ID A0A395I873_ASPHC Unreviewed; 512 AA.
AC A0A395I873;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative sporulation-specific N-formyltyrosine oxidase Dit2 {ECO:0000313|EMBL:RAL16166.1};
GN ORFNames=BO97DRAFT_421391 {ECO:0000313|EMBL:RAL16166.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL16166.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL16166.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL16166.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; KZ824270; RAL16166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395I873; -.
DR STRING; 1450537.A0A395I873; -.
DR VEuPathDB; FungiDB:BO97DRAFT_421391; -.
DR OrthoDB; 1701697at2759; -.
DR Proteomes; UP000248961; 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: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; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF223; CYTOCHROME P450-DIT2; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..512
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017459483"
FT BINDING 449
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 512 AA; 58867 MW; A7CA4A9758623B75 CRC64;
MFALLLIFFI LLGTSAILYA LTILETPAPD YPTIPIWQTL YDHARGITRA ESYNTRIRPI
IERHGAVNLW HAGRWVVLAT RPDLVAQIFR QDDIFIKGGN IKKIPHSTFA RIFGVNIIDS
HGALHTSFTE IIKPGIQRRF DLEPAKASSA QLAESLLREQ AQHPAKGVGI DHGIMEWAVR
VFADSFLDLD AERVQVYFPR VVEAMDRFKD GVATRLQTLL YNIFPSLERL HWLLPSGHYG
VRIADRLEDL IMELAELTDE DHANATRSRD NEQVIHRLRK AYRAGSITKY HYRCNLKQLF
IAGVENIDIV LNSALWELGK NVALQRRLRH EVLTKLPGNY TESDLDELPL LTATVYETLR
LYPPLINLIN RYTSEPVQFG SDTTHPLPKD TWVGWHSYGT HTDPCVWGTS AREFDPDRWG
WDTVTIHNMF RGMQVKGKFF PFATHGRRCL ASKFALTQMK LALCELLRRV EWERDEDYNL
SLVTGVLLGP RNCKLFFRER VKKELNEPSL DC
//
