ID Q6WP49_BOTFU Unreviewed; 510 AA. AC Q6WP49; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 24-JUN-2015, entry version 57. DE SubName: Full=CND5p {ECO:0000313|EMBL:AAQ16576.1}; GN Name=CND5 {ECO:0000313|EMBL:AAQ16576.1}; OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=40559 {ECO:0000313|EMBL:AAQ16576.1}; RN [1] {ECO:0000313|EMBL:AAQ16576.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T4 {ECO:0000313|EMBL:AAQ16576.1}; RX PubMed=14651630; DOI=10.1046/j.1365-2958.2003.03798.x; RA Viaud M., Brunet-Simon A., Brygoo Y., Pradier J.-M., Levis C.; RT "Cyclophilin A and calcineurin functions investigated by gene RT inactivation, cyclosporin A inhibition and cDNA arrays approaches in RT the phytopathogenic fungus Botrytis cinerea."; RL Mol. Microbiol. 50:1451-1465(2003). RN [2] {ECO:0000313|EMBL:AAQ16576.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T4 {ECO:0000313|EMBL:AAQ16576.1}; RA Brygoo Y., Faivre B.; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {ECO:0000256|RuleBase:RU000461}. 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; AY277723; AAQ16576.1; -; Genomic_DNA. DR ProteinModelPortal; Q6WP49; -. DR STRING; 40559.EDN24585; -. 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:UniProtKB-KW. 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; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|RuleBase:RU000461}; KW Iron {ECO:0000256|RuleBase:RU000461}; KW Metal-binding {ECO:0000256|RuleBase:RU000461}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}. SQ SEQUENCE 510 AA; 58162 MW; A591F786FC5D565C CRC64; MGLLSDVINN FLPETPLAWA ALILASFTLY SVQLVVRRLY FHPLSKIPGP FLARSRYWYE FYQDIILGGI YVKNYAALHE KYGPVLRASP DRVHVSDPDF FHEVYSSGSK YMKDPAFFQA AGGIPEALPA IVDVEYHRRR RKLINDLFSA KSMEALSHLV LKVVQNALSK AHEHHEANKV LDIQRLYTGI TIDTIMQVLC DRTLNFIDAK EEEEPPFLAT LRTFSENFFL LKHFPILIWM ALNIPKSIAQ KLIPGEFEFR ASINQWIRDR ASEHELGVEK AEDGRKTVID LLLRPEDGGR PLTHQAVEDE TYSFAFAGTH TTSHTMSMGT YYLLSHPAKL QKLRDELKPI PKNDQGLYEY KTVRSLPYLN ACIKESLRMS SPVPGILPRL VPAEGMTWRG HYLPPGTSVS SSIYSVHTDP NIFPNPEQFI PERWLANENL DHYLVVFGKG SRACIGLNVA WMETYLTFSN FFTSLNMTLF ETNEQSTDWT DCGNAMIKKH VRVKVDSLAS //