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Database: UniProt
Entry: B4MKV5_DROWI
LinkDB: B4MKV5_DROWI
Original site: B4MKV5_DROWI 
ID   B4MKV5_DROWI            Unreviewed;       937 AA.
AC   B4MKV5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=SWIRM domain-containing protein {ECO:0000259|PROSITE:PS50934};
GN   Name=Dwil\GK16943 {ECO:0000313|EMBL:EDW72880.1};
GN   ORFNames=Dwil_GK16943 {ECO:0000313|EMBL:EDW72880.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW72880.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW72880.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
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; CH963847; EDW72880.1; -; Genomic_DNA.
DR   RefSeq; XP_002061894.1; XM_002061858.2.
DR   AlphaFoldDB; B4MKV5; -.
DR   SMR; B4MKV5; -.
DR   STRING; 7260.B4MKV5; -.
DR   EnsemblMetazoa; FBtr0247594; FBpp0246086; FBgn0218942.
DR   GeneID; 6638853; -.
DR   KEGG; dwi:6638853; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_004498_5_1_1; -.
DR   InParanoid; B4MKV5; -.
DR   OMA; CKESHET; -.
DR   OrthoDB; 5402444at2759; -.
DR   PhylomeDB; B4MKV5; -.
DR   Proteomes; UP000007798; 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:EDW72880.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798}.
FT   DOMAIN          202..301
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          1..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          476..550
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        104..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         309..337
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         338
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         344
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         360..361
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         848
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT   BINDING         857..858
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ   SEQUENCE   937 AA;  101928 MW;  638A3365ECEE0568 CRC64;
     MKPTTQAGGV GGGGGVAGGG YSSGAAAGNG AGTSSSVAAK LPEPIDYVTL ISDDSDGEPS
     PKRTPGSSGK PKFDDDSNDA TTPSTTATSD ERRTSRRNKP KVDYTNTNKT TTGNTLNTTS
     ENTPSEKSSS TTASASSAST SQMSDRRSQS NNHQSRKSET STTNGGGGNS TTTSTSGNGG
     TGNGTTGESG RDMGTPTVLA GQEGAVFQSR LPFSKMTTNE EACFPDISGS GILGHRVFLN
     IRNSLLHMWV DNPKVQLTFD NALKNIPPPF DSEPNLVRRV HSFLERHGFI NFGIFRRLQP
     IPSKKLGKVI VIGAGISGLA VAQQLQQFGM DVIVLEARDR VGGRIATFRK NSYIADLGAM
     VVTGVYGNPM TILSKQIGMD LVPIQQTCPL YGPDGKPVPK EKDDVIEREF NRLLESASYL
     SHRLDFNYAG NCPVSLGDAL EWIISMQEKH AMQKRAMHMH EIIAAQNKII EHRKKVKAVK
     QTVATLRLEH KALLRQRAPK SAISDDVTYA RQEYNIRNTQ LKLEDTRQLL DELRQQSKQL
     ELKLYELEQN GPSDVYLSSR DRLILDWHFA NLEFANATRL NNLSLKHWDQ DDDFEFIGHH
     TTVRNGYSCV PVALTENLDI RVNSAVKEIK YGSQGVEIVA ENLKTSNSQM TYKADLVVCT
     LTLGVLKVAV AHEESQQGNT VKFDPPLPDW KQQAIRRLGF GNLNKVVLCF DRIFWDPNAN
     LFGHVGSTTA SRGELFLFWS ISSTPVLLAL VAGMAANIVE SVTDDIIIGR CMSVLKNIYG
     NNSVPQPKET VVTRWRSDPW ARGSYSYVSV GSSGSDYDLL AAPVIPNVDH PHPSKDSEGL
     PRLFFAGEHT IRNYPATVHG AYLSGLREAG RIADYYLGYP EGTPSDIGYS VVEAANSVSV
     GNVVKLRDLS PNLSDSTSSK KSEENSNSNT ADSVELQ
//
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