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Database: UniProt
Entry: A0A261BXB2_9PELO
LinkDB: A0A261BXB2_9PELO
Original site: A0A261BXB2_9PELO 
ID   A0A261BXB2_9PELO        Unreviewed;       407 AA.
AC   A0A261BXB2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=FL83_10361 {ECO:0000313|EMBL:OZG14370.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG14370.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG14370.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG14370.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZG14370.1}.
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DR   EMBL; NIPN01000068; OZG14370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261BXB2; -.
DR   STRING; 1503980.A0A261BXB2; -.
DR   Proteomes; UP000216463; 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; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 2.
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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216463}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG14370.1"
SQ   SEQUENCE   407 AA;  46315 MW;  FB53F7B34071D417 CRC64;
     MPSSKICIIG AGAAGLVTAK HAIKDGHEVE IFEQTESVGG TWVYSEKTGC HSSMYKIMKT
     NLPKEAMLFQ DEPFREDLPS FMSHEDVLEY LDDYSKHFPI QFNTTVTDVR RDGEKWKVTT
     STNSNQPVSH FYDVVFVCNG HFFEPLNPYE NSEFEGEMIH SHDYRRAEHF EGKTVVIVGA
     GPSGIDITLQ VALTAFQVTL ISKKAVHPVL PKTVRQIASH VKSVDRHGVI TDEGERVYAD
     VIIVCTGYVF KFPFLDSSLI QLKHNDLMVS PLYQHLCHVD YPDSLFFIGL PLGTITFPLF
     EVQAKYALSL VSGTGKLPSD TLKIQNFEAE RLQGLQNPAA FHILIEEQWD YMKELAEMGG
     FEEWSYMETI RKLYCYIMSE RKKNVIGYKM VNFEMNKDET DFRVVGI
//
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