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Database: UniProt
Entry: A0A484BU58_DRONA
LinkDB: A0A484BU58_DRONA
Original site: A0A484BU58_DRONA 
ID   A0A484BU58_DRONA        Unreviewed;       897 AA.
AC   A0A484BU58;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=SWIRM domain-containing protein {ECO:0000259|PROSITE:PS50934};
GN   ORFNames=AWZ03_002378 {ECO:0000313|EMBL:TDG51291.1};
OS   Drosophila navojoa (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG51291.1, ECO:0000313|Proteomes:UP000295192};
RN   [1] {ECO:0000313|EMBL:TDG51291.1, ECO:0000313|Proteomes:UP000295192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG51291.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:TDG51291.1};
RX   PubMed=30423125; DOI=.1093/jhered/esy059;
RA   Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT   "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT   the mojavensis Cluster.";
RL   J. Hered. 110:118-123(2019).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038051-1};
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
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:TDG51291.1}.
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DR   EMBL; LSRL02000010; TDG51291.1; -; Genomic_DNA.
DR   RefSeq; XP_017956032.1; XM_018100543.1.
DR   AlphaFoldDB; A0A484BU58; -.
DR   STRING; 7232.A0A484BU58; -.
DR   GeneID; 108651092; -.
DR   KEGG; dnv:108651092; -.
DR   OMA; SSRGEMF; -.
DR   OrthoDB; 5402444at2759; -.
DR   Proteomes; UP000295192; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:UniProt.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 1.10.287.80; ATP synthase, gamma subunit, helix hairpin domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR017366; Hist_Lys-spec_deMease.
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; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   PIRSF; PIRSF038051; Histone_Lys-demethylase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR038051-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR038051-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295192}.
FT   DOMAIN          164..263
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         271..299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         300
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         306
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         322..323
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         810
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         819..820
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ   SEQUENCE   897 AA;  98640 MW;  1A29863E9CAA10F4 CRC64;
     MKPTQSGGSG TSAAKMGEPI EYVTLISDDS DGEPSPKRNP SGSGSQAASH TKAKFDDDSN
     DTPATSDERR TSRRNKPKVD YTNKPATASA ENTASDKCSS GSSGSSSGLT DKRSQGQAEQ
     RTRKTEAGAN QSTGTGSRST LPKDTNGTNG EARDNSTPTV LSGQEGAVFQ SRLPFSKMTP
     NEEACFPDIS CSGILGHRVF LNIRNSLLHM WVDNPKTQLT FDSALKRLPP PFDSDPNLVR
     RVHSFLERHG FINFGIFKRL SPIPSKKLGK VIVIGAGISG LAVGQQLQQF GMDVIVLEAR
     DRVGGRIATF RKNSYIADLG AMVVTGVYGN PMTILSKQIG MDLVPIQQTC PLYGPDGKPV
     PKEKDDVIER EFNRLLESAS YLSHRLDFNY AGNNPVSLGD ALEWIINMQD KAVQEKRAAH
     MHEIISAQTR IIEHRKRLKA TLQKIATLRS DLQNLIKQRQ PRSAHNENSY ASQEYAIRNT
     QIKLEDAISS EAEQRIEGHK LEMKLQEIEQ NAPSQVYLSS RDRLILDWHF ANLEFANATR
     LDNLSLKHWD QDDDFEFIGH HTTVRNGYSC VPVALTENID IRLNSAVKEI KYTSKGVEIV
     AENLKTSNSL MTYKADLAVC TLTLGVLKVA VTQEEAHHAN TVKFDPPLPD WKQQAIRRLG
     FGNLNKVVLC FDRIFWDPNA NLFGHVGSTT ASRGEMFLFW SISSSPVLLA LVAGMAANIV
     ESVTDDIIIG RCMSVLKNIF GNTSVPQPKE TVVTRWRSDQ WARGSYSYVS VGSSGSDYDL
     LAAPVIPPTS HEPHFSKDTE ELPRLFFAGE HTIRNYPATV HGAYLSGLRE AGRIADYYLG
     YPEGTPPDIG YSVTEAANSV SVGNVVKLRD LSPHLSDSPV SKKSEENSNI ADSTDVQ
//
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