DMAD_DROME
ID DMAD_DROME Reviewed; 2860 AA.
AC M9NEY8; M9NDF7; M9PDW4; M9PEE3; Q8T0I1; Q8T9G4; Q9VZX4;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=DNA N6-methyl adenine demethylase {ECO:0000305};
DE EC=1.14.11.51 {ECO:0000269|PubMed:30078725, ECO:0000305|PubMed:25936838};
DE AltName: Full=DNA 6mA demethylase {ECO:0000303|PubMed:25936838};
GN Name=Tet {ECO:0000312|FlyBase:FBgn0263392};
GN Synonyms=DMAD {ECO:0000303|PubMed:25936838};
GN ORFNames=CG2083 {ECO:0000312|FlyBase:FBgn0263392},
GN CG43444 {ECO:0000312|FlyBase:FBgn0263392},
GN CG9973 {ECO:0000312|FlyBase:FBgn0263392};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2109-2860.
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 598-CYS--CYS-601 AND 1886-HIS--ASP-1888.
RX PubMed=25936838; DOI=10.1016/j.cell.2015.04.018;
RA Zhang G., Huang H., Liu D., Cheng Y., Liu X., Zhang W., Yin R., Zhang D.,
RA Zhang P., Liu J., Li C., Liu B., Luo Y., Zhu Y., Zhang N., He S., He C.,
RA Wang H., Chen D.;
RT "N(6)-methyladenine DNA modification in Drosophila.";
RL Cell 161:893-906(2015).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WDS, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 1886-HIS--LEU-1889.
RX PubMed=30078725; DOI=10.1016/j.molcel.2018.07.005;
RA Yao B., Li Y., Wang Z., Chen L., Poidevin M., Zhang C., Lin L., Wang F.,
RA Bao H., Jiao B., Lim J., Cheng Y., Huang L., Phillips B.L., Xu T., Duan R.,
RA Moberg K.H., Wu H., Jin P.;
RT "Active N6-Methyladenine Demethylation by DMAD Regulates Gene Expression by
RT Coordinating with Polycomb Protein in Neurons.";
RL Mol. Cell 71:848-857.e6(2018).
CC -!- FUNCTION: Dioxygenase that specifically demethylates DNA methylated on
CC the 6th position of adenine (N(6)-methyladenosine) DNA
CC (PubMed:25936838, PubMed:30078725). N(6)-methyladenosine (m6A) DNA is
CC present at a relatively high level at the very earliest embryonic
CC stages but at low levels at the late embryonic stages and may act as a
CC regulator of gene expression (PubMed:25936838). Promotes
CC differentiation of early germ cells in ovary (PubMed:25936838).
CC Contributes to neuronal morphology, development, and function in the
CC brain (PubMed:30078725). By interacting with histone modifier wds,
CC binds to a specific set of genes, modulates intragenic (N(6)-
CC methyladenosine) DNA levels and thereby maintains transcriptional
CC activation (PubMed:30078725). {ECO:0000269|PubMed:25936838,
CC ECO:0000269|PubMed:30078725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(6)-methyl-2'-deoxyadenosine in DNA + O2
CC = a 2'-deoxyadenosine in DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:49524, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:90616; EC=1.14.11.51;
CC Evidence={ECO:0000269|PubMed:30078725, ECO:0000305|PubMed:25936838};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q6N021};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q6N021};
CC Note=Binds 3 zinc ions per subunit. The zinc ions have a structural
CC role. {ECO:0000250|UniProtKB:Q6N021};
CC -!- SUBUNIT: Interacts (via C-terminus) with wds (via WD repeats).
CC {ECO:0000269|PubMed:30078725}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30078725}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A;
CC IsoId=M9NEY8-1; Sequence=Displayed;
CC Name=C; Synonyms=D;
CC IsoId=M9NEY8-2; Sequence=VSP_057821;
CC Name=E;
CC IsoId=M9NEY8-3; Sequence=VSP_057823;
CC Name=B;
CC IsoId=M9NEY8-4; Sequence=VSP_057822, VSP_057824;
CC Name=F;
CC IsoId=M9NEY8-5; Sequence=VSP_057822, VSP_057823, VSP_057824;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:30078725}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed during early embryonic stages but
CC is highly expressed during the later embryonic stages.
CC {ECO:0000269|PubMed:25936838}.
