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Protein

Histone-lysine N-methyltransferase eggless

Gene

egg

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 in ovary. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting Su(var)205/HP1 to methylated histones. Plays a central role during oogenesis.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi948Zinc 1By similarity1
Metal bindingi948Zinc 2By similarity1
Metal bindingi950Zinc 1By similarity1
Metal bindingi954Zinc 1By similarity1
Metal bindingi954Zinc 3By similarity1
Metal bindingi960Zinc 1By similarity1
Metal bindingi962Zinc 2By similarity1
Metal bindingi1000Zinc 2By similarity1
Metal bindingi1000Zinc 3By similarity1
Metal bindingi1004Zinc 2By similarity1
Metal bindingi1006Zinc 3By similarity1
Metal bindingi1010Zinc 3By similarity1
Binding sitei1069S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei1071S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei1191S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi1197Zinc 4By similarity1
Metal bindingi1250Zinc 4By similarity1
Metal bindingi1252Zinc 4By similarity1
Metal bindingi1257Zinc 4By similarity1

GO - Molecular functioni

  • double-stranded methylated DNA binding Source: FlyBase
  • histone-lysine N-methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity (H3-K9 specific) Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • DNA hypermethylation Source: FlyBase
  • female germ-line stem cell asymmetric division Source: FlyBase
  • histone H3-K9 methylation Source: FlyBase
  • instar larval or pupal development Source: FlyBase
  • negative regulation of gene expression, epigenetic Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • negative regulation of transcription involved in meiotic cell cycle Source: UniProtKB
  • oogenesis Source: UniProtKB
  • positive regulation of methylation-dependent chromatin silencing Source: FlyBase
  • regulation of gene expression, epigenetic Source: FlyBase
  • regulation of gene silencing Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • wing disc development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Differentiation, Oogenesis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiR-DME-3214841. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase eggless (EC:2.1.1.43)
Alternative name(s):
SETDB1 homolog
Gene namesi
Name:egg
ORF Names:CG12196
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0086908. egg.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • nucleus Source: UniProtKB
  • polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Oogenesis arrests at early stages. This arrest is accompanied by reduced proliferation of somatic cells required for egg chamber formation, and by apoptosis in both germ and somatic cell populations.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002818221 – 1262Histone-lysine N-methyltransferase egglessAdd BLAST1262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei215Phosphoserine1 Publication1
Modified residuei217Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ32KD2.
PRIDEiQ32KD2.

PTM databases

iPTMnetiQ32KD2.

Expressioni

Tissue specificityi

Expressed in ovary (at protein level).1 Publication

Developmental stagei

Present most strongly at early stages of oogenesis, in germ cells in the germarium. Present in germ stem cells and dividing germline cyst cells. Weakly or not expressed in somatic cells at the tip of the germarium, including the terminal filament, inner sheath cells, or cap cells, but it is present at low levels in somatic cells in regions 2 and 3 of the germarium, including the prefollicular cells and the follicle cells of stage 1 egg chambers. Soon after egg chambers budd off the germarium, levels increase in the follicle cells. By mid-oogenesis it decreases in the nurse cells, while levels continued to increase in the follicle cells (at protein level).1 Publication

Gene expression databases

BgeeiFBgn0086908.
GenevisibleiQ32KD2. DM.

Interactioni

Protein-protein interaction databases

BioGridi63532. 12 interactors.
DIPiDIP-46503N.
IntActiQ32KD2. 3 interactors.
MINTiMINT-749161.
STRINGi7227.FBpp0111689.

Structurei

3D structure databases

ProteinModelPortaliQ32KD2.
SMRiQ32KD2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini529 – 602Tudor 1Add BLAST74
Domaini629 – 686Tudor 2Add BLAST58
Domaini818 – 884MBDPROSITE-ProRule annotationAdd BLAST67
Domaini946 – 1018Pre-SETPROSITE-ProRule annotationAdd BLAST73
Domaini1021 – 1237SETPROSITE-ProRule annotationAdd BLAST217
Domaini1246 – 1262Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1031 – 1033S-adenosyl-L-methionine bindingBy similarity3
Regioni1194 – 1195S-adenosyl-L-methionine bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili353 – 420Sequence analysisAdd BLAST68

Domaini

In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation
Contains 2 Tudor domains.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1141. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
InParanoidiQ32KD2.
KOiK11421.
OMAiIAFFDGT.
OrthoDBiEOG091G014F.
PhylomeDBiQ32KD2.

