ID F8NX73_SERL9 Unreviewed; 507 AA.
AC F8NX73;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SERLADRAFT_468039 {ECO:0000313|EMBL:EGO24548.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO24548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO24548.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; GL945434; EGO24548.1; -; Genomic_DNA.
DR RefSeq; XP_007318567.1; XM_007318505.1.
DR AlphaFoldDB; F8NX73; -.
DR GeneID; 18819343; -.
DR KEGG; sla:SERLADRAFT_468039; -.
DR HOGENOM; CLU_001570_2_3_1; -.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000008064; 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; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11065; CYP64-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46300:SF7; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
SQ SEQUENCE 507 AA; 56306 MW; 0A60E02A56ABC5E1 CRC64;
MPCTMGYLDI ALAALGVYLI KRLFQAKSRL PLPPGPKGVP ILGNIFEMPS EKAWLAFEKL
SEKHGNLSSM NIFGHCLILV NSAAIAEELL DKRSVSYSDR PPMVMAGELS GWNKALLMTK
YGERFRQIRK YFHQAIGART SIRAFVPIVE HETLRFAQKV LCDDTRLEAH VRKTAGAIIL
RISHGYEVQD GIDPLVELAD KALEQLSETA APGAYLVDII PILKYIPEWF PGAGFQKTAK
RYAKTLQDAA DQAHNYAKTQ IASGIAPNSF TSRLFEGCSL TETEEDNVKW AAASVYLGGS
DTTVSANYAF FLAMTLYPDV QKKAQAELDV VIGKDRLPTY ADRGSLPYVE ALFKEILRWN
IVAPLTIRRA SKDDVCGGYF IPKDAHVIVN IWHILHDERT YVNPMEFNPE RFLASEGREP
ETDPRNTCFG YGRRICPGLH LAEVSVFMTC ALSLAVLDVR KTVENGVEIT PEIEYLGGSI
CHPAPFKCSI KARSIQAEAL LSQSNDS
//
