ID J3KJA5_COCIM Unreviewed; 1080 AA.
AC J3KJA5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:EAS36125.3};
GN ORFNames=CIMG_01479 {ECO:0000313|EMBL:EAS36125.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS36125.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
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).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; GG704911; EAS36125.3; -; Genomic_DNA.
DR RefSeq; XP_001247708.1; XM_001247707.2.
DR AlphaFoldDB; J3KJA5; -.
DR STRING; 246410.J3KJA5; -.
DR GeneID; 4567715; -.
DR KEGG; cim:CIMG_01479; -.
DR VEuPathDB; FungiDB:CIMG_01479; -.
DR InParanoid; J3KJA5; -.
DR OMA; KIQWDGD; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000001261; 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; PROSTAGLANDIN G/H SYNTHASE; 1.
DR PANTHER; PTHR11903:SF37; PSI-PRODUCING OXYGENASE A; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00067; p450; 1.
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:UP000001261}.
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378
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 1080 AA; 121595 MW; 87E6EE3F00B60131 CRC64;
MVLDSSSRRG VLDDLAKYFP HFGGIANGSL WPITPDSGHH SPSQGPTGGL LQDLGSLDVK
DVGTVLELIK NTASGAPVED KRYIMERVIQ LASSLPSTSH NRTTITNTLL AQLWNDLSHP
PVSYLGRDVI YRQADGSYNN IYWPQIGKAG SNYARSVQPK SIQPASRPDP GLLFDGLLAR
QQFKEHPNKL SSVLFYLAAL IIHDLFRTDP TDSSRNMTSS YLDLSPLYGC NQEEQNQVRT
FKDGKLRPDC FSERRVFGFP PGVGVLLIMF NRFHNYVVQN LAAINENNRF RKPDESDADA
CAKYDNDLFQ TGRLITCGLY INIILKDYVR NILNINQTDS DWSLDPRSDV KELLSHKPVQ
EAGGNMVAAE FNLVYRWHSC LSDRDDRWMQ EIFEKALDGK DLDTIGMPEF LGKIRKLQSS
IPDDPMLRPF ANLERQSNGS YDDNDLVKIL TESIEDCAGS FGARHVPKVL RSVEILGILQ
ARSWNLSSLN EFRKYFNLAP HTSFEDINSD PEVVEQLRHF YGHPDNVELY PGIVVEEGKP
RIVPGSGLCA SYTISRTVLS DAVALVRGDR FYTVDYTPQN LTNWGYNEAN YDMTVNNGHI
FHKLILRAFP RHFKPDSVYA HFPFVIPSEN KKILSDLGLA EKYSWERPGA VPHPTVILSH
GACNAILHNK EDFKITWGEK VKHIMARNSI PYGADFMLSG DEQVHEDSRQ MMKKALYIED
WCGQVRAFYE RITLELLHSK SHRISGVSQV DIVRDVANLA AIHFSSNIFL LPLKTEGLPH
GVFTDTELYR SMALILNYIF YDVDPTQSFK LRERSRSESQ KLGELVMLNV QAISKTGFIG
SIIDKLHGNE ALANYGVHMI RRLLATQMPI DELVWTHILP TAGGMVANQA QLFSQCLDFY
LSEQGSRHWP EIRRLAGLNT KEADDLLLRY FLEGARIRST VALYRDVSKD CKVQDHGKEV
NLHAGQRIIC NLMSACKDPE VFPEPDEVDL TRDLDSYIHL GVGPHECLGK GMVQIGLTTM
LKVVGRLDNL RRAPGPQGQL HSIPGPGGIP LYMSEDESEV SPFPATMKVL WDGELPPLPQ
//