GenomeNet

Database: UniProt
Entry: A0A2H3JSE8_WOLCO
LinkDB: A0A2H3JSE8_WOLCO
Original site: A0A2H3JSE8_WOLCO 
ID   A0A2H3JSE8_WOLCO        Unreviewed;       518 AA.
AC   A0A2H3JSE8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:PCH45080.1};
GN   ORFNames=WOLCODRAFT_78067 {ECO:0000313|EMBL:PCH45080.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH45080.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH45080.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH45080.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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; KB468168; PCH45080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3JSE8; -.
DR   STRING; 742152.A0A2H3JSE8; -.
DR   OMA; ERFMDCD; -.
DR   OrthoDB; 2900138at2759; -.
DR   Proteomes; UP000218811; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd11065; CYP64-like; 1.
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; PTHR46300:SF7; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   518 AA;  58439 MW;  038E7A0B34D48660 CRC64;
     MSSFQTSGLA AAVAALLFAA LCRGLYRHLS AQRKRFPPGP RPLSFIGNSH QILSTYMQRR
     FAEWKAEYGD VVYARLFQKP VVILNSAQAA RDLMEKKNAI YSDRPRTVLY DEIMEWDSGM
     LFMKYGDRWK KHRKWAQNAY NDKAALMSYR PLQRREVHTL LSGLLDAPDQ FEGHIKRYFA
     ALVMETAYGH TIASVDDFYV RMADEAVSAT GSTGAPGASL IDIFPFLRYV PPWLPGAGFM
     RRAYKIGQLV KATNHIPYEN VKNAMNEGTA KPCLVSSLVR DATAAGLLTA EHEEDIKGAA
     GILYAGADFA TLASFILAMM IYPDVLKKAQ EEIDRVVGRS RLPDFEDRDS LPYLECLVKE
     TYRWSCPLPL GIAHRVMEED HYRGYYIPKG STIIPNVWCM TQDPAVYSEP EKFRPERFQD
     LTQGEAEQKD PNSFVFGFGR RICPGRHFAD ASIWLAIACT AALFDIRKAR SADGQEITPA
     PDFNTGFVSH PKRFPCEIKP RSAGTKKLLS EYSYLVQI
//
DBGET integrated database retrieval system