ID Q2UUJ8_ASPOR Unreviewed; 1134 AA.
AC Q2UUJ8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Flavin-containing amine oxidoreductase-domain containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AO090009000288 {ECO:0000313|EMBL:BAE54767.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE54767.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE54767.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; AP007150; BAE54767.1; -; Genomic_DNA.
DR RefSeq; XP_001816769.1; XM_001816717.1.
DR AlphaFoldDB; Q2UUJ8; -.
DR STRING; 510516.Q2UUJ8; -.
DR EnsemblFungi; BAE54767; BAE54767; AO090009000288.
DR GeneID; 5988699; -.
DR KEGG; aor:AO090009000288; -.
DR VEuPathDB; FungiDB:AO090009000288; -.
DR HOGENOM; CLU_004498_1_2_1; -.
DR OMA; WCAENPF; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR Pfam; PF01593; Amino_oxidase; 2.
DR Pfam; PF04433; SWIRM; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT DOMAIN 199..294
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 964..1044
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 964..1044
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 90..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 124303 MW; 17150DC851C6531B CRC64;
MAPLASNMGA AASMKTHGLN GQSYEITTHL DQYIPTNISF NGSGHVALLP SNQTLPKSSL
QLNASVMKAH ASHLDNNFNQ ASVTNLYSVP NSNSNPGLRV GRTSLEGVDS SSRSTDYLSQ
DAHATTAHGR SSDSITTTSF LSQPSQTKPT PSITNINKLS SSSLVTDTKN ADSVNGLPKY
RPRSSIPSRL PAAVYAQQCV SAAYASRLNP YALHIKEQEA LQDYLCHLHV TVYLNIRNGI
LRLWTRNPMV SVTKEEALGC AKDYRWMNLA SFAYEWLVRN GYINFGCVEI PMPFVTPKKG
RRREGPVVVV IGAGMSGLGC ARHLEGLFQH YRDASTTPRV ILLEGRRRIG GRIYSHPLRS
LQTSKLGPGL VPKAEMGAHI VVGFDRGNPL DPIIRSQLAL PYHLLRDIST IYDIDGSPVD
EIQDAMDERL YDDVLDRSGF YRHKSIVVPT AEGERELIDS GRDLSTSDGV TVRQYEEARA
SGTIGLLLPT KRVRRGVGHK TADIKAPGAS GADLARSEEQ PAALTCQLNG WRLNDGIPAN
ATLNLDPVAK ISSSQTLGAA LDEGIRQYQR MLPLSPKDMR LINWHFANLE YANATNVNRL
SLSGWDQDIG NEFEGEHSQV VGGYQQVPYG LFSLPTKLDV RTNKIVSKIL YDPSGMGKQN
TVVHCEDGES FVADKVVFTG SLGVLKHQSI QFEPPLPEWK CGAINRLGFG VMNKVILVFD
EPFWDTERDM FGLLREPTNR NSTIQEDYAT NRGRFYLFWN CLKTTGLPVL IALMAGDAAL
QAECTPDDQI IGEVTSQLRN IFKHTVVPDP LETIITRWKS DKFTRGSYSY VAAQALPGDY
DLMAKPIGNL HFAGEATCGT HPATVHGAYL SGLRAGAEVI ESILGPIALP NPLVPEKGKA
ELSTPTTAGQ KRKEPHMSVA SSTGNTPTNP ADSTSPTSAR QQAYEQAMWT SVQSEIGPPM
PRPARTGLNP FLLYQKDYWG ICRAQCDEAR RAATNDPNAK AARDEIRHEL GLMWRRASEE
EKRPYIEQTE VNRQTNAEMW SRWKQQIAEW EQKAGELKTK WYAANPFASW GIHSADTAVP
TNHLSTGAGG TTSSISSLGQ HINNSRDQTQ GGTIAATVHP QTNGVQVNGS LHTS
//
