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Database: UniProt
Entry: K5VQI0_PHACS
LinkDB: K5VQI0_PHACS
Original site: K5VQI0_PHACS 
ID   K5VQI0_PHACS            Unreviewed;       600 AA.
AC   K5VQI0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHACADRAFT_211396 {ECO:0000313|EMBL:EKM53733.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM53733.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM53733.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM53733.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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DR   EMBL; JH930474; EKM53733.1; -; Genomic_DNA.
DR   RefSeq; XP_007398413.1; XM_007398351.1.
DR   AlphaFoldDB; K5VQI0; -.
DR   GeneID; 18913094; -.
DR   KEGG; pco:PHACADRAFT_211396; -.
DR   HOGENOM; CLU_015676_1_0_1; -.
DR   InParanoid; K5VQI0; -.
DR   OrthoDB; 5488474at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   PANTHER; PTHR43539:SF78; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF54427; NTF2-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370}.
SQ   SEQUENCE   600 AA;  66630 MW;  CF68E55224AE7A48 CRC64;
     MTSLTDTHSI TANWLAAFAR AISDGDAQRV AATFLPEGWL RDVLTFVWDT RSLRGREAIQ
     RYLTESNHLS QAQIFNIALE TDPFYTPRES FAPTGDRVGV ETGFKYETRY AICRGYAHLR
     QVEDGTWQAI TVGMIALDLK AHPEPMNVAL DWEASGRTWD VLEAERKAKI ETDPHVLIIG
     AGQCGLSTAA RFRQMDIPTL VIEKNARIGD NWKKRYKSLA LHTPDFYSPM LYQPFPSDWP
     EYAPRDKLAS WFESYAVNQH LTIWTKSTLA AQPQYDESEG VWHVSIDRDG KNVTLRPKHI
     VLATGVLGAP RVPDLPDQTS FAGTVLHAAQ FVEPAPFAGK RVIVVGAGNS SIDICQDLAT
     GGAASVTMVQ RSQTCVVSRS SVKGDMRHNW LPGEPVAVGD FKFSAQPLGF FKEMAQSMPE
     VLWAREKELH DKLRKGGLNL YLGPEGEGQF LMVFERGGGY WMDKGGADLI ASGQIKIKQG
     SSPKSFATDG LIFSDGSKLP ADVVIFATGY ELLRDVQKHT FGEGVIDRTS ETWGLDEESE
     INGCFRPSGH PALWYAIGDF FNCRFMSKQL AILIKAAELG LYNPEQDQRK VTVDAPRAKM
//
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