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
//