ID A0A1A5ZWP1_9TREE Unreviewed; 503 AA.
AC A0A1A5ZWP1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=I303_06981 {ECO:0000313|EMBL:OBR82222.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR82222.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR82222.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR82222.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI894035; OBR82222.1; -; Genomic_DNA.
DR RefSeq; XP_018260064.1; XM_018410255.1.
DR AlphaFoldDB; A0A1A5ZWP1; -.
DR STRING; 1296121.A0A1A5ZWP1; -.
DR GeneID; 28970680; -.
DR VEuPathDB; FungiDB:I303_06981; -.
DR OrthoDB; 1449909at2759; -.
DR Proteomes; UP000078595; 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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000078595}.
SQ SEQUENCE 503 AA; 55837 MW; 6BE6403E7E67C80F CRC64;
MHIAIVGAGY SGLATASTLL SFGHSVVIFD SSPDVGGVWS SINHYPGLKA QNDKDTYCFS
TLPMPKDYPT HPDGQQIQAY LELYVKMQGL DKEGGLRLNT KVIKAERRPE GWVLEVHCNH
STQLLSFDYL ICATGVFSQP FVPAFAGAEE FTQAGGIISH TSNFHRLVDI KDKDVIVVGF
GKSACDTAVA ASSCAQSVTI VARNIIWKLP TYVGGVLHYS YLLLTRCGEA LFPYIRPWKS
QKFLNYGYGK PIRDVILALV GYIISIQLKL VQFNLVPNKP FETLARSSVS LATPGIVKAF
STGKIKVERG VTITSLSPGK AILSNGKELS ADVVICGTGW THHAPDFLPK EYEKQLLDEN
KDWILYRHVF PTDIPGLAFM GYNSSVFCPL TAEMTAIWLA SHLENDIRLI KPLPPVEERR
HVAETEAAWH RKRTEGHHAN GTSIVPFSLS NIDEMLADLK VKVGWSSYIR EWLLPVDPAA
YRNILPEVLR RRDNLRAELK KTV
//
