ID K5V834_PHACS Unreviewed; 577 AA.
AC K5V834;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHACADRAFT_205130 {ECO:0000313|EMBL:EKM58936.1};
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:EKM58936.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM58936.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM58936.1,
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).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; JH930469; EKM58936.1; -; Genomic_DNA.
DR RefSeq; XP_007391524.1; XM_007391462.1.
DR AlphaFoldDB; K5V834; -.
DR GeneID; 18912335; -.
DR KEGG; pco:PHACADRAFT_205130; -.
DR HOGENOM; CLU_006937_6_1_1; -.
DR InParanoid; K5V834; -.
DR OrthoDB; 49786at2759; -.
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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF7; FLAVIN-BINDING MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
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:UP000008370}.
SQ SEQUENCE 577 AA; 65088 MW; EBF0FC662F2A3F24 CRC64;
MSSTNDLAKA YQGASTFKLL EEPVDRARPV RVIIIGAGLS GIALTHKIIR SLQNVDLVIY
EKNSDVGGTW LENQYPGVAC DVPALCYQFS FALSTEFSSY YPPGEETLHY LQDVATRIGV
PKYTEFNRKV VNASWSESEG KWTLEIERTD DGSHFQDSAH LVISAIGILN RWTMPDIPGI
NDFRGSLVHT ANWTLGQVNS SWADRRVAVI GSGSTAIQVV PAIQPHVKQL DNYVRGQTWT
AHVALPLLKR YSDGHTGNHV FTEEEKQLFR EDPAVYLELV RQCEDFLNAS HALTIAGSQM
QQTVRKRLTE YMQEALKANP HIAEAIIPDF PVVCRRLSPG FGYLAALQAN NVGFVKAGIA
RFTTDGIETK DGERRQYDVI VCATGYDPTF IPRFPVIGRN GTTLKDYWQE YPRTYISLCQ
DQHPNWFQMV GPNSAMALGS LVPVVEAQAD YLVACISKIQ RQRIKTMVVR KEAVDDFQRH
LDSYFPRTVF ARKCRSWYKR GDADGKVVAL WPGSSLNELR VLGQPRWEDF EYTFVDDNAS
HNRFYWLGNG STQAEEEGKR GSRAWYIPDK PQMLAKL
//
