ID A0A2I2GBU4_9EURO Unreviewed; 1072 AA.
AC A0A2I2GBU4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Putative flavin-containing amine oxidase {ECO:0000313|EMBL:PLB50350.1};
GN ORFNames=P170DRAFT_445678 {ECO:0000313|EMBL:PLB50350.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB50350.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB50350.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB50350.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PLB50350.1}.
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DR EMBL; MSFO01000003; PLB50350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GBU4; -.
DR STRING; 1392250.A0A2I2GBU4; -.
DR VEuPathDB; FungiDB:P170DRAFT_445678; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0010468; P:regulation of gene expression; 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; 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; PS50934; SWIRM; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT DOMAIN 157..252
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 118354 MW; E3AD7BCAAC83EAC5 CRC64;
MSPFSQGSST NAIVNGSGRL SLLSPYKPTG SELGDGVDTN TNALPHPPPN HIPAWNPQKP
TLTPGLDTGS QSTDDVSRDL DTDTVHGTPN DSATTASFLS TASHKKSTSP LATLNALSSF
SSAADPKETE SRPHSPRYRP KSSIPSRLPA GVYAQQCIAA AYASRLNPYA LHKKEQEALQ
DHLCHLHVTV YLNIRNGILR LWTRNPMVSV TKEEALGCAK DYRWMNLASF VYEWLIRNGY
INFGCVEIPT ALVSSKKGRR RDGPVIVVIG AGMAGLGCAR QLEGLFQHYH DQAASPRVVV
LEGRRRIGGR IYSHPLQSLR SSKLPPGLVP KAEMGAHIVV GFDHGNPLDQ IIRGQLALSY
HLLRDISTIY DIDGSPVDEL RDAMDERLYN DVLDRSGFYR HKSVIVPTAE GNREFIDSGR
DVSTSDGLTV RQYEEARASG TIGQLFPNKR VRRGVGHKTA DIKTGAPAAD LDRNEEHPVA
LASQTMGWKL NPGVSVNDTL NLDPIAKASR FQTLGAVMDD GIRQYQRMLQ LSPKDLRLLN
WHLANLEYAN ATNIDQLSLS GWDQDIGNEF EGEHSQVVGG YQQVPYGLYA WPTRLDVRPN
KAVSKITYDP TGLGKQKAVV QCEDGDSIVA DKVVFTCPLG VLKDRSIQFS PSLPYWKLGA
IDRLGFGVMN KVILVFEQPF WDTERDMFGL LREPQTRDSM AQEHYSANRG RFYLFWNCMK
TTGLPVLIAL MAGDAALQAE CTPDAEIIAE VTGQLRNVFK HAAVPDPLET IVTRWRSDKF
TRGSYSYVAA QALPGDYDSM AQPIGNLHFA GEATCGTHPA TVHGAYLSGL RAASEVIDSL
LGPIELPHPL VPEKGKADFF SVNTPPTSGQ KRKQPAPSLA NLEPAALPAP KSPEAALREA
YEHAMWAAIH SEIGPPVPRP ARTVGLNPFL LYQKDYWVPC RLQCDETRRK ATNDPNAKAA
RDEIRHALGL MWRQAREDVK RPYIEQAEVN QQTNAEMSSR WRQNMAEWEK KMDRVKERWC
AAHPFDLWKS AGAANAGMLM PMLIPPASVL PISMAPMDRS HKNKTLYPNP LP
//