MOF_DROME
ID MOF_DROME Reviewed; 827 AA.
AC O02193; A8B845; A8B850; A8B854; A8B859; A8B879; A8B889; A8B895; A8B8A1;
AC A8ILB7; A8ILC1; A8ILC8; A8ILD1; A8ILD6; A8ILE1; A8ILE5; Q9W463;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Males-absent on the first protein;
DE EC=2.3.1.48 {ECO:0000269|PubMed:11258702, ECO:0000305|PubMed:16543150};
DE AltName: Full=Histone acetyltransferase MOF;
GN Name=mof; ORFNames=CG3025;
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 [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF GLY-691.
RX PubMed=9155031; DOI=10.1093/emboj/16.8.2054;
RA Hilfiker A., Hilfiker-Kleiner D., Pannuti A., Lucchesi J.C.;
RT "mof, a putative acetyl transferase gene related to the Tip60 and MOZ human
RT genes and to the SAS genes of yeast, is required for dosage compensation in
RT Drosophila.";
RL EMBO J. 16:2054-2060(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-5; SER-48; GLU-119;
RP ASP-156; CYS-202; VAL-254 AND TYR-384.
RC STRAIN=Africa-1, Africa-3, Africa-4, Africa-5, Africa-7, Amherst, Congo 13,
RC Congo 159, Congo 194, Congo 216, and Congo 8;
RX PubMed=17878295; DOI=10.1073/pnas.0707445104;
RA Rodriguez M.A., Vermaak D., Bayes J.J., Malik H.S.;
RT "Species-specific positive selection of the male-specific lethal complex
RT that participates in dosage compensation in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15412-15417(2007).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-827, AND VARIANTS ASP-156 AND
RP TYR-384.
RC STRAIN=Mof.591A.s, Mof.639A.s, Mof.732A.s, Mof.774A.s, Mof.799A.s,
RC Mof.820A.s, Mof.852A.s, and Mof.859A.s;
RX PubMed=18039888; DOI=10.1534/genetics.107.079459;
RA Levine M.T., Holloway A.K., Arshad U., Begun D.J.;
RT "Pervasive and largely lineage-specific adaptive protein evolution in the
RT dosage compensation complex of Drosophila melanogaster.";
RL Genetics 177:1959-1962(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-577; 578-LEU--TYR-580
RP AND GLY-691.
RX PubMed=11258702; DOI=10.1093/embo-reports/kve022;
RA Akhtar A., Becker P.B.;
RT "The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate
RT recognition.";
RL EMBO Rep. 2:113-118(2001).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE MSL COMPLEX, AND IDENTIFICATION IN THE NSL
RP COMPLEX.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
RN [9]
RP FUNCTION IN CHROMATIN MODIFICATION, FUNCTION IN TRANSCRIPTION REGULATION,
RP IDENTIFICATION AS PART OF THE MSL AND NSL COMPLEXES, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20620954; DOI=10.1016/j.molcel.2010.05.021;
RA Raja S.J., Charapitsa I., Conrad T., Vaquerizas J.M., Gebhardt P., Holz H.,
RA Kadlec J., Fraterman S., Luscombe N.M., Akhtar A.;
RT "The nonspecific lethal complex is a transcriptional regulator in
RT Drosophila.";
RL Mol. Cell 38:827-841(2010).
RN [10]
RP FUNCTION, INTERACTION WITH MTOR, AND DISRUPTION PHENOTYPE.
RX PubMed=34133927; DOI=10.1016/j.celrep.2021.109236;
RA Aleman J.R., Kuhn T.M., Pascual-Garcia P., Gospocic J., Lan Y., Bonasio R.,
RA Little S.C., Capelson M.;
RT "Correct dosage of X chromosome transcription is controlled by a nuclear
RT pore component.";
RL Cell Rep. 35:109236-109236(2021).
RN [11]
RP STRUCTURE BY NMR OF 367-454.
RX PubMed=15964847; DOI=10.1074/jbc.m501347200;
RA Nielsen P.R., Nietlispach D., Buscaino A., Warner R.J., Akhtar A.,
RA Murzin A.G., Murzina N.V., Laue E.D.;
RT "Structure of the chromo barrel domain from the MOF acetyltransferase.";
RL J. Biol. Chem. 280:32326-32331(2005).
