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Database: UniProt
Entry: A0A135TV05_9PEZI
LinkDB: A0A135TV05_9PEZI
Original site: A0A135TV05_9PEZI 
ID   A0A135TV05_9PEZI        Unreviewed;      1106 AA.
AC   A0A135TV05;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:KXH52000.1};
GN   ORFNames=CSIM01_07819 {ECO:0000313|EMBL:KXH52000.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH52000.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH52000.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH52000.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL   Submitted (FEB-2014) 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:KXH52000.1}.
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DR   EMBL; JFBX01000049; KXH52000.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135TV05; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000070328; 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: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   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}.
FT   REGION          1..75
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        37..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         414
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   1106 AA;  124006 MW;  9629993DC00CD06C CRC64;
     MKTSRNGSNS SAGADTYKPT TTGPSMKNPH PGPSRADPRY GSHDVKKKGF SDIRQASKRP
     LPTQNGDGTY PSDLTRPTMV QNLKALQAAD LKTLVQIIKS KIKREKIQDD KTMIMERTIQ
     IVAKLPHNSR LREQLTNTFI EELWGSLDHP PMLYMGDEYK YRQADGSYNN PMLPRLGAAG
     GPYARSVKPR IVTLGAMPDP GLIFDAVMGR TSYKKHPNNV SSILWYWATI IIHDLFWTDF
     KDMTKSKTSA YLDLSPLYGS NQEMQNSIRT FKDGKLKADS FADKRLIGMP PGVCVLLIMF
     NRFHNHVAEN LAAINEGGRF TPPSKDLNEE QTAAALKKYD EDLFQTARLV TSGLYINITL
     VDYVRNIVNL NRTNTTWTLD PRQEAGIDAG TPDGAEAGTG NVNSAEFNLC YRWHSCISDK
     DDKWIQKFYG KLLGNKGQMS PQEMACVFGQ FEKSIPDDPG MRTFAEYERG ADGKFDDDDL
     VDCISSAIED CAGAFGARNV PQVMRPVEIM GILQGRKWNV AGLNEFRKHF GLKPHETFED
     INSDPAVADQ LRNLYQHPDY VELYPGLVAE EAKTPLTPGV GIAPTYTISR VVLSDAVCLV
     RGDRYYTTDY NPRHLTQWGY KEVEYDLNVN HGCVFYKLFL RAFPNHFKGN SVYAHYPMVI
     PPENQQILTD LGRVNQFDFE RPKPIPTRTN ITSFGGAKYV LDSQSRFKVT WDEGLSFLMG
     KGGGRFMLSG DTDFHTGQKK CMSAQLYQDD WSSHVKRFYA EITEQLLREK SYKLAGQTHV
     DIIRDVGNIA HVHFAARVFN LPLKTHKNPK GVFTEQEMYQ ILAVIFVCIF FDIDPAKSFP
     LRQAAKEAAQ SLGKLIETNV KITTKTGLRG IFTGSADKQD PLALYGTNVI KGLDKAGLST
     YDIAWSQILP TSGAMVPNQA QVFAQAVDYY LSPPGSKHLD QIHAVAKAPS TKESDAVLLG
     YAMEGIRLAG TFGSYREAAQ DDVIVEDGGR EVPVRRGDKI FVSFVSAAKD ANHFPHPEEV
     NPRRPIDSYI HYGLGPHSCL GRDVSQVALT EMFRVLFRKT NVRRVPGPQG LLKKVPRPGG
     FFVYLKEDWG QIWPFPVTMK VMWDDE
//
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