ID B2AEQ5_PODAN Unreviewed; 491 AA.
AC B2AEQ5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Cytochrome P450 E-class, group IV {ECO:0000313|EMBL:CDP28996.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 5, supercontig 1 {ECO:0000313|EMBL:CAP61921.1};
GN ORFNames=PODANS_5_1827 {ECO:0000313|EMBL:CAP61921.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP61921.1};
RN [1] {ECO:0000313|EMBL:CAP61921.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP61921.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP61921.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP61921.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP28996.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; CU633457; CAP61921.1; -; Genomic_DNA.
DR EMBL; FO904940; CDP28996.1; -; Genomic_DNA.
DR RefSeq; XP_001904144.1; XM_001904109.1.
DR AlphaFoldDB; B2AEQ5; -.
DR STRING; 515849.B2AEQ5; -.
DR GeneID; 6188386; -.
DR KEGG; pan:PODANSg1161; -.
DR VEuPathDB; FungiDB:PODANS_5_1827; -.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_001570_14_10_1; -.
DR OrthoDB; 2419619at2759; -.
DR Proteomes; UP000001197; Chromosome 5.
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; 2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF112; L-ORNITHINE-N5-MONOOXYGENASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 2.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 282..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 56362 MW; 7174FA879044CCAB CRC64;
MREAYSSYQA PGRNAWQLGT KLSSHTIMLV HSLTSQEFLW AGGALSGVAI HLTLFIRGEW
HVHAPEILCA YGALVAVSTL AGILYEATII GQALACHLLG LTASIITYRI FFHRLTRAGF
PGPFWARFTK LGHVWYFRHS KNNLYLDELN AKYGDVVRTA EFYDLIWPEM ALFAARDRSV
HSRRRRDWQP AFSPQDIIEE KVLLHIEELD QQLELKAKSG AVVNVIDFLL WFTFDLMVIK
DWYESVDWCQ EQIQARLAKG PAPELRDLTY YIMEKEKENK VDAGPWLRGD TNRASPRRGP
PRAGAAPRAY RQAPRRAGRH MPNRHQRPGR APHLNAVIQE AMRLHPFLPI GGIRKTTDTG
VTIRDVHIPP HTTVLTPLYT ISRRESRPIP YLTDIKLTLK CHPGEDCFEQ GSSFIPDRWT
TRPEMVRNAA AHAPFSLGKY NCIGQHLAMR MMRYTLAPVI KKYSQSVTSR EICFWFWKTY
YQNLRTISLP S
//