CC -!- DISRUPTION PHENOTYPE: Lethality at the pupa stage. A small population
CC of mutant animals are however able to pass through the pupa stage but
CC die within 3 days post-eclosion. Strong developmental defects and
CC significantly increases the abundance of N(6)-methyladenosine (m6A)
CC modification in DNA. RNAi-mediated knockdown results in mushroom bodies
CC abnormalities, including beta-lobes which erroneously cross the
CC midline, missing or misdirected alpha- and beta-lobes, as well as
CC truncated or overbranched lobes (PubMed:30078725). RNAi-mediated
CC knockdown in neurons results in mushroom body abnormalities in adult
CC flies (PubMed:30078725). Simultaneous RNAi-mediated knockdown of Tet
CC and wds results in enhanced mushroom body alpha lobe development
CC defects compared to the single Tet knockdown (PubMed:30078725).
CC {ECO:0000269|PubMed:25936838, ECO:0000269|PubMed:30078725}.
CC -!- SIMILARITY: Belongs to the TET family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39446.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL39925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF47691.4; -; Genomic_DNA.
DR EMBL; AE014296; AFH04252.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04253.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04254.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94038.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94039.1; -; Genomic_DNA.
DR EMBL; AY069301; AAL39446.1; ALT_INIT; mRNA.
DR EMBL; AY069780; AAL39925.1; ALT_INIT; mRNA.
DR RefSeq; NP_001246581.1; NM_001259652.2. [M9NEY8-1]
DR RefSeq; NP_001246582.1; NM_001259653.1. [M9NEY8-4]
DR RefSeq; NP_001246583.1; NM_001259654.2. [M9NEY8-2]
DR RefSeq; NP_001261343.1; NM_001274414.2. [M9NEY8-3]
DR RefSeq; NP_001261344.1; NM_001274415.1. [M9NEY8-5]
DR RefSeq; NP_647750.4; NM_139493.4. [M9NEY8-2]
DR SMR; M9NEY8; -.
DR IntAct; M9NEY8; 1.
DR STRING; 7227.FBpp0306013; -.
DR PaxDb; M9NEY8; -.
DR EnsemblMetazoa; FBtr0309117; FBpp0301125; FBgn0263392. [M9NEY8-1]
DR EnsemblMetazoa; FBtr0309118; FBpp0301126; FBgn0263392. [M9NEY8-4]
DR EnsemblMetazoa; FBtr0309119; FBpp0301127; FBgn0263392. [M9NEY8-2]
DR EnsemblMetazoa; FBtr0309120; FBpp0301128; FBgn0263392. [M9NEY8-2]
DR EnsemblMetazoa; FBtr0333880; FBpp0306012; FBgn0263392. [M9NEY8-3]
DR EnsemblMetazoa; FBtr0333881; FBpp0306013; FBgn0263392. [M9NEY8-5]
DR GeneID; 38347; -.
DR KEGG; dme:Dmel_CG43444; -.
DR UCSC; CG2083-RB; d. melanogaster.
DR CTD; 38347; -.
DR FlyBase; FBgn0263392; Tet.
DR VEuPathDB; VectorBase:FBgn0263392; -.
DR eggNOG; ENOG502QURD; Eukaryota.
DR OMA; QTGSYID; -.
DR BioGRID-ORCS; 38347; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Tet; fly.
DR GenomeRNAi; 38347; -.
DR PRO; PR:M9NEY8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0263392; Expressed in central nervous system and 50 other tissues.
DR Genevisible; M9NEY8; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IMP:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0035514; F:DNA demethylase activity; IMP:FlyBase.
DR GO; GO:0070579; F:methylcytosine dioxygenase activity; ISS:FlyBase.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006211; P:5-methylcytosine catabolic process; IEA:InterPro.
DR GO; GO:0080111; P:DNA demethylation; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
DR GO; GO:0035511; P:oxidative DNA demethylation; IDA:UniProtKB.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0009451; P:RNA modification; IMP:FlyBase.
DR InterPro; IPR024779; 2OGFeDO_noxygenase_dom.
DR InterPro; IPR040175; TET1/2/3.
DR InterPro; IPR002857; Znf_CXXC.
DR PANTHER; PTHR23358; PTHR23358; 3.
DR Pfam; PF12851; Tet_JBP; 1.
