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Database: UniProt
Entry: R7SZM9_DICSQ
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Original site: R7SZM9_DICSQ 
ID   R7SZM9_DICSQ            Unreviewed;       528 AA.
AC   R7SZM9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:EJF61644.1};
GN   ORFNames=DICSQDRAFT_147086 {ECO:0000313|EMBL:EJF61644.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF61644.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF61644.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF61644.1,
RC   ECO:0000313|Proteomes:UP000053319};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617}.
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DR   EMBL; JH719409; EJF61644.1; -; Genomic_DNA.
DR   RefSeq; XP_007365739.1; XM_007365677.1.
DR   AlphaFoldDB; R7SZM9; -.
DR   GeneID; 18836630; -.
DR   KEGG; dsq:DICSQDRAFT_147086; -.
DR   HOGENOM; CLU_001570_14_10_1; -.
DR   OMA; FWPGTQN; -.
DR   OrthoDB; 2117278at2759; -.
DR   Proteomes; UP000053319; 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   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; PTHR24305:SF187; -; 1.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         472
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   528 AA;  59487 MW;  C09C087493D060B2 CRC64;
     MLVDSDWVTA VHQVFRKIDT YSTLFHAIFL LCPPVLITSF VTDATSSSIY QRTLVSCYGV
     FYLALALSIV AYRLSPSHPL ARYPGPFWYR TSSFCHAFLS VSGQRNTYLK ALHERYGDVV
     RTGRVVYIGA FLGQIFPLVG ISTVEEHVRR RRAWNRGLGP AALKEYEQLT TQRARQLADA
     LEQQRRVSLE KWFDYFAYDL MSDMAFGGGS ELMLEGDKDG VWSILQQGTR AASFFSTVPW
     LGLCIGKIPV AVRPLHIFIT HGKEAVVKRM RCGSTTRDLF HYLNNEDLPD KEPAPMQQLV
     DDGILAVTAG SDTTASALTS IFFCLLTHPN VYASLCEEVD TFYPKGEDAF VTKHHGTMPY
     MNAVINEALR LYAPITTGGS RQVPRESDGV YAGSIYLSAG TTVYFPAYSL HRDARNFSFP
     DAFWPERWLI ASGQVALEDA RPPPSSTLKP TSSKFAHEEI AFIPFSAGPM NCVGRGFAMQ
     EMRMVLCALA QRFRFRPREG WDIREYETHY KDYFVSTRPP LPAIVQPR
//
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