ID   A0A1Y2MEA1_EPING        Unreviewed;      1104 AA.
AC   A0A1Y2MEA1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B5807_01720 {ECO:0000313|EMBL:OSS54291.1};
OS   Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX   NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS54291.1, ECO:0000313|Proteomes:UP000193240};
RN   [1] {ECO:0000313|EMBL:OSS54291.1, ECO:0000313|Proteomes:UP000193240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS54291.1,
RC   ECO:0000313|Proteomes:UP000193240};
RA   Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT   "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT   strain isolated from New Zealand.";
RL   Genome Announc. 0:0-0(2017).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; KZ107838; OSS54291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2MEA1; -.
DR   STRING; 105696.A0A1Y2MEA1; -.
DR   InParanoid; A0A1Y2MEA1; -.
DR   OMA; EEPAHAF; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000193240; 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; cd20612; CYP_LDS-like_C; 1.
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; IPR001128; Cyt_P450.
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   Pfam; PF00067; p450; 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:UP000193240}.
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         366
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   1104 AA;  122086 MW;  E05D689024945A8F CRC64;
     MPSQLRSLLG TIRKKPTKAS DGRSDEDASG MAATKKTAVS SDLRNLGLKN ARFAVEAITT
     LASGDPIDDK ELMLEHGVEM LQGLPLNSGL SAKVSDGFIS MLWNDLPHPT PTMAGPTARY
     RKHDGSGNNP WNPEMGKAGS PYARNVPPSK PKGPNLPNVE DVYEALLKRD GPFRPHPSGL
     NRLFFSFATI VIHECFQTSR ENPWINETSS YVDLSTLYGN TEKEQPRVRT YKNGLIYPDS
     IASERIMMMP PGVVVVLLMF SRNHNHVAES LLTVNEDGKY KPWDQLSEED QKKQDEDIFQ
     ITRNINVGFF ASVVLKDYVA AILNTPRANS EWSLDLGKEI KQGGTRVERG TGSHVSVEFA
     VLYHWHAALS AADDNWMEEI IRSVKPDLGS IDDVNLEMFK EVVKFHGHKL FAPGVHAKDW
     TFGGLQRGPD GRFSDRDLGE LIKNCIDEPA HAFGAHGTPA SLKVVDLMGQ MQARDMFNVC
     TLNEFRRYLN LKAYTTFEEW NPDKETARAA ELLYGHIENM ELYPGLMAEC TKPPMPGSGV
     CPGQTTGRGI LDDAVALVRG DRFLSYDFNA NTLTNWGAAL LQQKTPGAYG GVLPRLLFQG
     LPGAFTGTST YALLPFYTPE AAKGIVHGNK ALEKYDLKRS PSDNDIVSVQ TQEGCKKVFE
     DRDNFVVMYQ AAIRNCTAGH DFMIGWDDAK KHDDRSNILH KIFFEDGFEK NTTDFFTAHV
     RKQILKNTVK GPKGRRSIDV VRDVTNIVPI LWLADRFALP LKTQEQPKGL LTLHEAFTAY
     LVLFMYQSFN IMPANEWKLK EGAMKAAAPL RQIFETHIKT QTGRFEGVVD WMAKGSAFEV
     GPHADRIYKA LADTKLPLGD QVGDCIGMGA PVAGNITQQA SLLIDLYLRP GYEKYKERII
     ELAHMDSAAS DRELQGFVYE GMRHVGVVPG LPRVATRDVT IMDGVRGPVT VKKGHTVLIA
     TSKAAMDPLA FPDPEVLNPL RPFKDYTLLG YGLHFCFGAR LVGPSIAATL REVFKLKNVR
     RAPGKQGRFT TTEHKLAGIT MRHYLDASSN ESPIPTSLTL HYDDETVVNG TSGVNGRQNG
     TNGYSNGYVN GSAVNGLTTG GLAR
//