DR SMART; SM01333; Tet_JBP; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..2860
FT /note="DNA N6-methyl adenine demethylase"
FT /id="PRO_0000433611"
FT ZN_FING 591..631
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 51..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..2666
FT /note="Interaction with wds"
FT /evidence="ECO:0000269|PubMed:30078725"
FT REGION 1966..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2198..2229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2263..2334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2350..2371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2422..2444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2536..2598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2729..2860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2031..2060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2070..2115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2208..2229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2263..2290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2423..2439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2536..2567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2730..2744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2745..2761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2762..2785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2795..2817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2819..2852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 616
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 625
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 630
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 1638
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1640
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1725
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1767
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1777
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1779
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1878
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1886
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1888
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1891
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 1919
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 2642
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 2657..2659
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 2663..2665
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT BINDING 2673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q6N021"
FT VAR_SEQ 1..804
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_057821"
FT VAR_SEQ 589
FT /note="K -> KQDYGRRHHLPPPTLNHPPMTLPPPTITITPTTHNHNHQNHNHNHSN
FT DNNSSSCSLF (in isoform B and isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_057822"
FT VAR_SEQ 637
FT /note="K -> KEPKAKT (in isoform E and isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_057823"
FT VAR_SEQ 684
FT /note="Missing (in isoform B and isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_057824"
FT MUTAGEN 598..601
FT /note="Missing: In DMAD(Del-CXXC); flies are viable and
FT fertile."
FT /evidence="ECO:0000269|PubMed:25936838"
FT MUTAGEN 1886..1888
FT /note="HRD->YRA: In DMAD-CD(mut); abolishes ability to
FT demethylate m6A DNA."
FT /evidence="ECO:0000269|PubMed:25936838,
FT ECO:0000269|PubMed:30078725"
FT CONFLICT 2196
FT /note="P -> T (in Ref. 3; AAL39925)"
FT /evidence="ECO:0000305"
FT CONFLICT 2218
FT /note="A -> T (in Ref. 3; AAL39925)"
FT /evidence="ECO:0000305"