CC -!- FUNCTION: Histone acetyltransferase that plays a direct role in the
CC specific histone acetylation associated with dosage compensation as
CC part of the male-specific lethal (MSL) complex (PubMed:9155031,
CC PubMed:16543150, PubMed:34133927). Dosage compensation insures that
CC males with a single X chromosome have the same amount of most X-linked
CC gene products as females with two X chromosomes (PubMed:9155031). May
CC be directly involved in the acetylation of histone 4 at 'Lys-16' on the
CC X chromosome of males where it is recruited by the MSL complex
CC (PubMed:11258702). As part of the nonspecific lethal (NLS) complex may
CC associate with promoters of X chromosomal as well as autosomal genes
CC and positively regulate their transcription through chromatin
CC modification (PubMed:20620954). {ECO:0000269|PubMed:11258702,
CC ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:20620954,
CC ECO:0000269|PubMed:34133927, ECO:0000269|PubMed:9155031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:11258702, ECO:0000305|PubMed:16543150};
CC -!- SUBUNIT: Component of the male-specific lethal (MSL) histone
CC acetyltransferase complex at least composed of mof, msl-1, msl-2 and
CC msl-3 (PubMed:20620954, PubMed:16543150). Component of the non-specific
CC lethal (NLS) histone acetyltransferase complex at least composed of
CC mof, nls1, dgt1/NSL2, Rcd1/NSL3, Rcd5/MCRS2, MBD-R2 and wds
CC (PubMed:16543150, PubMed:20620954). In males, interacts with
CC nucleoporin Mtor (PubMed:34133927). {ECO:0000269|PubMed:16543150,
CC ECO:0000269|PubMed:20620954, ECO:0000269|PubMed:34133927}.
CC -!- INTERACTION:
CC O02193; A4V2Z1: nsl1; NbExp=4; IntAct=EBI-138539, EBI-9630827;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:20620954}. Nucleus
CC {ECO:0000269|PubMed:20620954}.
CC -!- PTM: Autoacetylation at Lys-638 is required for binding histone H4 with
CC high affinity and for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in male salivary glands,
CC decreases chromosome X gene expression (PubMed:34133927). Simultaneous
CC RNAi-mediated knockdown of mof with RNAi-mediated knockdown of Mtor in
CC male salivary glands rescues the decrease in chromosome X gene
CC expression (PubMed:34133927). {ECO:0000269|PubMed:34133927}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; U71219; AAC47507.1; -; Genomic_DNA.
DR EMBL; EF630368; ABU97211.1; -; Genomic_DNA.
DR EMBL; EF630369; ABU97212.1; -; Genomic_DNA.
DR EMBL; EF630370; ABU97213.1; -; Genomic_DNA.
DR EMBL; EF630371; ABU97214.1; -; Genomic_DNA.
DR EMBL; EF630372; ABU97215.1; -; Genomic_DNA.
DR EMBL; EF630373; ABU97216.1; -; Genomic_DNA.
DR EMBL; EF630374; ABU97217.1; -; Genomic_DNA.
DR EMBL; EF630375; ABU97218.1; -; Genomic_DNA.
DR EMBL; EF630376; ABU97219.1; -; Genomic_DNA.
DR EMBL; EF630377; ABU97220.1; -; Genomic_DNA.
DR EMBL; EF630378; ABU97221.1; -; Genomic_DNA.
DR EMBL; EF630379; ABU97222.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46095.1; -; Genomic_DNA.
DR EMBL; AY102685; AAM27514.1; -; mRNA.
DR EMBL; EU167134; ABV82526.1; -; Genomic_DNA.
DR EMBL; EU167135; ABV82527.1; -; Genomic_DNA.
DR EMBL; EU167136; ABV82528.1; -; Genomic_DNA.
DR EMBL; EU167137; ABV82529.1; -; Genomic_DNA.
DR EMBL; EU167138; ABV82530.1; -; Genomic_DNA.
DR EMBL; EU167139; ABV82531.1; -; Genomic_DNA.
DR EMBL; EU167140; ABV82532.1; -; Genomic_DNA.
DR EMBL; EU167141; ABV82533.1; -; Genomic_DNA.
DR RefSeq; NP_511051.1; NM_078496.3.
DR PDB; 2BUD; NMR; -; A=367-454.
DR PDBsum; 2BUD; -.
DR AlphaFoldDB; O02193; -.
DR SMR; O02193; -.
DR BioGRID; 58017; 30.
DR DIP; DIP-46346N; -.
DR IntAct; O02193; 3.
DR STRING; 7227.FBpp0070794; -.
DR PaxDb; O02193; -.
DR EnsemblMetazoa; FBtr0070829; FBpp0070794; FBgn0014340.
DR GeneID; 31518; -.
DR KEGG; dme:Dmel_CG3025; -.
DR CTD; 31518; -.
DR FlyBase; FBgn0014340; mof.
DR VEuPathDB; VectorBase:FBgn0014340; -.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000159512; -.
DR HOGENOM; CLU_012139_1_0_1; -.
DR InParanoid; O02193; -.
DR OMA; SNTVICV; -.
DR OrthoDB; 629545at2759; -.
DR PhylomeDB; O02193; -.
DR BRENDA; 2.3.1.48; 1994.
DR BioGRID-ORCS; 31518; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; O02193; -.
DR GenomeRNAi; 31518; -.
DR PRO; PR:O02193; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0014340; Expressed in cleaving embryo and 22 other tissues.
DR ExpressionAtlas; O02193; baseline and differential.
DR Genevisible; O02193; DM.
DR GO; GO:0072487; C:MSL complex; IDA:FlyBase.
DR GO; GO:0044545; C:NSL complex; IDA:FlyBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IDA:FlyBase.
DR GO; GO:0000805; C:X chromosome; IDA:FlyBase.
DR GO; GO:0016456; C:X chromosome located dosage compensation complex, transcription activating; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:FlyBase.
