ID A0A1Y2GZG5_9FUNG Unreviewed; 456 AA.
AC A0A1Y2GZG5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ORZ27700.1};
GN ORFNames=BCR41DRAFT_299799 {ECO:0000313|EMBL:ORZ27700.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ27700.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ27700.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ27700.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, 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:ORZ27700.1}.
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DR EMBL; MCFF01000003; ORZ27700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GZG5; -.
DR STRING; 64571.A0A1Y2GZG5; -.
DR InParanoid; A0A1Y2GZG5; -.
DR OrthoDB; 4950799at2759; -.
DR Proteomes; UP000193648; 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; IPR047146; Cyt_P450_E_CYP52_fungi.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR24287:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 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}; Iron {ECO:0000256|RuleBase:RU000461};
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:UP000193648}.
SQ SEQUENCE 456 AA; 52666 MW; 1CC2BCB3ADCDD63B CRC64;
MIDVAYAYVS SRIRGNELKY VQNLSKQGYT LNTSVIGHNL TLVFEPSSVQ HILVKNFENY
PKGAAFHRAF SAFMGTGIFN ADGAAWKNQR AIARPHFQVT EYKGAAHIET QINQVFGILD
KAIEAGDILD VQDLWSRYTI DTATGFLFGA CANALDVPQS KFVSAFNYTQ KICGWKIRLC
DYQSLIYAPE FPQKIKDMDA FLMPIVDQAV AKEIKRREDG KLGDANEDRH ENLLTHFLNS
VDENGKPFDR IYLRDMLMNF LLAGRDTSTN LLSFMCYHLG KYPDVMERVR QEIFEVVGRD
RKPEHDDIKR LKFLKQVINE TLRLYPAVPF NIKTSLEDDV LPNGYFVPKG SIVVHSSYVT
HRMKEYWGED AEEFDPDRWG PERVKIIRPF MFFPFHAGPR ICLGQNFAYN QAMNTLTRLI
QRYTWRVADG FEPIPESDIT MYSRNGMQII FEKYRD
//