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Database: UniProt
Entry: K5WM45_PHACS
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ID   K5WM45_PHACS            Unreviewed;       606 AA.
AC   K5WM45;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHACADRAFT_132762 {ECO:0000313|EMBL:EKM60259.1};
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:EKM60259.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM60259.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM60259.1,
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; JH930468; EKM60259.1; -; Genomic_DNA.
DR   RefSeq; XP_007389730.1; XM_007389668.1.
DR   AlphaFoldDB; K5WM45; -.
DR   GeneID; 18908239; -.
DR   KEGG; pco:PHACADRAFT_132762; -.
DR   HOGENOM; CLU_015676_1_0_1; -.
DR   InParanoid; K5WM45; -.
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; 3.10.450.50; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; PR00411; PNDRDTASEI.
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   606 AA;  67792 MW;  F6C4DE7C6FD1E201 CRC64;
     MATAHTDLPT TKRLGITTKD VTSADADKVA TEWLKKFEEN ILENDIDGVL SLLTDDAWWR
     DLLAMTWDLR SFQGPARIRR FLEDRLQPAQ LHNFRLTSAQ ADDLYADLAW VRVHYTCENE
     VGACSGVARL VPVRGTWQAH NVFTNLEALH GHPEASGPLR DPAPNHGKWL EQRARAREFV
     DRDPEVLVVG GGQSGLEIGA RLKLLGVPTL VCEKHKRIGD NWRHRYAALC LHDVVWYDHM
     PYIPFPASWP VYTPAQKLAD WLEYYANAME VDYWTDARVI NARREASGPN AGKWQVTVER
     GDKNRVLYVD HVVFAIGVGG GTPNMPKIPG MDEFEGQVLH STQHDKATDH AGKKVAVVGA
     CTSAHDIAAD YADNGVDVTI VQRASTYIMT NKEGMPRLMK GVYWEDGPPT EVGDLIDNSM
     PILYRKMVHK RITKDIAEAD KELLDGLHKV GFKTNLGVDG SGFLILAMLR LGGYYLDVGA
     SQMIVDGKIK LKSSGPIKRF TKDGLVFEDG SEMKADVVLF ATGYGDPRGP IRDIVGPEVG
     KQLTPVWGID DEGELRSCWK EIGVENLWLM MGNFAWCRFY SKRLALQIKA RQEGIMGERY
     SAPVKW
//
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