ID B3NQY4_DROER Unreviewed; 1292 AA.
AC B3NQY4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV57067.2};
DE EC=2.1.1.43 {ECO:0000313|EMBL:EDV57067.2};
GN Name=Dere\GG19893 {ECO:0000313|EMBL:EDV57067.2};
GN ORFNames=Dere_GG19893 {ECO:0000313|EMBL:EDV57067.2};
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220 {ECO:0000313|EMBL:EDV57067.2};
RN [1] {ECO:0000313|EMBL:EDV57067.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV57067.2};
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).
RN [2] {ECO:0000313|EMBL:EDV57067.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV57067.2};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:EDV57067.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV57067.2};
RG FlyBase;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CH954179; EDV57067.2; -; Genomic_DNA.
DR RefSeq; XP_001976667.2; XM_001976631.2.
DR EnsemblMetazoa; FBtr0139947; FBpp0138439; FBgn0112094.
DR GeneID; 6548401; -.
DR KEGG; der:6548401; -.
DR eggNOG; KOG1141; Eukaryota.
DR HOGENOM; CLU_003279_0_0_1; -.
DR OrthoDB; 2877903at2759; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0010369; C:chromocenter; IEA:EnsemblMetazoa.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005700; C:polytene chromosome; IEA:EnsemblMetazoa.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046974; F:histone H3K9 methyltransferase activity; IEA:EnsemblMetazoa.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IEA:EnsemblMetazoa.
DR GO; GO:0031507; P:heterochromatin formation; IEA:EnsemblMetazoa.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IEA:EnsemblMetazoa.
DR CDD; cd01395; HMT_MBD; 1.
DR CDD; cd10517; SET_SETDB1; 1.
DR CDD; cd20382; Tudor_SETDB1_rpt1; 1.
DR CDD; cd21181; Tudor_SETDB1_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR047232; SETDB1/2-like_MBD.
DR InterPro; IPR041292; Tudor_4.
DR InterPro; IPR041291; TUDOR_5.
DR PANTHER; PTHR46024; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR PANTHER; PTHR46024:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF18358; Tudor_4; 1.
DR Pfam; PF18359; Tudor_5; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Methyltransferase {ECO:0000313|EMBL:EDV57067.2};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDV57067.2}.
FT DOMAIN 853..919
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 981..1053
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 1056..1267
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1276..1292
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 144949 MW; 9ADDB8775490707A CRC64;
MSGESIAMDS TESSGIAVVS GQETPASREK SYSTPVEGEN RSESTVSAKK EGQAAKDVEM
ADLTLEDPPH SEAIDTPDST RKQPPDVGNT PDEPGKRGEE SEDPKGGNKK DVSIDIASSP
VLVAVDSDSS VELIESPAKS PSSDESVKDP PISDTANGAA AVEAKEAEEL ADSSIDLITS
PTSESTPEKD EGIKKQEQQK NENEPDNSTK ETEAPGMEVE QDVEASISHA NEEDKIEKTL
KEHKPISSME IEDHHIVDKK DDVLEVELEK GTVPKAAQDE QLNDLPSDGE MFYDKDCVNC
NCKKLHKQYV LANMATLNFY QVLRKTSKQQ FLCMGCHDTA MDLYEECAGQ LLANQPLLLK
DFQQDQADFV ALDSSDEEDE EKQPEKAHFS KNKLQFIEEE LEDAITSVLN KVDFTVQLSW
SKTILQAKAD HLERQFALAD VELEKVQTTA DKMHYALYNS CPVAHKHLPP LDIEPSVGDY
VHHVPPAGEI VRPPIQLGET YYAVKNKAIA SWVSIKVIEF TESTAINGNT MKSYKIRYLN
TPYQMIKTVT AKHIAYFEPP PVRLTIGTRV IAYFDGTTLS RGKDKGVVQS AFYPGIIAEP
LKQANRYRYL IFYDDGYTQY VPHRDVRLVC QASEKVWEDV HAASRDFIQK YVEKYSVDRP
MVQCTRGQSM NTESNGTWLY ARVIDIDCSL VLMQFEGDKN HTEWIYRGSL RLGPVFRETQ
NTMNSSSAQQ MRVPRRTEPF IRYTKEMESS SKVNQQMRAF ARKSSASGQN VALAAAASSS
ATSGGGRTNV GGASTSNSAS AVRHLNNSTI YVDDENRPKG HVVYFTAKRN LPPKMYKCHE
CSPNCLFKIV HRLDSYSPLA KPLLSGWERL VMRQKTKKSV VYKGPCGKSL RNLAEVHRYL
RATENVLNVD NFDFTPDLKC LAEYSIDPSI VKDTDISRGQ EKMAIPLVNY YDNTLPPPCT
YAKQRIPTEG VHLNLDEEFL LCCDCEDDCS DKSKCACWQL TVAGVRYCNP KKPIEEIGYQ
YKRLHEHVPT GIYECNSRCK CKKNCLNRVV QFSLEMKLQV FKTSNRGWGL RCVNDIPKGA
FICIYAGHLL TETMANEGGQ DAGDEYFADL DYIEVAEQLK EGYESEVDHS DPDAEEDNGG
PDAEDDDDFR PNYHYQRKIK RTSRSNSTQS SELDSQERAV INFNPNADLD ETVRENSVRR
LFGKDEAPYI MDAKTTGNLG RYFNHSCNPN LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT
ELTWNYNYEV GVVPGKVLYC QCGAPNCRIR LL
//
