRWGVCSLNE FRKFLGLKPY ETFLEWNSDP DVARTAELLY
     GDINKLELYV GLQAEEAKPL VDGAGLCPGY TCSRAILSDA IALTRGDRFF THDFTPFNLT
     AWGYQDCQRD PNAWGFGSTM ARLFLRTLPE DFDEKSVYTF FPLMTPQSMK VHLTKLNQLD
     NYDLARPKRN PCPTIIRDYP SVVAILNEPL GFRSPYSQKT RKIINGPIKG FYPAEGPKEQ
     DVVRKALSGS PEVVGKVGTY FYEQIKKTID ENSYTFVNGK KRGIDVVKKV INTVPTAWLG
     DLGGLHVKTS KDSAGNYTVD ELFQQLSEIY SFIFLNVDPA KVMVLQEKVR KYLKVIIPDI
     KDNFTGSFSL TGLFNTVFKY KKPVHHEIIS RLTENETLKN HDVLSNVILA LVVVGNAEIT
     LASTNILDYY LGSDKAADIG KLAAAGDVAG LKPYIYEALR AVPPFAGVYR VSTREQIFAG
     RKFAESERVF LDITAANNQS REESTKEILR AEGAFEYLGE ELTVEILAQI IRAIFERPGL
     TRAPGHSGQM SRFKTDNRPE CHHTYLHHGE RVTEWPYTLS VLYDAA
//