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Database: UniProt
Entry: F2SCX2_TRIRC
LinkDB: F2SCX2_TRIRC
Original site: F2SCX2_TRIRC 
ID   F2SCX2_TRIRC            Unreviewed;       522 AA.
AC   F2SCX2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TERG_01500 {ECO:0000313|EMBL:EGD85224.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD85224.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; GG700648; EGD85224.1; -; Genomic_DNA.
DR   RefSeq; XP_003239515.1; XM_003239467.1.
DR   AlphaFoldDB; F2SCX2; -.
DR   STRING; 559305.F2SCX2; -.
DR   GeneID; 10375073; -.
DR   VEuPathDB; FungiDB:TERG_01500; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_024886_0_0_1; -.
DR   InParanoid; F2SCX2; -.
DR   OMA; PNWYLQV; -.
DR   OrthoDB; 1826198at2759; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF62; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G14280); 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        453..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   522 AA;  58501 MW;  B0F781D4B08FCD65 CRC64;
     MTLISSVGRS LAHIYSQCFI ICYTLIQDIL VYVFATNAPP PSSRNKRLRR PRVAIIGSGL
     TGVSAAAHCV GHGFDVKIFE ARPKDKGLGG IWSRVNSTSS LQIHSIMFRF HPSVKWKDAY
     PNQQQIKDQI VELWKTYHLD DKTVFDTPVK STRKNDQGRW VINDDEDTHG TFDGIVAAVG
     SCGDPKMPTL PHQDKFTGQV YHSSELDGLD AKGKRIVVVG GGASAVEALE FAVNAGAANI
     DVLSRSDKWI IPRNVVVDVL LACNIFGQET ILSFIPETLL RKLFYRDLED IAPSGKGLFT
     DTPMVNSDLF ELIRAGKARW LRGDILSVEE DGISFNHRAQ GVPKSGPGHE IFVKADIIIM
     ATGFIRPSLS FLPQEVFEPP YDPPNWYLQI FPPAYPSICT NNSTFVNAIG TVGNYHIGIY
     TRLLLMFLID PLSRPREYLM KRWVDMTRIM KRFAPTGAFD FFTYAELLYW FVFVMVFNPF
     RWKWAAFVFF GLGRVLPMAV VDKEDDAREL LGADSRSSVS GN
//
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