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Database: UniProt
Entry: A0A1J9RW95_9PEZI
LinkDB: A0A1J9RW95_9PEZI
Original site: A0A1J9RW95_9PEZI 
ID   A0A1J9RW95_9PEZI        Unreviewed;       561 AA.
AC   A0A1J9RW95;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=High nitrogen upregulated cytochrome p450 monooxygenase 1 {ECO:0000313|EMBL:OJD31749.1};
GN   ORFNames=BKCO1_4500059 {ECO:0000313|EMBL:OJD31749.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD31749.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD31749.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD31749.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
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:OJD31749.1}.
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DR   EMBL; MNUE01000045; OJD31749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RW95; -.
DR   STRING; 236234.A0A1J9RW95; -.
DR   OrthoDB; 2419619at2759; -.
DR   Proteomes; UP000183809; 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:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11061; CYP67-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305:SF187; -; 1.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Monooxygenase {ECO:0000313|EMBL:OJD31749.1};
KW   Oxidoreductase {ECO:0000313|EMBL:OJD31749.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   561 AA;  62988 MW;  CB2273F3E19CC5D1 CRC64;
     MASNMSLENP LSPALCAAAA GVLLHLGVFI RGEWEKYVAQ LALLQVTGPL VVLGSLVAFL
     GQPLSQAAAT AALLTASFNV GLYGSISVYR LFFHPLRRFY GPTGGKLTSL WAMKETFPDL
     KFYVKLQKLH QDHGDFIRFQ PRALSINNAE AIQDIYGSTS KCTKGPFYDL DYPGRSLHMT
     RDRKFHSQRR KQWDRAFTSR ALSNYEKRLK EHFKYLDLRI SENMGKPINA TDLCEYWGFD
     VMGDLMFGRP FNQLKENKAH FALEMARKAK FIGGLTLYPY WIFMLLQRLP IVSSLRLKWL
     RWCRSQMEQR RQSKPEVLDL YSYLLEDSSA EKAGDANNSA TADLDALFDA ELAIVAGSDT
     SSATLAASLY LLAKHPHVQS KLRQEVDDAV AAAGGELSYQ TLVNRPLLGG VINEALRLYP
     PVVPGLQRLT PPEGATIAGR FVPGDTLVSV QCWSVQRDPR NFPQPEDFIP ERWSSMPELA
     LHKEALIAFS TGTYSCVGRP LAMMELKLAV AMVARRFEVA FADPAESVRL FEESPGWQDS
     FTARVPPVKV CFREREKRDL A
//
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