ID L8WH51_THACA Unreviewed; 1077 AA.
AC L8WH51;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:ELU37245.1};
GN ORFNames=AG1IA_08723 {ECO:0000313|EMBL:ELU37245.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU37245.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU37245.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
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:ELU37245.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFRT01002772; ELU37245.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WH51; -.
DR STRING; 983506.L8WH51; -.
DR HOGENOM; CLU_002329_0_0_1; -.
DR Proteomes; UP000011668; 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; 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:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 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:UP000011668}.
FT BINDING 376
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 1077 AA; 120190 MW; 48B3BEED1DCF781B CRC64;
MSEPGLAYRA VDASLGALSH LATSIDNSLR PVTANANAYS RDPDQEVNAA TAVIEGFRRQ
YSVVDAIQNS KSLDDRKMLL EHALVFMSRL PRGSALAQKG QDAVISMLYK DLPHPPATYV
GDAYRFRAAD GGNNNLLIPD LGRAGTPYSR SVPQTHPLPP AELPDPELVF ECLLKRDKVT
PHPAGLSAMF FSFATLVIHT CFRTNHRDVT INETSSYVDL APLYGNNQED QDSVRRWDGT
GRLKEDVFTE NRLLFLPPVS QRVTLLTRRP ETWQFIARKL FLINEEGTFR DPETLKEEQR
KQQDHVLFNT ARLINVGFFV SIVLGDYLAS ILGIVREGSD WSLNPFQDIV QSERNHVPRG
EGNSVSVEFN LLYHWHSTTS AIDEQWTEGV FRKIFGDKPF EQITPGEFAK ASALVASAEP
DKAKWEFGGM KRGSDGRFND AELAQTIINA TSHVASAFKA RGTPPVLRVV EILGIMSSRK
WGVCSLNEFR KFIGLKPYDS FTEWNSDPEI ATAAMRLYKH PDNLELYVGL QAEEAKPVVP
GAGLCPGYTI SRAILSDAIT LTRGDPHTAN NLTCWGFDDA TRDTENPSFG GMLGKLFYRT
LPGQFPENSI YLWFPLMTPD AMKTNFTKVG IAGDYDFSRP TAPQPVQDVT SRAHVMDVIM
ETACIHTPYG KKVQAMFDKD PGFFLALNDE HDHTFKTIIY QNLIAPSGTY FQSYFYEVTK
TLLQDMSYTL GSHQSKCLDI VDVFENVVMR FVSEEIGGLS LKSESNPRGL YFERCGSNIL
AHRHVFTDVD IQHIFRIAKN AKSFSKRLLL HINQTYIAPI TERIFGFFSG TGRPSYDFMR
RLHKTGKPKD QLCKAVLAAI VASFEYVPAL INVVNFYLDP AQAEHKTQLV ALASSKDPQA
NNVIAGYVRE FSHARRVVVE NTSVKGSNYK RGDSLFLSIA DSNLDPDTFP NPKSVDPRRP
ADSYTLMGDG LHRCFSDEFV HSTMACAVRA VFQLNNIRRG PGKSGILKRF TDSDGTTASS
CYLNSKQIIT PFPTSLTLQI ASRKYVASPP SSPTTHKVEN KLLEKMLSFN SGRATVI
//