FT CONFLICT 2240..2243
FT /note="Missing (in Ref. 3; AAL39925)"
FT /evidence="ECO:0000305"
FT CONFLICT 2468
FT /note="S -> A (in Ref. 3; AAL39925)"
FT /evidence="ECO:0000305"
FT CONFLICT 2500..2502
FT /note="Missing (in Ref. 3; AAL39925)"
FT /evidence="ECO:0000305"
FT CONFLICT 2527
FT /note="L -> Q (in Ref. 3; AAL39925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2860 AA; 306700 MW; 35507410CB8B0709 CRC64;
MASSILAQSS TGATVDSSNL GATAAAATSV EATVSSLHNT HLNQLSSLSQ HYTTPYHHPH
SHSHPHHHYQ QHYPQQQHLQ QQQQQQHHAQ QQHQQQQQQQ QQQQQQHWDY YARQQQQHQQ
QQQQQQQPAA ATGNTNGNSS NNGNNGNNGN NSNPDGSNTT VPAPLGSSNN SSSNHANAAS
GGNSGQRHGD ANANAISAAS AAVGNPGNQQ PNNSAGNANS NSNSNSNSNG SYTRPWEMES
KDNGPQPPQT QPHLQLKSGF EPFSKLPSFQ SQFHGFNEQL LPDGTPMPVP IGAGVPPGSA
AAVAAATGSI PPGSVGPNSV AGPVGPTAMS SLQTVAMSPA SISVSSPGMM SVGSPLTQLS
SLQTSITPPS AGSFPAPPPP NAFAHHHALN PHHHHRGASG YPTPYAELPL YPGFTPLSVK
KEPISGGSDF EMLLKKEDFD LSNSGGAGLI HHPLQHGQPH PIPMGMHTPT SYDGNNSNNS
YPQAAGGGSG SHTPHTTTTQ PTPTTTTPVK VEKLLQSPIA RLEARKKERR KQRPNSLESS
AESEASGMDV DPSNPGQVDA VSSTANFKSP LSALGMGDSN DANASGCDKQ SKKKRKRCGE
CVGCQRKDNC GECAPCRNDK SHQICKQRRC EKLTEKKIVF GADGQPVRPD SKRGRGKGKS
SGSGNGTVNA TGIAAGNGTP TTGQSRARKN STKANKLNAA AASATSPRLS PVPAATLLPQ
QSPNTTSATG NLQQQQQQQQ QQYQQHQQLL SQQQLLSQQQ QQYQQPQQQQ QHFQQQQQQH
LQQQHAQQQH LPQQQHQITA QIQTMKDQPQ QPMAPMAFYP TWQADPSQGW QNQFIQQIPQ
NTPAITSLNS LDFQTQSYAY PSNGYVQSGL GFDPNYGRSP YAAPVQRYDF QSQQLSTAPS
AINQVGLQSV AGFAPSYAGQ VSAAPVPPSQ QQQQQQQQQQ QQHLGADLNK TMSGNDTPGY
PRVSSVPPRS LNCNGYSGDY SGSPATNSNS NNNSSSNTSN TNNSNASNNN ATTVVSGGTT
TPAPPPTVVA QPASSPMQPP NQAVPQSPTR SNMLQQQQQQ HQSPTGNGLQ PYVAPQQQQQ
QQQQQHLSSP PMQDWNWQQQ QQQQQSLGGE GYAQGERLHL NTRIKSMIMR KSDPKDPPPD
LQQQPQQVQQ QQQTGHFLSY SHHLRPEAAL SANGPSSATP THPLPNLQQQ QQQVQQVQQV
QQQQQQQQAV GGQVAAEPIG GGGDHIWKPH HANSFKKPSV VSGYPASQDA QLQLQLQQHQ
PGQHTTINHS VDPPVVPPQQ HPPVAAAQPK KSRSRSKASR AAAAAAAAAE AAAEIDRDRN
STDPGGGGLK PLSAHYPPHP HAAGGPPPGQ DYHSQYIKTE PGLLGPPQPN KMEGYERNYQ
NFIQYADFCQ NDGQGQPVQQ HHGHGQQDYA GYHHNSAYYG AGASSFQQNF QQNFVPGYQH
STYGARGKPP ANQPHQIHGH GQSLMELDRK PDTNSIIPLP TNYEKDIPAY PIPPHRYALG
HGAPPHLSHH GMLEPKIEDM GMLGHGGGYA YLGSEGKPLN NGFSCCRQGG TRPPTAEHLK
DGTCLGLGIQ PKEELIDEDE LIDTHGNGLK PIGGVGKAKG KQKPDEIPEI VVKHEKINPM
FDTTDRLEKG NKTEIPECEC FQSDKNPPEP GTYYTHLGTA SSLMDLRREF EERCNLTGRQ
LRIEKIVYTG KEGKTSQGCP VAKWVIRRAD LEEKILVVVK KRPGHRCIAA YIVVCMVAWD
GMPRLEADNA YKNLIPKLNK YGLPTTRRCA TNENRTCACQ GLDPESSGAS YSFGCSWSMY
YNGCKYARSK TVRKFRLSVK SEEAAIEDHM NLIATLLAPV FKQVCPRSYD NQTKYEHEAS
DCRLGLEPGK PFSGVTACLD FCAHSHRDLH NMQDGCTVHV ALLKPGNRDT RLPDDEQFHV
LPLYTMDGTD EFESVEGQRD KHRTGAVQML DKFPCEVRVR STPLIPCRRH GKKRKDGDEA
APPDGDQDAV GDANSQSSSS NGAQSQTQAN NQQSSPPALG TAHIKKENGN GVNANGASSK
SKGKGKSNQS NNSSASTPGS APPSTPSPRC QTPVTNNPSP AGSAFSTPPV HGSNANPQSN
GGQGTGNQPG QLMSSNSSLM NMATMIDTFT DAQLQSNQIS STVLDSPYSY DYQTASYIDS
RNYYGQWPTP HAPMGMQAQV GGLGGGGPGG TVAGVPPLTP STPTAQPQLG VPPATSIAGG
TTTGAPTGAL PATAPPTATP TQLETSNGYG PGNYQTLVSN PASNLTNPGG VTTEVQQQHQ
QAQQQSALTG GVGPGGLPVV GGAPGDLKGR LVSEENPDST TLVNHHHHHH NLTESKLTAL
TAMQPMTNLA PLTTSHHPQE GFVKPKPPPS DYTAQYTAQY PNNYQMYPPP PPPPHSAYSA
YDAYQNMNYN YGYHQAYSPY GMYPQQTPPP TPPPPSPNWN MYGHHQTGSV NSGYGSANPA
AGAGSLISSH GSVASAGVGL QKAMVPVPGP LHHQQQQVLQ QQQQQQQQQQ QQQQQQQQQQ
QQQVQQLQQE APQTILPDLS NGQTNSDTVA TPTPTGDSSS NDAGPGNPGA GNQAPASGAG
AATTAPPIAS PGSTNSTKIE PIGEVAEINE NIEAFQDPQM GGVAIALNHG SVLIECAKHE
MHATTAVRRP DRHHPTRMTL IFYQHRNLNR CRHGIDEWEE KMRVKKINTD LDNKAKEERE
RLIKKAAGED MDELDEDALM QDEPVPIKKE SSANGQQLKN GASGSKKKKS SDSKKSQANE
QSKNEKVALH APTLTTTSWT TLFPTHPCVV SGKYPEGNSS PTSSTNNAPN GGGCPAQQQQ
HLPPPPGSGL IHPPPGTPTG TAAPPPLPTP HQQLPQQQQT
