ID D8RNJ2_SELML Unreviewed; 475 AA.
AC D8RNJ2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Uncharacterized protein CYP74L2 {ECO:0000313|EMBL:EFJ25872.1};
GN Name=CYP74L2 {ECO:0000313|EMBL:EFJ25872.1};
GN ORFNames=SELMODRAFT_98717 {ECO:0000313|EMBL:EFJ25872.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ25872.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; GL377585; EFJ25872.1; -; Genomic_DNA.
DR RefSeq; XP_002972651.1; XM_002972605.1.
DR AlphaFoldDB; D8RNJ2; -.
DR STRING; 88036.D8RNJ2; -.
DR EnsemblPlants; EFJ25872; EFJ25872; SELMODRAFT_98717.
DR GeneID; 9651730; -.
DR Gramene; EFJ25872; EFJ25872; SELMODRAFT_98717.
DR KEGG; smo:SELMODRAFT_98717; -.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; D8RNJ2; -.
DR OMA; VYWSNER; -.
DR OrthoDB; 447408at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
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; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR CDD; cd11071; CYP74; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286:SF255; ALLENE OXIDE SYNTHASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|PIRSR:PIRSR602403-1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT BINDING 432
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 475 AA; 52829 MW; B884864E2152B333 CRC64;
MASSGSSNLP TKEVPGSYGL PVLGAQKDNL DFLHLQGEVE FFKSRVAKYN STVFKVNFIP
GNPAFPDPRG IALLDQSSFP VLLDSSKVDK TNVFTGSYKA SDDFTGGYRV LSYLDTTDPK
HATLKNFAFE VLKRNGRKFL PEFQSAFHAA FDAAESELSS GKNKADMAPL LNQLAFQFLA
KSIVNVDPLT TKLADQGPTH LLRWIGIQFA PVAPGNSTPL PGFAEDVVIR TAPLPFLLVK
ADYDKLCEFF QLATEMLDMG EKEFGLSREE AVHQLLFLVG MNSWFGFSAR VLPNLLYRVG
TLGAEFQKRL GDEIRAAIDV SDPAGSFYGA LEKMPLLKST VLEVFRFDPP VLYQYGRPRE
DMVVESHDAK FVIKKGQLLG GSQALVCRDP KVFEEPDQLI PDRFVGKEEL QANVFWSNGR
NTKSPTADDK QCAGKNFVET IARFYLVQLF ARYKTFELSE DSTLNTPFLK SFARN
//