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
//