ID D8RF82_SELML Unreviewed; 478 AA.
AC D8RF82;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Uncharacterized protein CYP74L1 {ECO:0000313|EMBL:EFJ28824.1};
GN Name=CYP74L1 {ECO:0000313|EMBL:EFJ28824.1};
GN ORFNames=SELMODRAFT_92382 {ECO:0000313|EMBL:EFJ28824.1};
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:EFJ28824.1, 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; GL377578; EFJ28824.1; -; Genomic_DNA.
DR RefSeq; XP_002969700.1; XM_002969654.1.
DR AlphaFoldDB; D8RF82; -.
DR STRING; 88036.D8RF82; -.
DR EnsemblPlants; EFJ28824; EFJ28824; SELMODRAFT_92382.
DR GeneID; 9645914; -.
DR Gramene; EFJ28824; EFJ28824; SELMODRAFT_92382.
DR KEGG; smo:SELMODRAFT_92382; -.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; D8RF82; -.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
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; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF49; INACTIVE LINOLENATE HYDROPEROXIDE LYASE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT BINDING 423
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 478 AA; 52926 MW; 1A077EA1377B6D32 CRC64;
MEVPGSYGVP WLSAIKDKLD FHYIQGEVEF FKSRVKKYKS TVLKVNFIPT PPGFPNPAGI
ALLDQRSFPV LFDNSKVEKR DVFVGSYKPS DAFTGGVRTL AYLDTEEEKH ARLKEFVFQI
LKSTGPRFLS EFEAEMASAL AGVEAEMESG TKNSIAVSSK LLDLAFNFMV KAVTGGADPS
SQFGSYGPLL MQLWIGVQFA PISPRTQLPA VIEELLLRSF PLPPLIVRWP YDRIAGFLSD
NATALIDMGE KQFGLDREEA LHNLVFVVGV NGFLGFSRML PSLLFYVASQ SEAFQQRLGG
EIRGAMGDDG SARKFMAAVE RMPLLKSTVL EVMRIAPPVL YQYGRARREF VVESGDGREF
LIRKGELLGG SQALVCRDPT VFDSPDEFVP DRFLGAQGRE LERCVFWSNG RNTDSTSSAN
KQCGAKDFVE TIGRLFVAQL YLRYESIELG PDSKPDSPVI KSLRKISVAT RTGNKVSA
//