Family and domain databases

Gene3Di3.30.890.10. 1 hit.
InterProiIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00391. MBD. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q32KD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGQPTAVDC LESSGSTVED VQETPASREK SYGLPVRKGE NSLESPAEQA
60 70 80 90 100
AKDVEIEELT HSEAIAATGS TRKQCPYGGK APDEPGKLAD ESEDRKGENT
110 120 130 140 150
KAIASSPVLV AVDSDSSVEL IESPVKFSSA NESEKDPPKP DAVNEAAAKE
160 170 180 190 200
AEEMTDSSIS SPTSESFPEK DEKTNKENEQ EPPGMEVDQD VEESISRPAE
210 220 230 240 250
EYKIENTLKG HKRISLTEIE EHKIVDKKDD VLEVELEKGT APKAAEDEKL
260 270 280 290 300
NALLSDGDVF YDKECVNCNC TKLHKQYVLA NMATLNFYQV LRKSSKQQFL
310 320 330 340 350
CMGCHDTAMD LYEEYAGQLM AKQPLLLKDF HQDHADFVAL DSSDEEEEEK
360 370 380 390 400
QPEKSDFSKN KLQLIEDELD DAIKNVLNKV DFTAQLSWSK TILQAKADHL
410 420 430 440 450
ERQFALADVE LEKVQTTADK MHCALYNSCP VAHKHLPTLD IEPSDYVHEV
460 470 480 490 500
PPPGEIVRPP IQLGETYYAV KNKAIASWVS IKVIEFTEST AINGNTMKSY
510 520 530 540 550
KIRYLNTPYQ MIKTVTAKHI AYFEPPPVRL TIGTRVIAYF DGTTLSRGKD
560 570 580 590 600
KGVVQSAFYP GIIAEPLKQA NRYRYLIFYD DGYTQYVPHR DVRLVCQASE
610 620 630 640 650
KVWEDVHAAS RDFIQKYVEK YSVDRPMVQC TRGQSMTTES NGTWLYARVI
660 670 680 690 700
DIDCSLVLMQ FEGDKNHTEW IYRGSLRLGP VFRETQNNMN SSSAQQLRVP
710 720 730 740 750
RRTEPFIRYT KEMESSSKVN QQMRAFARKS SASAQNNALA AASSAATPAG
760 770 780 790 800
GRTNAGGVST SNSASAVRHL NNSTIYVDDE NRPKGHVVYF TAKRNLPPKM
810 820 830 840 850
YKCHECSPNC LFKIVHRLDS YSPLAKPLLS GWERLVMRQK TKKSVVYKGP
860 870 880 890 900
CGKSLRSLAE VHRYLRATEN VLNVDNFDFT PDLKCLAEYS IDPSIVKDTD
910 920 930 940 950
ISKGQEKMAI PLVNYYDNTL PPPCTYAKQR IPTEGVHLNL DEEFLLCCDC
960 970 980 990 1000
EDDCSDKSKC ACWQLTVAGV RYCNPKKPIE EIGYQYKRLH EHVPTGIYEC
1010 1020 1030 1040 1050
NSRCKCKKNC LNRVVQFSLE MKLQVFKTSN RGWGLRCVND IPKGAFICIY
1060 1070 1080 1090 1100
AGHLLTETMA NEGGQDAGDE YFADLDYIEV AEQLKEGYES EVDHSDPDAE
1110 1120 1130 1140 1150
EDNGGPDAED DDDFRPNYHY QRKIKRSSRS GSTQNSSTQS SELDSQERAV
1160 1170 1180 1190 1200
INFNPNADLD ETVRENSVRR LFGKDEAPYI MDAKTTGNLG RYFNHSCSPN
1210 1220 1230 1240 1250
LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT ELTWNYNYEV GVVPGKVLYC
1260
QCGAPNCRLR LL
Length:1,262
Mass (Da):141,946
Last modified:December 6, 2005 - v1
Checksum:iA89DFF1CC6FCED1C
GO

Sequence cautioni

The sequence AAK93223 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAN71064 differs from that shown. Reason: Erroneous initiation.Curated
The sequence ABC86335 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF47268.3.
BT023947 mRNA. Translation: ABB36451.1.
BT024273 mRNA. Translation: ABC86335.1. Different initiation.
AY051799 mRNA. Translation: AAK93223.1. Different initiation.
BT001309 mRNA. Translation: AAN71064.2. Different initiation.
RefSeqiNP_611966.3. NM_138122.5.
UniGeneiDm.14397.

Genome annotation databases

EnsemblMetazoaiFBtr0112777; FBpp0111689; FBgn0086908.
GeneIDi37962.
KEGGidme:Dmel_CG12196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF47268.3.
BT023947 mRNA. Translation: ABB36451.1.
BT024273 mRNA. Translation: ABC86335.1. Different initiation.
AY051799 mRNA. Translation: AAK93223.1. Different initiation.
BT001309 mRNA. Translation: AAN71064.2. Different initiation.
RefSeqiNP_611966.3. NM_138122.5.
UniGeneiDm.14397.

3D structure databases

ProteinModelPortaliQ32KD2.
SMRiQ32KD2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63532. 12 interactors.
DIPiDIP-46503N.
IntActiQ32KD2. 3 interactors.
MINTiMINT-749161.
STRINGi7227.FBpp0111689.

PTM databases

iPTMnetiQ32KD2.

Proteomic databases

PaxDbiQ32KD2.
PRIDEiQ32KD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0112777; FBpp0111689; FBgn0086908.
GeneIDi37962.
KEGGidme:Dmel_CG12196.

Organism-specific databases

CTDi37962.
FlyBaseiFBgn0086908. egg.

Phylogenomic databases

eggNOGiKOG1141. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
InParanoidiQ32KD2.
KOiK11421.
OMAiIAFFDGT.
OrthoDBiEOG091G014F.
PhylomeDBiQ32KD2.

Enzyme and pathway databases

ReactomeiR-DME-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

GenomeRNAii37962.
PROiQ32KD2.

Gene expression databases

BgeeiFBgn0086908.
GenevisibleiQ32KD2. DM.

Family and domain databases

Gene3Di3.30.890.10. 1 hit.
InterProiIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00391. MBD. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSETB1_DROME
AccessioniPrimary (citable) accession number: Q32KD2
Secondary accession number(s): Q29QW7
, Q8IHC9, Q8MMD1, Q960X1, Q9W110
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.