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Database: UniProt
Entry: D4DK51_TRIVH
LinkDB: D4DK51_TRIVH
Original site: D4DK51_TRIVH 
ID   D4DK51_TRIVH            Unreviewed;       587 AA.
AC   D4DK51;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   22-FEB-2023, entry version 35.
DE   RecName: Full=Amine oxidase domain-containing protein {ECO:0000259|Pfam:PF01593};
GN   ORFNames=TRV_07572 {ECO:0000313|EMBL:EFE37773.1};
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:EFE37773.1, 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   -!- 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:EFE37773.1}.
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DR   EMBL; ACYE01000452; EFE37773.1; -; Genomic_DNA.
DR   RefSeq; XP_003018418.1; XM_003018372.1.
DR   AlphaFoldDB; D4DK51; -.
DR   GeneID; 9584346; -.
DR   KEGG; tve:TRV_07572; -.
DR   HOGENOM; CLU_004498_8_2_1; -.
DR   OrthoDB; 3597164at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.20.1440.240; -; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10742:SF342; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..587
FT                   /note="Amine oxidase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003055940"
FT   DOMAIN          73..556
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          180..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  66991 MW;  54BAF90FC9819FBC CRC64;
     MAFPLFLTLC FCITVLAHPT YPPNNSKNGP RHGKPLLSDF DALGAWFDGI AALEGTTIPR
     QPNVTVAIVG GGISGLATGL MLDSIGFHNW EIIEASDRVG GRFRTVFVGG TQEFAEMGPM
     RLPYTITYKS DNSTHEYTDH RMTFQLAEWL NEMNGYNSTW KIEFIPWVQH HPNELIARGT
     GRHPDGRVPT RGEIAANPSL GRPPPLVTAE YNNTKEQMNR ILKDEKTLRA IQKDIWRAHK
     WAMDQGLDDY SQQSMMRHVF HASENVTDAI WTSTDYDVFW DEMVHNSNLA QDGSKDAFGE
     TEWKCINGGF NRLSDAFIPH VSNRLVLNRK ITKLEPVNDN TNHTRTRLSW YSGTGKNRTS
     DSKDYDYTIM TVPFTMTRFM DLPKFSSVLD RAMGETGLRF KSACKVSLLF KERFWEKGER
     PIFGGYSMPE SLGIGALYYP SYGLNESRPG LITHYRGGDW SDRFVSMSDE QHTQLVLDAV
     VSLHGEQARE LYTDDFVRLC WLQDEHSATS WCRPDVEQHK LYIPAYHRTE HNTIFIGEHT
     APTHAWISSS LHSAVRGSIQ LLLELGMVEE AKQLNHRWMG RWIKHHD
//
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