ID A0A2V1CPV4_9HELO Unreviewed; 504 AA.
AC A0A2V1CPV4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:PVH87676.1};
GN ORFNames=DL98DRAFT_544836 {ECO:0000313|EMBL:PVH87676.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH87676.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH87676.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH87676.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KZ804112; PVH87676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1CPV4; -.
DR STRING; 1485229.A0A2V1CPV4; -.
DR Proteomes; UP000244409; 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; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24296; CYTOCHROME P450; 1.
DR PANTHER; PTHR24296:SF8; CYTOCHROME P450 704B1; 1.
DR Pfam; PF00067; p450; 1.
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};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409}.
SQ SEQUENCE 504 AA; 56794 MW; 45EFE44A8681750C CRC64;
MHASTLFALF SVLFFAAYFL FRSPTLRRNG IALKRPPNTL PLVGNGILFL QARHKLFSWF
VRCERRFGFE TFQISVPSLP PGVVINDPKN LEYVFKNEGI FAKGDFFKRR SWDLFGNGII
NADGELWKVQ RKAGLHFLNN ANLKVLTDVA LPTYLNETVK SLQEEEEGSV VDLEEMLHEL
TTQLMGRMAY NMDIHNSDPF SKAFDYASGA TGQRFQNPLW QISEIFLGER FRDSVAQVKA
FGSMIVANAI QTRKNKTTET DSALDVMSGS LINSLLDSID DQDMVADAVL NYLSAGRDTT
AQALTWTFYL LMRNPSKAEA VRREVMQVAE LDPSFKPGTS PKGSAQELNT AVFRPIALPY
VTAVFYEALR LYPPVPFELK QCEQATTLPD GTYLPKNSIL VWCTWAMNRS RLIWGKDSEE
FKPERWLSDG VLISKTAFEY PVFNGGPRTC LGKTMAVSVA VQAIATLQAK FDFQLTDEKE
RISKNSLTLP MEGGLPCRVN MRED
//
