ID B2AD48_PODAN Unreviewed; 741 AA.
AC B2AD48;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Hydroxylase {ECO:0000313|EMBL:CDP27718.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 4, supercontig 1 {ECO:0000313|EMBL:CAP61363.1};
GN ORFNames=PODANS_4_70 {ECO:0000313|EMBL:CAP61363.1};
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:CAP61363.1};
RN [1] {ECO:0000313|EMBL:CAP61363.1, 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:CAP61363.1};
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:CAP61363.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP61363.1};
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:CDP27718.1}
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 -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; CU633454; CAP61363.1; -; Genomic_DNA.
DR EMBL; FO904939; CDP27718.1; -; Genomic_DNA.
DR RefSeq; XP_001903588.1; XM_001903553.1.
DR AlphaFoldDB; B2AD48; -.
DR GeneID; 6187842; -.
DR KEGG; pan:PODANSg603; -.
DR VEuPathDB; FungiDB:PODANS_4_70; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_2_1; -.
DR OrthoDB; 2712941at2759; -.
DR Proteomes; UP000001197; Chromosome 4.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF16; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 86..454
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 479..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 81259 MW; B69E9B4B63897F2E CRC64;
MARALPPHTW ENGFKKPIQA SATPWVWKND EQDDDPHSFV TPPSKELLTS TAHNRVGINV
IRTWPTLFDG TNNPHGTPDW WKPSDEVDVL IVGAGPSGLE VALSLARQGV SFRIIDKAPT
PLIAGRADGV QPRFLETVAT WGLASEIAEE GPLIERTAIY LDGKKLLFNR SHQCDSRYRG
LHIITQGQIE RIFIRDLARH KSLVERERIL SKYTVEGQGE YPVRATVKNE RTGQEDIVRA
KYLVGSDGAA SSIRKSLSIP FDGVSTDIYW GIMDCVFETD YPHAWVFGSV ISSKHGGCVI
IPREDGYIRL YTQLDVSQTG PIAAARQQSD ASFAEAGGRV EIETVTPEEV LEQANRIFAP
YKLKFAAPLS WFAIWKISER VARSYSSHDN RVHLVGDAAH VHSVMGAFGL NASILDAANL
AWKLGLAAKN LADPQALLPT YSLERREHAV RVIEVSGAYL RFVTGSAMPV PNLRNFDALG
SSSKANGHQT NGHTNGHTNG HTNGVNGHSS DANGDSKQVH LHVESTSASA DSPPRTQEDA
LNFLAKFFQA HGQFLLGVDC PYATSPIAPQ TAPLLSSPAP VKLNNGVRAP NPRLCFSDNQ
TGYLYDLFEG PPKFHILVFG SSFRGEQVRN NIAKLSSVLS SKTGFWTRYG GQDRFTLTVV
VKRMPFEAGD DALLDDLTHK LGAKVVFDDR QPDEDAHTTY GANHTKGGVV VIRPDLWVGV
TAFPHEPEKI GGYFDGFLVP V
//
