ID B8LXP5_TALSN Unreviewed; 1054 AA.
AC B8LXP5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Lysine-specific histone demethylase Aof2, putative {ECO:0000313|EMBL:EED24546.1};
GN ORFNames=TSTA_079030 {ECO:0000313|EMBL:EED24546.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED24546.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; EQ962652; EED24546.1; -; Genomic_DNA.
DR RefSeq; XP_002341933.1; XM_002341892.1.
DR AlphaFoldDB; B8LXP5; -.
DR STRING; 441959.B8LXP5; -.
DR GeneID; 8102517; -.
DR VEuPathDB; FungiDB:TSTA_079030; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR InParanoid; B8LXP5; -.
DR OMA; WCAENPF; -.
DR OrthoDB; 5402444at2759; -.
DR PhylomeDB; B8LXP5; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 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 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:EED24546.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transferase {ECO:0000313|EMBL:EED24546.1}.
FT DOMAIN 182..277
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 26..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 117791 MW; D18B76E6A2279C9C CRC64;
MASGQGANSS GMSAGTKSIT FKHYTFTPAP QSSLPPYKRR RITEPAQPAY PYIKGADRET
STDGVNGSYK LDCLKQPTHV GIPNNNILGN TASFSSQSAS ERSYRAEQDS DLTGHNTPNT
SVSNTSPWPQ IRSMSPAATA TNLAEKPKQV HEPEVEAPNY EEFKPRSSIP STLPGPVYAQ
QCITAAYASR LNPFALHKNE QNAFQHHLCH LHVTTYLNIR NGILRLWTRN PMISVTREEA
LGCAKDYRWM GLADFAYEWL VRNGYINFGC VEVPQPLITP KKGRRKDDGP VIVIVGAGVA
GLACARQLDG LYQQYRDKVA SLKIIVLEGR RRIGGRIYSH PLKSHQKTAL PKGLRPTAEM
GAQIIVGFDR GNPLDPIIRS QLALRYHLLR DISTIYDVDG SAVDEMQDAM DERLYNDVLD
RSGNYRHKAA IQSTAEGDRE MINHGRDIPI DDGVTVHQYE EARAAGTHHL MLPAARFRRG
IGHNASRILP PPSTAQISDL GPDEELPAAM ECQSMGWKLR DGISPRDDLQ LDNIAKTSPT
QTLGAVMDEG VRQYQHMLPL TPKDMRLLNW HYANLEYANA TNLNSLSLSG WDQDMGNEFE
GEHSQVIGGY QQLPRGLWAF PTKLDVRTNE TVVNITYDAT GKIKNRKTIV HTENGPISAD
HVVYTGSLGT LKHRTVEFSP TLPDWKNGAV DRLGFGVLNK VVLVFDEPFW DTTRDMFGLL
REAEVPGSMS QAHYTKNRGR FYLFWNCIRT SGIPVLIALM AGDAAHQAEE MPDKEIVTEV
LSELRNIFKS KTVPDPLETI VTRWKSDKFT RGTYSYVAAD ALPGDYDLMA KAVGNLHFAG
EATCATHPAT VHGAYLSGLR AAAEIMEEII GPIAIPTPLV PRRRRAIPIL HLGAPSMTKT
VNKPSPPPPT TFANSTTSAE QQKHYLYKIA LENHIRATLG APPTKPAKIA LNPFLTFQKD
YWIRAKQRCE TNKRQSTNDF EAKAARDEIR AVLGQMWREA EEEVKRPYQE QMVVNRRMND
EMAKTWEESM KEYERRSLEV GKEFTFEKWA SMNP
//
