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Database: UniProt
Entry: A0A162MYN5_9PEZI
LinkDB: A0A162MYN5_9PEZI
Original site: A0A162MYN5_9PEZI 
ID   A0A162MYN5_9PEZI        Unreviewed;       600 AA.
AC   A0A162MYN5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Cytochrome p450 {ECO:0000313|EMBL:KZL85333.1};
GN   ORFNames=CI238_07363 {ECO:0000313|EMBL:KZL85333.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL85333.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL85333.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL85333.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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, 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:KZL85333.1}.
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DR   EMBL; LFIW01000652; KZL85333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162MYN5; -.
DR   STRING; 1573173.A0A162MYN5; -.
DR   Proteomes; UP000076584; 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   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   Membrane {ECO:0000256|SAM:Phobius};
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:UP000076584};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         545
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   600 AA;  67373 MW;  A7834643D331F2F6 CRC64;
     MASVGTTQPA MPAMFELGTL DNLGATHRLF GIVAASIAIA LYALYQYLLP KPIAGIPFNA
     SALQSIFGDI PAMLKNCNGT PLGWMASQGQ RCNSPIFQLF VMPFSKPSVV VSDFREAQDI
     LMRRKEFDRS DMTIDLLGGE IPQFHINLKT GPEWKGHRRL LQDLMTPQFL NRVAAPNIYT
     SATHLVDLWK TKARIADGRP FSAEQDIYFT ALDAVLDFGF SDSYPHRALK PQLELLRALE
     DQPVQPARNL LVDPIEFAVV QPHESIQAIL AAGDTIQDIA DSGFVRLAWW WKGLQPRERK
     FVKMRAEFAK EQAALAINKL NKDTDEENES WVKSAVELVI QRERKFARKE GRDPVYWSPV
     MKDELLGFIT AGHDTTSTTL CWGVKLLADC EHAQTRLRQE LWAAHAKAHA ENRAPSHNEI
     SKTKIPYLDA VIEEILRLAH TVSVIERQCT QDTVILGHHI PEGTLVLLPN SGPSFTSPPI
     AIDEKLRSET SQLAAKERGI RLWPVDDMEA FRPERWLVLD KETGEEAYDA TAGPAIPFGL
     GTRGCFGRKL AYLEMRLLVS LIIWNFELLP CDKEISSYEH IEGITSRPKQ CYVRLGRVTA
//
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