ID   A0A0F0IHD4_ASPPU        Unreviewed;      1139 AA.
AC   A0A0F0IHD4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Animal heme peroxidase {ECO:0000313|EMBL:KJK67229.1};
GN   ORFNames=P875_00117368 {ECO:0000313|EMBL:KJK67229.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK67229.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK67229.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:KJK67229.1}.
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DR   EMBL; JZEE01000198; KJK67229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IHD4; -.
DR   STRING; 1403190.A0A0F0IHD4; -.
DR   Proteomes; UP000033540; 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; 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:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF00067; p450; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000313|EMBL:KJK67229.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1139 AA;  128732 MW;  1470D2387824EDBF CRC64;
     MKGVPSSAEA SNSMPGSSLP SQGALEPLTH KQPTLEHPRK QSVQSISSEH GGMAENFSKI
     TKVVQAARRP LPTETGDGTY IEPENGGSLW RDLRALGIKD ANTLKDLIEN KAGGLVKGSG
     QVVDDKTMLM ERIIQLVAKL PTESRNRVKL TNMFLGELWD SLPHPPLSYV GDKYAYRSAD
     GSYNNPTLPW LGAANTEYAR TIEPLKVRPA SLPDPGLIFD SLFARDTFKP HPNNVSSVFF
     TWASLIIHDI FQTGHPDENF NKTSSYLDLS ILYGDNQEEQ NMMRTFEHGK IKPDCFSEPR
     LHALPAACGV ILVMLNRFHN HVVEQLAAIN ENGRFTKPPK HIIDPVEARA AWAKYDNDLF
     QTGRLITCGL YINITLYDYL RTIVNLNRDN TTWTLDPRAH MEHDTVPTAL GNQCSVEFNL
     AYRWHSTISR KDEAWTEQAY QAIVGKPGSE ATVQDLMSGM RRLGANMPKD PSKREFAGLK
     RQSCGKFKDE ELVDVLTMAI DEVAGSFGAR NVPKVLRSVE ILGMEQARRW NVGSLNEFRK
     FFDLKPYQSF EEINSDPEVA DQLRHLYEHP DYVELYPGIV AEEAKKPMIP GVGIAPGYTV
     SRAVLSDAVA LVRGDRFYTK EYNSRNLTNW GYEEANYDLE INQGCVFYKL ALRAFPQYFK
     QNSIFAHYPM TTPSANRDIM KMLGREEDFS WDRPSYTPPR TTLFDYANVR RILEDSSNFR
     VIWDEATGYV FGKGGYDFML SGDSPFHANQ RRIMKESLYR SQWHEAVKEF YLEITEQLLS
     EKSCRLGNVN QIDISRDVGN LAHVHFASNI FSLPLKTKEH PHGVLTEHEM FDVMSIIFTA
     IFFDVDPSKS FRLRHMARKA AETLGPLVEA NVKAVSSASF LSTLIDGIRT NKNALSGYGV
     HMIRRLLDHG LDASEVTWSQ ILPTAVAMVP NQAQVFTQII DYYLSDEGKE HLPNIQQLAK
     EDTPASDEML LRYVMEAIRL NGIFGSYRKS HTNLTVDDKN KMVQIKPGDT VFVSFVDANR
     DPNVFPNPNK VDLNRPMESY IHYGVGPHTC LGGDASKVAL TAMLRVVGRL KNLRRAPGPQ
     GELKKIPRDH GFYTYMRADE TSLYAFPMTW KLHYDGTIPG RERYVPEKLT CNVPGHWHD
//