ID A0A165NL08_9APHY Unreviewed; 664 AA.
AC A0A165NL08;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KZT67097.1};
GN ORFNames=DAEQUDRAFT_729516 {ECO:0000313|EMBL:KZT67097.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT67097.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT67097.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT67097.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV429080; KZT67097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165NL08; -.
DR STRING; 1314783.A0A165NL08; -.
DR OrthoDB; 3640568at2759; -.
DR Proteomes; UP000076727; 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; 2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; Cytochrome P450; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 214..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 73543 MW; 2C8134EF04B31540 CRC64;
MLHDLLSSSL LVGAGLVLYA LSTFLLLVLR QALSPLRNLR GPSSPSFFMG NLREMHDQEN
TNLVVRWEQQ YGTTFVYRGF MGGARLMTTD PVAVAHILGR GYDYPKPDFV RDNLSNMAAG
EHGLLTVEGE DHRRQRKILG PAFTSAHIKS LSPIFWNKAV ELRNIWLDIA SSSQSHAAPS
DPFHVIQSSK APKGDRAFAI TTSVLPNPFS SFMPGKTTAR GQNNHASITR PDSTTGSTSE
GSSARVDVLA WLARATLDVI GEAGFGYRFS SLASTVKDDE KVEKENELAR AFGVIFSSAR
KFRVMTILQA WFPALRRFRR EGAVEREARE TMRRIGLSLI EKRQAEATKE QAAALHTRPT
PFPANAELTP GTEHATAGRD LLSVLIRSNI SSVPSQRLSL EETLCQISTF LSAGHETSSA
ALTWTLYALA RAPDVQARLR RELRSIPFPS SAPPAEAIAA ILDHPYLDAV VRESLRLHAP
VTSTMRVAGA DDVVPVARPF LDRRGRPCNA IHVRRGDIIT VPVQAMNKSK EVWGGDAEVF
RPERWLVRGE DRDWSDEEAE ERERREGKPG RGQKRAGAPG LWGNMLTFLN GNPLNGNRAC
IGFRFAINEI KIFLYVLLHD IEFSIDPTIQ IEKKINVVTR PAVRSEPHMG NQMPLNIRRI
ASGS
//
