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Database: UniProt
Entry: A0A0G2FU59_9PEZI
LinkDB: A0A0G2FU59_9PEZI
Original site: A0A0G2FU59_9PEZI 
ID   A0A0G2FU59_9PEZI        Unreviewed;      1770 AA.
AC   A0A0G2FU59;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE            EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN   ORFNames=UCDDS831_g07636 {ECO:0000313|EMBL:KKY15413.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY15413.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY15413.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY15413.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY15413.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY15413.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-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:KKY15413.1}.
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DR   EMBL; LAQI01000195; KKY15413.1; -; Genomic_DNA.
DR   Proteomes; UP000034182; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:0007155; P:cell adhesion; IEA:InterPro.
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; 2.60.40.2080; -; 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; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR037221; H-type_lectin_dom_sf.
DR   InterPro; IPR019019; H-type_lectin_domain.
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; PF09458; H_lectin; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF141086; Agglutinin HPA-like; 1.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1496..1547
FT                   /note="H-type lectin"
FT                   /evidence="ECO:0000259|Pfam:PF09458"
FT   REGION          1326..1474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1410..1424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1451..1465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         580
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   1770 AA;  192536 MW;  182E8D3F496FB004 CRC64;
     MAEPCNGGAA ILPAKGLGPL AFLIPLLGLL AVAVFTKFVR KRPLSSLVPN LKSFNPKSLL
     DPKNLHLPKL SLPKSFPSLP KLPFSLPKPH FSLPNAKLPT SPVKSPLAGL ANLPNGKLLS
     SHLPKGHFLS GKVPKSLLPE LPWYLKFLSP TGLVKNLVFK VFNLHKVPGL RDIVSWFMKP
     KGFVPKGTLA TLSSLRSIRP GLLSKLNPFN LKIFNKKALA SQADDEKFQA GEPYGDPDVV
     SSNLVEDLRT VGFSAATKDL KTLIEVFKAK GKPQNDREML MEKMIALTAS LPRHSKTRDK
     LSGVIIDTLW SSLQHPPLTY MGEKFQYRTP DGSYNNPMNP DLGKAGSHYA RSVPRIKSQH
     GVPPDPGLLF DLLMARSDET FKENPAGISS MLFYHATIII HDIFRTNRFD NNISDTSSYL
     DLAPLYGSSL EDQLKIRTME KGLLKPDTFH ERRLIGQPPG VNVILVMYNR FHNYVADVLL
     KINEGGRFTL VPGETDEEKA AAIAKQDNDL FQTARLIVGG LYINISLHDY LRGLTNCHHS
     ATDWTLDPRI AASRLFDPDG IPRGVGNQVS AEFNLLYRFH SIISKKDETW LNEFLSSLFP
     GSSKPLDELT PQEFVQGLFA FEQTIPADPS KREFGNLKRG PDGRFADADL EREMTAAMED
     PAGLFGPRMV PKFLKIVEIT GILTARKWQL GSLNELRDFF KLKRHDTFED VNPDPAVADL
     LRKLYDHPDM VEMYPGMFLE DAKPRMDPGC GGCPPYTVGR AVFSDAVTLV RSDRFCTLDY
     TAGNLTNWGF NEVAADYDVL GGSKFYHLFQ RALPGWYPFN SLHIMQPMFT RQMNEQIATE
     LGTIADYTTK GPAPPKKPIL LVKHSTITKM LEDQANFHIP WVAYEGLFPG KKSFAGFMLG
     GDSPANTAQK KLVKDVLYTP AEFGRLLADT AVAYGRKLIK RECLELKKDL AQLDIIRDVA
     IPLNTKLIAD LWCQDLQTDE NPTGTLSTPQ LYKYLMDVRT FGFNNNDPAM TWRRRLWARE
     AAEVLIPSTI KAIKEGTASL ASPGGLLKRA GAGVAKGLGK VPLLGKLVPQ AKEEGGSLRW
     YGHNVAREIM AAGRTLEETA DICWLTALAG VGAPVSMFAD VLSFFLRPEN VHHWEQIQNL
     ATSGADRTAT DKTLRQYVLE AERMVSNLRG ARVCVGATEI DGQKFAPGDA VVCLFGPACR
     KEGGLVPEPE SFQLDRPASA YIHWGAGPHE CLGKEIAIGI VVSLVKVCAE LKCLRPAPGD
     MGELKSIMVG TERCYLNDSW SWLTFDPTTW KVHFDGYGKG VYRESAAAAA KGRDLKALYS
     TLVKQNSKGP KGVTPGGLLP PTQAAAAPNG VTNGYKEEEP VAAKPKPNKP APAATNGASN
     GEEEEGEGGA VQPPAANGAS KPAQQPDGWS FDGIDNNNDN NNDDGGGAVK PPAAVEVDGK
     DSNPAPPAEE QTEPEKPKEE EDPPPPPPAD PDVLQTGRLA KKADSSDEGG LGSYTASVTF
     DKPYSTPPRI FLGFATLDIG ATAAQSPNFH QEARDVTTAG FTLAVAVAPS SAPLRQLDSV
     WLVVPTDAAH RDVLVGVWDT SKTPGKPVGS GGTAVDSAFI PLRCADGEPP APGRRAVVPW
     LAGFALDTAP AEPFGVKVDA RSATNDAGEP GAIVSFRTPS SLVPRLPTSV RVNFLVFPPN
     GALGLSPASA RAEFPNVDTD SITVLATANK PIRSVVGIDM FQYVEDAEAI CLRVVDRQKE
     PDEAKYSLES WGEPLVHDLS AGIVKIPKTD
//
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