ID E4URW7_ARTGP Unreviewed; 522 AA.
AC E4URW7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGYG_03441 {ECO:0000313|EMBL:EFR00438.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
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; DS989824; EFR00438.1; -; Genomic_DNA.
DR RefSeq; XP_003173268.1; XM_003173220.1.
DR AlphaFoldDB; E4URW7; -.
DR STRING; 535722.E4URW7; -.
DR GeneID; 10028573; -.
DR VEuPathDB; FungiDB:MGYG_03441; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_024886_0_0_1; -.
DR InParanoid; E4URW7; -.
DR OMA; SEKWIIP; -.
DR OrthoDB; 1826198at2759; -.
DR Proteomes; UP000002669; 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:UP000002669};
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; 58534 MW; 43CC674759FC433A CRC64;
MTVISSVAYS VAHIYSQCFV MLYSLMQDIL VYVFASNAPP PSSRNKRLRR PRIAIIGSGL
TGVSAAAHCV GHGFDVKIFE ARPKDKGLGG IWSRVNSTSS LQIHSIMFRF HPSVKWKNAY
PKQQQIKDQI VELWEAYHLD DKTAFDTPVK STRKNDKGRW VINEDEDTHG TFDGIIAAVG
SCGDPKMPTL PHQANFTGKV CHSSEMDGLD AKGKRVIVVG GGASAVEALE FAVNAGAANI
DVLSRSDKWV IPRNVVVDIL LACNIFGQET LLSFIPETLL RKLFYRDLED IAPSGKGLFT
DTPMVNSDLF ELIRAGKARW LRGDILSIKE DGISFNHRAQ GVPKSGPGHE IFVKADIIVM
ATGFIRPSLS FLPQEIFEPP YDPPNWYLQI FPPEYPSICT NNSTFVNAIG TVGNYHIGIY
TRLLLMFLID PLSRPREYMM KRWIDMTRMM KRFAPTSAFD FFTYAELLYW FIFVMVFNPF
RWKWAAFVFF GLGGVLPMAV VDKEDNAREL LGADSRSSIS DN
//
