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Database: UniProt
Entry: D4DDH9_TRIVH
LinkDB: D4DDH9_TRIVH
Original site: D4DDH9_TRIVH 
ID   D4DDH9_TRIVH            Unreviewed;       420 AA.
AC   D4DDH9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=MAK1-like monooxygenase, putative {ECO:0000313|EMBL:EFE40046.1};
GN   ORFNames=TRV_05190 {ECO:0000313|EMBL:EFE40046.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE40046.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:EFE40046.1}.
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DR   EMBL; ACYE01000266; EFE40046.1; -; Genomic_DNA.
DR   RefSeq; XP_003020664.1; XM_003020618.1.
DR   AlphaFoldDB; D4DDH9; -.
DR   GeneID; 9577363; -.
DR   KEGG; tve:TRV_05190; -.
DR   HOGENOM; CLU_009665_19_1_1; -.
DR   OrthoDB; 1422702at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   PANTHER; PTHR13789:SF236; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G12060)-RELATED; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:EFE40046.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          21..52
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   420 AA;  44891 MW;  C16EC4DCED594FF2 CRC64;
     MATAGVGPDG VAQPHSSGIK VIIVGLGVAG LTAAVECHRK GHTVIAFEKV KEMKPLGDGI
     GLASNAARVI SKWGGGSIQE TLESFTSVMN PSAIYDESGT LKARAPIPGY GKGEGYLLHR
     GDLALTQFDH VKSLGIDVRM GVYVTEYWET ETAAGVIVDG ERIEADCVIA SDGVHSQARG
     PITGQSPRIR ASGRAIYRAW FDASALEGAP AASWIFEPRT EGADNAHIFL AQDVVCIMTE
     VDDVLEYIKD WPAKPKIEAV MRRIPSGNLI DYPLLTGDPI ENCVSKGGRM TLIGDATHPY
     LPTSGQGACQ AIEDGAVVAI ALELAGKDNV PLALEVTKRM RAQRTAEIHK LGLSALESLV
     NPDWSESEKN SKLLSMPNPG WVLNHDCQKY AYEEYSKVVA SIKDGTEYKP LNTPAAQVSN
//
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