ID   C4JKV3_UNCRE            Unreviewed;      1104 AA.
AC   C4JKV3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Linoleate diol synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UREG_00168 {ECO:0000313|EMBL:EEP75322.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP75322.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; CH476615; EEP75322.1; -; Genomic_DNA.
DR   RefSeq; XP_002540655.1; XM_002540609.1.
DR   AlphaFoldDB; C4JKV3; -.
DR   STRING; 336963.C4JKV3; -.
DR   GeneID; 8441388; -.
DR   KEGG; ure:UREG_00168; -.
DR   VEuPathDB; FungiDB:UREG_00168; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   InParanoid; C4JKV3; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000002058; 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; 2.
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; 1.
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   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:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         401
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;  124357 MW;  1C5DF5A3F7C9BA2C CRC64;
     MSATNGTSNG AHHANGAAPS SKPATNSTPN TKHSNRGVKR PEVESTFKQY AQLIHAARRP
     LPTQSGDGSY LRKSKAKSSL LKDLRSMGPR GWGTLLAVRK SKRSGDLIDD KTYIMERVIN
     LVAGLPPEST MRTQLTNAFV KELWDTLPHP SLPAFGDEYM YRSADGSNNN PLFPKLGAAN
     TPYARSIIPS SIQLGALPDP GLIFDSLFAR EEFVPHPNGV SSVFFGWASL IIHGRAKSDA
     NFQRWKIETR LLLRTQASGP SPRLQCYSCH VQPVKLLQLS TGGGKANNFR FHNYAAEQLA
     HINEGGRFNK PRPGLSPEEL AKAWAKYDND LFQTARLVTC GLYINITLYD YVRTIINLTR
     SNTTWCLDPR VNMRTNATPE AASSGVGNQC SVEFNLAYRW HSCIGQQDER WTEDIYQELF
     GKSAETITMP DLLMGMKKWQ MELPKDPAQR SFAGLERKPD GRFNDDDLVK IMTESIEQIA
     GSFGPRNVPK ALRAVEILGM QQARKWGCGS LNEFRKFFGL KEYTTFEEIN SDPYIADQLR
     HLYEHPDHVE LYPGIVAEEP KIPMIPGAGI CPTYTLSRAI LSDAVALVRG DRFYTTDYHP
     KNLTNWGFSE THYDLNINQG CMFYKLMLRA FPNHFQPDSI YAHYPMTIPS ENRKIFATLG
     RENHFSWEKP SFIPPRINLT SYLGAKTVLE NARDFRVTWG EATGFLFGKE GLNFMLSGDS
     PKHAKQRQVM GKALFQERWK QQVKEFYEDI TIKLLKQKSC TIAGVHQVDI TRDVGNLAHV
     HFASNVFSLP LKTEENPRGI YTEHEMFMIM CVVFTCIFFD LDPAKSFPLR QAARTVAQQL
     GKIVEAYVKS VKATSVISGL LDRFRKTETA LQDYGVHMIR RLLASGLSVS EVAWSQIMPT
     AGAMVPNQAQ VFTQIMDYYL SDEGRIHLPE IQRLAQEDTP ESDDKLLHYC MEGIRLNGTF
     GSYREAATAM EVDDDGQHVS IKAGDKVFVS FVSANRDPDV FPNPNEVRLD RPLDSYIHYG
     QGPHTCLGRD ANMVALTSML RVVGKLKNLR RAPGPQGELK KIPRPGGFYI YMREDHGSYF
     VFPMTFKVHF DGELPDFPKR KAPS
//