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Database: UniProt
Entry: R1EZM3_EMIHU
LinkDB: R1EZM3_EMIHU
Original site: R1EZM3_EMIHU 
ID   R1EZM3_EMIHU            Unreviewed;      1219 AA.
AC   R1EZM3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Lipoxygenase domain-containing protein {ECO:0000259|PROSITE:PS51393};
GN   ORFNames=EMIHUDRAFT_205326 {ECO:0000313|EMBL:EOD26334.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD26334.1};
RN   [1] {ECO:0000313|EMBL:EOD26334.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD26334.1};
RG   DOE Joint Genome Institute;
RA   Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA   Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA   Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA   Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA   Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA   Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA   Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA   Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA   Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA   Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA   Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA   Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA   Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT   "Genome variability drives Emilianias global distribution.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000013827}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA   Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA   Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA   Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA   Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA   Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA   Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA   Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA   Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [3] {ECO:0000313|EnsemblProtists:EOD26334}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; KB865188; EOD26334.1; -; Genomic_DNA.
DR   RefSeq; XP_005778763.1; XM_005778706.1.
DR   STRING; 2903.R1EZM3; -.
DR   PaxDb; 2903-EOD26334; -.
DR   EnsemblProtists; EOD26334; EOD26334; EMIHUDRAFT_205326.
DR   GeneID; 17271879; -.
DR   KEGG; ehx:EMIHUDRAFT_205326; -.
DR   HOGENOM; CLU_270899_0_0_1; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR036226; LipOase_C_sf.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF153; LIPOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        422..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        511..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        550..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        658..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          884..1112
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
SQ   SEQUENCE   1219 AA;  130463 MW;  213EA64E8A0DDA70 CRC64;
     MRATRHLLDA HLLDGTLAVS RARQRRRSHM PSCCFSALVI SGTSAILLAG ALSSLDGALK
     FARLDLALRS SLVDTAGADL EAGLPTAARL ALLAAFEVPV AVATGMDPAA HLDVYVRASG
     RQPFLFGKGI AVPGYDDVST LVSSPQQERR AMVLAHPVLI ADPVPPACMG GGTLIYLSTG
     AKHTALRRAI GRAVTGFALK RGRGPPLLFP RGAAPAEWDS RAVRETAPLL GAALDSQANA
     TLETRLALKA AVLASPLGGR LRKANRADKL DADELAQQVA DGLLFAGGYG TTHLTLAALE
     RISSDPALYA DPDAFLVESA RLDPPVTSVS AIAPKGGQQL QGPGGGQLRV AQGVPMQLLL
     SHANRDPAVF ERPYAFDPSR RNLDKVLSWN GVDAAGSCDY SASDRPSEDL ELRNEHDDEA
     MYAYYGAGLV NIVLGVLALI VLGWFCLSQR LAFGALYVKG DAGIIRVQSW LGLLHYLGQA
     IAAFSWLRLH AVVTHADDAR ARAESASALR LCFGVMAIFV GAFAVFGTAA ACVLFVPAAA
     KSWIAIAMFW WRHGGVLVLA ACAFIAFWVG QVIAEQRGMS LIDYEAGSGI GVTLLARGLL
     GAEAAPHAWK YEVFARGFLA PSVYFAAAAH IDRVQGRGLG RAYPSELFMR RALRFKHSAP
     VLLALALAAI HSFAIPRSFG DITGCGEGGG EAAGPECAVD PTGGLDQYTK VYFSIIHLLD
     DGSQPGPSFV QAPNRTVQPL PKEQVVPGLV LPSYDEDEGL VTSRALANQA FSGYVKDGRL
     YPLEDLDLPW PEKDGAIEAL MGRLSGSLAP AELYDYDANI GGDSLIGDAG NPDFPPPASR
     RWFRTHSLEM CARHADFTYL APLTVRPGFE RYGAKATFDA AARPVSIWWS HGEKEVRPDD
     AAWTHAKFAF RSSLLTGVTL KDHLAATHLT IAATLVSASR DHLPATHPLR RLLKPFTYRT
     IALSLLHHTV ALDAAGLEAG FAFAFNRTRD TFDPANPARF LEYPLEYPLS SAAECAATPP
     SSQAACADEA DELAAFAADG TRYRAAVREY VGRYVGIYYA DDAAVGSDVV LASFWAALVA
     HFPRIPPLSS REALVEVLTG FVFHVTAGHR HVGAAYSAVK DPRYAGAKIR PGRDMSDVQA
     AVQVLAIALV TGFKQPMLLG DYSHVFLRDG HRNATRALWS DFQAKLLQVS AEVDERNRGP
     RRFKVRAFDP REMATSVSI
//
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