ID A0A178ATW7_9PLEO Unreviewed; 513 AA.
AC A0A178ATW7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:OAL00068.1};
GN ORFNames=IQ06DRAFT_276589 {ECO:0000313|EMBL:OAL00068.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL00068.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL00068.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL00068.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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; KV441713; OAL00068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178ATW7; -.
DR STRING; 765868.A0A178ATW7; -.
DR InParanoid; A0A178ATW7; -.
DR OrthoDB; 1761436at2759; -.
DR Proteomes; UP000077206; 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 CDD; cd11040; CYP7_CYP8-like; 1.
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; PTHR47582; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR47582:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 440
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 513 AA; 57561 MW; C8774BB67FC3BDD2 CRC64;
MALSTTTIGA IALVVAIGVY FSGLLDAKLD SREPPLVRPK VPYIGHIIGL LTDGPNYMKR
IANRCNHPIF TLPMLNGKTY VVTDPALAQA VQRASSTLDF DEIIVQATPR LVGLSDETTA
ILRDPTAREE GRTRMVHRAH NMINRPLLAQ NIANIAELQL SHFGDWVNKI ENGQEVDMYK
LITTEVVAAS MFSFYGPHNP FAVDPKLIDR FWEWDDGNVE YAMNICRKIT ARKAYYGMEA
CVQGFLEYTE KGLHREAQPF LTERRDMHFE GGITPVEHAR LEMGIAIGFN SNASVTSFWV
INNVFANAAL LQEIRDEIYN NAFEAPATIY SSRIRDSCPL INSVWRETMR HIAPMTSARV
VLEDTILSDT YLLRKGNVVQ IAGAAVHFDE NIWGPDAATF NPRRFVHNWN GNKSGVPLDS
KASAVHPAAY RCFGGGTSLC PGRHFAQMEI TSLAAVLAMG FDFEPMQGKE KVPWDPPRDE
KRFPLVVIKP TKRVEAKMVR RKGWEDVKWT LKV
//
