ID   A0A2C5ZKY9_9HYPO        Unreviewed;      1092 AA.
AC   A0A2C5ZKY9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDD80_3383 {ECO:0000313|EMBL:PHH79931.1};
OS   Ophiocordyceps camponoti-rufipedis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH79931.1, ECO:0000313|Proteomes:UP000226431};
RN   [1] {ECO:0000313|EMBL:PHH79931.1, ECO:0000313|Proteomes:UP000226431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map16 {ECO:0000313|EMBL:PHH79931.1,
RC   ECO:0000313|Proteomes:UP000226431};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PHH79931.1}.
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DR   EMBL; NJES01000030; PHH79931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5ZKY9; -.
DR   STRING; 2004952.A0A2C5ZKY9; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000226431; 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; 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   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:0000256|ARBA:ARBA00022964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000226431}.
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   1092 AA;  121841 MW;  0FA6121EFD2A2ED7 CRC64;
     MSSEAASRAV DGGQTNGSQV NGVKDDGQRQ NPRRRPQKAN TFPLSFYRQE SLRPLPTETG
     DGTYRAVNRR PGLTKDLRSI GWRDIKTVKE VIVSKLKGET QTDDKAMVME RIIRMVATLP
     DNSYRQETLT NFFIDELWNS LDHPALLYMG DEFRYRLPDG SNNNPLMPKL GAARTPYSRT
     VKPGKRNLGA LPDPETVYEA VMARGTFKRN PNNVSSILWY WATIIIHDLF NTNMQDANQN
     DSSSYLDLSP LYGSTKEAID SVRTFKNGLL KPDTFADRRL LGNPPGVCVL LIMFNRFHNH
     VAQKLAEINE HNRFPRPASN LSEADAAVGW KKHDEDLFQT ARLITSGLYI NITLIDYVRN
     IINLNRVDSA WTLDPRQEMG VSAGTSKGAE AGVGNAVSAE FNLCYRWHSC ISQMDEDWIQ
     DFYKELLGED HGEIDLPALI GAVKKFSMSM PADPAHRTFN GLKRGLDGRF DDDELVDCIA
     TAIEQPGGAF GAQNVPRIMK PVEILGILRG RKWNLAGLNE FRKHFGLKAY TTFEDINSDP
     QVSSALRNLY QHPDHVELYP GIVAEEAKTP MTPGVGIAPT YTISRVVLSD AVALVRGDRY
     YTTDYHPGYL TQWGYNEVNY DFKINHGCVF YKLFNRAFPN HFKRDSVYAH YPMVIPSENR
     KILTNLGRVD DFTFDRPRFA TPTVQVSSIS GIKHVLSNDE KYPVHWQAGL NKLMGDPGRA
     VSASGGRRHL DELIYKDSWK ASIKAFYAST AQRLLDDKAY KLAGRTHCDV VRDVGNLVHT
     HFVARLFNLP LKSADNPRGV FSEQEMYTTL STIFMSIFFD TDPVKSFPLW HEARKQASKL
     AGIVETNVKI TTLLGTTGLF TGKPKDNTLA AYGVNLIKGL SKAGLKAHDI AWGQILPTAG
     ALVPNEAQLF AQAVDFYLSP RGQPHLDEIY RLAAQGTSNE SDSLLLGYAL EGIRMSGPPG
     FCREASEADA YSDADGGETR IQAGDRIFVT FDAAVRDGSY FPNAGVVDPR RPVESYVHYG
     AEPLTRLGTE VSKLALVELF RALFRKKGLR RVAGPQGELK RVAGPSGSTV FMTEDWGATL
     PFPSSMKVIW DE
//