ID W3WRV5_PESFW Unreviewed; 513 AA.
AC W3WRV5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETS76595.1};
GN ORFNames=PFICI_11982 {ECO:0000313|EMBL:ETS76595.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS76595.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI912117; ETS76595.1; -; Genomic_DNA.
DR RefSeq; XP_007838754.1; XM_007840563.1.
DR AlphaFoldDB; W3WRV5; -.
DR STRING; 1229662.W3WRV5; -.
DR GeneID; 19276995; -.
DR KEGG; pfy:PFICI_11982; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_14_11_1; -.
DR InParanoid; W3WRV5; -.
DR OMA; YAGWHAI; -.
DR OrthoDB; 1774992at2759; -.
DR Proteomes; UP000030651; 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:InterPro.
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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305:SF226; -; 1.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|PIRSR:PIRSR602403-1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 435
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 513 AA; 57591 MW; 8F3E78943C14BB95 CRC64;
MDNKLQYAAG FIITLLLVFL GSRLLLNPLR GYPGPLVGRI TNGYAGWHAI KGDVHLIVLT
SKGKGPVVQQ APNRLVFNTL TAIQDIYLNP RVAKAPIYAY ARFRSTPSVF TALDRADHRR
RRRVVGQAIS ERSMRDFEPI MMSQIDVFLA KLLRSSQQKD VVEMTSCCKY LAMDVVGLLA
FGASWNTQTE EKLRILPRAF SALNPRVYLF MNWPKTHKID PGVQWLVRER IEKFRKILAG
FIADRMALPR DAKHDLFSFV ASDERIDQAQ NEGIRKSEIW GEAGGTTTGT AMCTVFYYLS
RNPSAYAELA SEVRTTFSSG RDIRHGPELA GCKYLRAVID ESLRISPPTP GVMWREKDPL
SPEPLIVDGH VIPPGTFVGV GTYSLMHNPE YFPEPFAFRP ERWLEGGNDE TPEGKDARSA
MRRAFIPFIL GDRACAGKAV AYLEISLTVA KTMWYFDFQR APGLTGELGS GRKGAGGGRD
RPDEYQLYDY FMADHEGPNL IFSPRDKHCE GLV
//