Conserved Protein Domain Family
Tudor_Agenet_AtEML-like

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cd20404: Tudor_Agenet_AtEML-like 
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins
This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Statistics
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PSSM-Id: 410475
Aligned: 45 rows
Threshold Bit Score: 49.1989
Created: 11-Dec-2018
Updated: 25-Oct-2021
Structure
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Aligned Rows:
 
putative
Feature 1:putative peptide binding site [polypeptide binding site]
Evidence:
  • Comment:based on the structures of other Tudor domain superfamily members with bound methylated/dimethylated peptides
  • Comment:In general, the Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                 #    # #                    #  # #             
Q9C7C4        137 IGRKVWTKWPEdnHFYEAIITQYNad---eGRHALVYD-IHAANETweWVDLKEI 187  thale cress
Q945S8        313 IGVVIRLSRPTs-DRCFGLVRHFDey---sRKHSVMFE-DGVTEFVdmSREDWEI 362  thale cress
PSC74476      393 LGRRIMMYRPAenKWSSGIVAAHTtdalgkPCHRVEYD-DGEVWLVvlGDQQFQW 446  Micractinium conductrix
PRW21068     1880 QNWGIKVWWQGdqMFYKGRVTSYKt-----GLHRVVYDeDGSSDKIdlLKERVQL 1929 Chlorella sorokiniana
EWM22435     3252 VGRHIDIQWSGd-EHYRGVVTHFSpr---sGKHHVRYE-DGDERDYrlQERQHIF 3301 Nannochloropsis gaditana
PXF45813       14 LGDEIQVWWAVekQYFNAVVDRVLp----nGRYHVTYE-DGEEETMrlTAERWRF 63   Gracilariopsis chorda
XP_007510208  562 VDKFFSILWPEdgGWYDGCVVSYDea---tREHFVAYE-DGSTEHVnlDKQRIKY 612  Bathycoccus prasinos
PXF41171       52 VGDRIEVYWPQdeRFYEGNVTKHNpr---tQKYSVNYP-DGDKEVLklQEEKWKY 102  Gracilariopsis chorda
PRW58738      510 RGCRIAVLWSKekQWYSGMVVDYNpsk-rrQQYSVEYD-DGDFQEEnlRAGEWRL 562  Chlorella sorokiniana
PTQ43313       10 VGTGIKVYWDGddTWYSAEVTDFDpe---tEWCKVLYE-DGEREEF--RLSEVKY 58   liverwort

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