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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//