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Database: UniProt
Entry: J5K0R7_BEAB2
LinkDB: J5K0R7_BEAB2
Original site: J5K0R7_BEAB2 
ID   J5K0R7_BEAB2            Unreviewed;      1079 AA.
AC   J5K0R7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Flavin containing amine oxidoreductase {ECO:0000313|EMBL:EJP70108.1};
GN   ORFNames=BBA_00977 {ECO:0000313|EMBL:EJP70108.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP70108.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP70108.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP70108.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
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DR   EMBL; JH725151; EJP70108.1; -; Genomic_DNA.
DR   RefSeq; XP_008594296.1; XM_008596074.1.
DR   AlphaFoldDB; J5K0R7; -.
DR   STRING; 655819.J5K0R7; -.
DR   GeneID; 19883989; -.
DR   HOGENOM; CLU_004498_1_2_1; -.
DR   InParanoid; J5K0R7; -.
DR   OrthoDB; 5402444at2759; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
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   CDD; cd00084; HMG-box_SF; 1.
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; PF09011; HMG_box_2; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   SMART; SM00398; HMG; 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:UP000002762}.
FT   DOMAIN          195..289
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   DOMAIN          941..1017
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        941..1017
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          117..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1079 AA;  118851 MW;  D041FF034353CA02 CRC64;
     METDPHSENR AGPENGHVLQ ACETRPMDSL SVLSNVATAA QARHDIPPGS TRAQDPTTYA
     QNSFYGPISI AEASAEMKGR GMVLSTVSSP PSHQLFSKIK IEKPDCEVPI PSFHNGATES
     FASDMSDLSS RQSSFSSKAT TPADNDTPRK RTSDISTPTI PQRSFSNDGD RLDFIVQPKS
     SIPRDMPSSQ YATECIVAAE NSRLNPYALH SEEYFLLRHH ISNAQVTTYL NVRNSILRLW
     LQKPWQGVSR EEAVGCANAR WFDAANVCYN WLVRRGYVNF GCLDLGRLAT KARYQKQISK
     RRTVAIVGAG ISGLSCARQL EGLFKQYANR FYDLGEDIPK VSLIEGRSRI GGRVYSRQLR
     SQPPSPMGGF DNKRCTAEMG GMIITGFDRG NPLNVLVRGQ LCLPYHALKA ETTIYDSDGK
     PVDAERDQLI ERLYNDCLDR VSEHKYKSVA ATLIQGNRDL LNEGKDSPID GSKSIAQSEE
     IAASQASESE QLQQNVGDVV PTIPVSSDKL TGRVYSEPGV PAASKASEKA VSMGWTLKQG
     IDTEKDLDLG HAVHDPDSTL GSVLDDAISQ YKSLVELNAL DHRLMNWHIA NLEYSNATNL
     HNLSLGLWDI DAGNEWEGSH TMVVGGYQSV ARGLLHCPTP LDITAKSPVK RISYQADTFA
     GPASIECEDG KVMEADSVVC TVPLGVLKHG DIEFDPPMPD WKTQAVERLG FGILNKVVLV
     YDKVFWDSDR HIFGVLKDAS DPQSTSQHAY RASRGRFFQW FNVTNTTGMP CLIALMAGDA
     GFDTETSSNK SLISEATKTL QSIFGPDVPH PLEAVVTRWG SDPFTRGSYS SAAPDMQPED
     YDSMARPVGN LFFAGEHTIG THPATVHGAY LSGLRAASEV LDRILGPIEV PTPLILPRDS
     LLLQKRKEAA KDPRQARIDA YETEAWNHVQ SKIGERPVAP GKVAGNAYLL FSKMYFDEAR
     RRCEENRKVG RTKAMPNEVR VMTSRMWKEA SEEVRRPFEE QAAEQKRAYA EAVAKHAQEV
     GKWDLEAIEI RAAYDRSNPF APELGDAAAG SGGRTPLTPK SRRARNVSYA EDNDSDMEL
//
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