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Database: UniProt
Entry: B3M4Q6_DROAN
LinkDB: B3M4Q6_DROAN
Original site: B3M4Q6_DROAN 
ID   B3M4Q6_DROAN            Unreviewed;       895 AA.
AC   B3M4Q6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=SWIRM domain-containing protein {ECO:0000259|PROSITE:PS50934};
GN   Name=Dana\GF25315 {ECO:0000313|EMBL:EDV39455.1};
GN   Synonyms=dana_GLEANR_9996 {ECO:0000313|EMBL:EDV39455.1};
GN   ORFNames=GF25315 {ECO:0000313|EMBL:EDV39455.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV39455.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV39455.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038051-1};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CH902618; EDV39455.1; -; Genomic_DNA.
DR   RefSeq; XP_001956649.1; XM_001956613.2.
DR   AlphaFoldDB; B3M4Q6; -.
DR   SMR; B3M4Q6; -.
DR   STRING; 7217.B3M4Q6; -.
DR   EnsemblMetazoa; FBtr0130015; FBpp0128507; FBgn0102307.
DR   GeneID; 6507938; -.
DR   KEGG; dan:6507938; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_004498_5_1_1; -.
DR   InParanoid; B3M4Q6; -.
DR   OMA; SSRGEMF; -.
DR   OrthoDB; 5402444at2759; -.
DR   PhylomeDB; B3M4Q6; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblMetazoa.
DR   GO; GO:0017053; C:transcription repressor complex; IEA:EnsemblMetazoa.
DR   GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0033696; P:heterochromatin boundary formation; IEA:EnsemblMetazoa.
DR   GO; GO:0007474; P:imaginal disc-derived wing vein specification; IEA:EnsemblMetazoa.
DR   GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IEA:EnsemblMetazoa.
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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|PIRSR:PIRSR038051-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR038051-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EDV39455.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801}.
FT   DOMAIN          166..265
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          1..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          433..460
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        39..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         273..301
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         308
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         324..325
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         806
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         815..816
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ   SEQUENCE   895 AA;  98582 MW;  3CF907189214AC34 CRC64;
     MKPTQTGGSG TKMSEPIEYV TLISDDSDGE PSPKRNAPPP GHTSTAASST AAQKQKPVPD
     DDSNDAPAGS TTAGDERRTS RRNKPKVDYS NRQGGSVENA NTEKSNTATV SGKDQVDRRS
     QNQTQARKSE AISTSVSGQA ATNPRPSQNG DSKERDVGTP TVLSGQEGAV FQSRLPFSKM
     TPNEEACFPD ISRSGILGHR VFLNIRNSLL HMWVDNPKVQ LSYENAMKAL PPPFDSEPSL
     VRRVHSFLER HGFINFGIFK RQRPIPTKKL GKVIVIGAGI SGLAVAQQLQ QFGMDVIVLE
     ARDRVGGRIA TFRKNSYIAD LGAMVVTGVY GNPMTILSKQ IGMDLVPIQQ TCPLYGPDGK
     PVAKEKDDVI EREFNRLLES ASYLSHRLDF NYAGNCPVSL GDALEWIISM QEMQVMNKRA
     VHMQEIIAAQ TKIIEHRQRL KSVKQNIANL KTEHQALLKQ PKPKGTANAA TYARQEFNKR
     NTQIKLEDTM KLYGELHEED KRLEAKLREL EQNRPSDVYL SSRDRLLLDW HFANLEFANA
     TRLNNLSLKH WDQDDDFEFI GHHTTVRNGY SCVPVALTEN LDIRVNSAVK EIKYGTNGVE
     VVAENLKTSN SLMSYKADLV VCTLTLGVLK LAVAHEESQQ SNTVKFDPPL PDWKQQAIRR
     LGFGNLNKVV LCFDRIFWDP NANLFGHVGS TTSSRGEMFL FWSISSSPVL LALVAGMSAN
     IVESVTDDII IGRCMSVLKN IFGNTSVPQP KETVVTRWRS DPWARGSYSY VSVGSSGSDY
     DLLAAPVIPP TCKEPEGLPR LFFAGEHTIR NYPATVHGAY LSGLREAGRI ADYYLGYPEG
     TPPDIGYSVA EAANSVSVGN VVKLRDLSPN LSDSPSSKKS EENSSSNTAD SAELQ
//
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