ID K2SFW0_MACPH Unreviewed; 485 AA.
AC K2SFW0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:EKG21329.1};
GN ORFNames=MPH_01321 {ECO:0000313|EMBL:EKG21329.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG21329.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG21329.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG21329.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG21329.1}.
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DR EMBL; AHHD01000052; EKG21329.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SFW0; -.
DR STRING; 1126212.K2SFW0; -.
DR VEuPathDB; FungiDB:MPH_01321; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_11_1; -.
DR InParanoid; K2SFW0; -.
DR OrthoDB; 1943676at2759; -.
DR Proteomes; UP000007129; 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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11058; CYP60B-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; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF240; CYTOCHROME P450 MONOOXYGENASE STCF-RELATED; 1.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 485 AA; 54615 MW; 4C64CEF2E1E04FFF CRC64;
MSSILDISKS LPSLPNVSGA DRLSTSMLPA LVLLSLLFVI LTKGLYNVYF HPLSKIPGPF
LSAFTELVYL WYWVRGDLVK HLCSLHQKYG KTVRIGPNRL SFIDAEVWKD IYGYKVGGNK
KAAIMKDPQM YGPESNGRFS ILAKFDDTEH KALRKVFQPG FSDRALRAQE PMIRGHVDKL
VRNIYELINH DKDIPLNFVR MFNCITFDII GELAFGESMG LLDDGKMYGW VESIDGALFL
GPYLSLFPWL MKLAMLILPG RLLESQAENI RYASNAVDKR LAKGKVTEKP DFWSLVLNSK
DSEVLDHEDM KANANLFMAA GSETTATSLS GLMYNLLSHP DKLEKLLKEI RSSFSSEADH
TIENIQKLKY LAACFDESMR LYPATPLSIP RLVVNGGGEV NGQFVPDQVV KTPPINPKTA
LTSLKTRVAI STFAAYHSPH NFKDPEDFVP ERWLPSDPLY AKYADDRRDV FQPFSYGPRN
CIGKK
//
