ID A0A0A1TSN6_9HYPO Unreviewed; 579 AA.
AC A0A0A1TSN6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=VHEMI10680 {ECO:0000313|EMBL:CEJ95183.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ95183.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ95183.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CDHN01000009; CEJ95183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1TSN6; -.
DR STRING; 1531966.A0A0A1TSN6; -.
DR HOGENOM; CLU_025001_1_0_1; -.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000039046; 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 Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
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; PR00465; EP450IV.
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|ARBA:ARBA00022617, 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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..579
FT /note="Cytochrome P450"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001990503"
FT BINDING 524
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 579 AA; 65290 MW; 1ADD595B36087E78 CRC64;
MSVEIILLVA ASALVVGHLV YRNALPKPLP GIPHKKVSAE RLMGDIPDML ADVSRRKNIN
LWWRDHSASF NSPICQVFLG GPFSKPTVLL ADYHEARDIE TRRTHEFDRS SRTRDVFGPL
APSFQFVLPS GSEWKAHRAL VQDVVSRQFL EAVVAPTLYQ SVTRLISLWD KKIALSGGRP
FTAIDDMFNV TFDAVLSFTF GSEFPHSAME PQVKLMDEYR AIDRDNCIAT EQPIDFPVAR
LHEELEAMQT LVGFAEGAIN AGSQNLYWFF QTRSAKFSAA KKSKDTCIRA AVRRASQKRL
EHLKSEVASD RSWIHSSVDY LIDRECKLAE KEGRKVDVFS SRIADELYGM VVAGHDSTSS
TMCWAVKYLA DNQAVQQRLR DDMRYGYRKA LLEGRAPTVT EILSTNMPYT DAFMEEVLRH
STIVPFGARQ ATQDTIILGR KIPKGTVVLY LKNGPGILSD GYTFDTSIES ETSRLDRSRI
PGSADIPLEI FSPDRWIKRD AGGNITYNPN AAPVHAFGFG PRSCFGRKLA YLEFRLLLTI
IVWNFELGQC ATELSGYDGR YKTFLMPWKC YVRPKRVTS
//