DR GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IMP:FlyBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; TAS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IMP:FlyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:FlyBase.
DR GO; GO:0006281; P:DNA repair; IMP:FlyBase.
DR GO; GO:0007549; P:dosage compensation; IMP:UniProtKB.
DR GO; GO:0009047; P:dosage compensation by hyperactivation of X chromosome; NAS:FlyBase.
DR GO; GO:0016573; P:histone acetylation; TAS:FlyBase.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; TAS:FlyBase.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000873; P:regulation of histone H4 acetylation involved in response to DNA damage stimulus; IMP:FlyBase.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:FlyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR037906; KAT8.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615:SF82; PTHR10615:SF82; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Chromatin regulator;
KW Chromosome; Metal-binding; Nucleus; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..827
FT /note="Males-absent on the first protein"
FT /id="PRO_0000051563"
FT DOMAIN 382..433
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 538..813
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 571..596
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 714
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 681..683
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 688..694
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 718
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 727
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 798
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 638
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT VARIANT 5
FT /note="E -> V (in strain: Congo 159, Congo 194 and Congo
FT 216)"
FT /evidence="ECO:0000269|PubMed:17878295"
FT VARIANT 48
FT /note="A -> S (in strain: Africa-1 and Africa-5)"
FT /evidence="ECO:0000269|PubMed:17878295"
FT VARIANT 119
FT /note="D -> E (in strain: Congo 216)"
FT /evidence="ECO:0000269|PubMed:17878295"
FT VARIANT 156
FT /note="G -> D (in strain: Congo 8, Congo 13, Congo 194 and
FT Mof.820A.s)"
FT /evidence="ECO:0000269|PubMed:17878295,
FT ECO:0000269|PubMed:18039888"
FT VARIANT 202
FT /note="G -> C (in strain: Africa-0)"
FT /evidence="ECO:0000269|PubMed:17878295"
FT VARIANT 254
FT /note="A -> V (in strain: Congo 194)"
FT /evidence="ECO:0000269|PubMed:17878295"
FT VARIANT 384
FT /note="F -> Y (in strain: Africa-0, Africa-3, Africa-4,
FT Congo 194 and Mof.591A.s)"
FT /evidence="ECO:0000269|PubMed:17878295,
FT ECO:0000269|PubMed:18039888"
FT MUTAGEN 577
FT /note="C->G: Abolishes histone acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11258702"
FT MUTAGEN 578..580
FT /note="LKY->GYG: Nearly abolishes histone acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:11258702"
FT MUTAGEN 691
FT /note="G->E: Strongly reduces histone acetyltransferase
FT activity. Males fail to metamorphose and hatch."
FT /evidence="ECO:0000269|PubMed:11258702,
FT ECO:0000269|PubMed:9155031"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2BUD"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:2BUD"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:2BUD"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:2BUD"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:2BUD"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:2BUD"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:2BUD"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:2BUD"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:2BUD"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:2BUD"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2BUD"
SQ SEQUENCE 827 AA; 92657 MW; 8B9C5E87E3B01317 CRC64;
MSEAELEQTP SAGHVQEQPI EEEHEPEQEP TDAYTIGGPP RTPVEDAAAE LSASLDVSGS
DQSAEQSLDL SGVQAEAAAE SEPPAKRQHR DISPISEDST PASSTSTSST RSSSSSRYDD
VSEAEEAPPE PEPEQPQQQQ QEEKKEDGQD QVKSPGPVEL EAQEPAQPQK QKEVVDQEIE
TEDEPSSDTV ICVADINPYG SGSNIDDFVM DPDAPPNAII TEVVTIPAPL HLKGTQQLGL
PLAAPPPPPP PPAAEQVPET PASPTDDGEE PPAVYLSPYI RSRYMQESTP GLPTRLAPRD
PRQRNMPPPA VVLPIQTVLS ANVEAISDDS SETSSSDDDE EEEEDEDDAL TMEHDNTSRE
TVITTGDPLM QKIDISENPD KIYFIRREDG TVHRGQVLQS RTTENAAAPD EYYVHYVGLN
RRLDGWVGRH RISDNADDLG GITVLPAPPL APDQPSTSRE MLAQQAAAAA AASSERQKRA
ANKDYYLSYC ENSRYDYSDR KMTRYQKRRY DEINHVQKSH AELTATQAAL EKEHESITKI
KYIDKLQFGN YEIDTWYFSP FPEEYGKART LYVCEYCLKY MRFRSSYAYH LHECDRRRPP
GREIYRKGNI SIYEVNGKEE SLYCQLLCLM AKLFLDHKVL YFDMDPFLFY ILCETDKEGS
HIVGYFSKEK KSLENYNVAC ILVLPPHQRK GFGKLLIAFS YELSRKEGVI GSPEKPLSDL
GRLSYRSYWA YTLLELMKTR CAPEQITIKE LSEMSGITHD DIIYTLQSMK MIKYWKGQNV
ICVTSKTIQD HLQLPQFKQP KLTIDTDYLV WSPQTAAAVV RAPGNSG
