dirigent protein 17 [Medicago truncatula]
Protein Classification
tudor domain-containing protein( domain architecture ID 15332901)
tudor domain-containing protein adopts a beta-barrel-like structure and may bind to proteins with dimethylated arginine or lysine residues, or to methylated histone tails to facilitate protein-protein interactions
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Tudor_AtPTM-like | cd20401 | Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent ... |
64-112 | 6.60e-16 | ||
Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent protein 17 (AtDIR17), and similar proteins; This family includes AtPTM and AtDIR17. AtPTM, also called DDT domain-containing protein 1, or PHD type transcription factor with transmembrane domains, is a membrane-bound transcription factor required for plastid-to-nucleus retrograde signaling. AtDIR17 imparts stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids, and thus plays a central role in plant secondary metabolism. Members of this family contain one Tudor 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. : Pssm-ID: 410472 Cd Length: 50 Bit Score: 67.20 E-value: 6.60e-16
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| Name | Accession | Description | Interval | E-value | ||
| Tudor_AtPTM-like | cd20401 | Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent ... |
64-112 | 6.60e-16 | ||
Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent protein 17 (AtDIR17), and similar proteins; This family includes AtPTM and AtDIR17. AtPTM, also called DDT domain-containing protein 1, or PHD type transcription factor with transmembrane domains, is a membrane-bound transcription factor required for plastid-to-nucleus retrograde signaling. AtDIR17 imparts stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids, and thus plays a central role in plant secondary metabolism. Members of this family contain one Tudor 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. Pssm-ID: 410472 Cd Length: 50 Bit Score: 67.20 E-value: 6.60e-16
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| DUF6763 | pfam20549 | Family of unknown function (DUF6763); This family of proteins is functionally uncharacterized. ... |
59-108 | 2.09e-04 | ||
Family of unknown function (DUF6763); This family of proteins is functionally uncharacterized. This family of proteins is found in proteobacteria. Proteins in this family are tipically between 95 and 160 amino acids in length. Pssm-ID: 466698 Cd Length: 97 Bit Score: 38.32 E-value: 2.09e-04
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| Name | Accession | Description | Interval | E-value | ||
| Tudor_AtPTM-like | cd20401 | Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent ... |
64-112 | 6.60e-16 | ||
Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent protein 17 (AtDIR17), and similar proteins; This family includes AtPTM and AtDIR17. AtPTM, also called DDT domain-containing protein 1, or PHD type transcription factor with transmembrane domains, is a membrane-bound transcription factor required for plastid-to-nucleus retrograde signaling. AtDIR17 imparts stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids, and thus plays a central role in plant secondary metabolism. Members of this family contain one Tudor 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. Pssm-ID: 410472 Cd Length: 50 Bit Score: 67.20 E-value: 6.60e-16
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| Tudor_Agenet_AtEML-like | cd20404 | Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ... |
74-105 | 5.38e-05 | ||
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. Pssm-ID: 410475 [Multi-domain] Cd Length: 51 Bit Score: 38.80 E-value: 5.38e-05
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| DUF6763 | pfam20549 | Family of unknown function (DUF6763); This family of proteins is functionally uncharacterized. ... |
59-108 | 2.09e-04 | ||
Family of unknown function (DUF6763); This family of proteins is functionally uncharacterized. This family of proteins is found in proteobacteria. Proteins in this family are tipically between 95 and 160 amino acids in length. Pssm-ID: 466698 Cd Length: 97 Bit Score: 38.32 E-value: 2.09e-04
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| Tudor_LBR | cd20381 | Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral ... |
76-104 | 4.99e-03 | ||
Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral nuclear envelope inner membrane (INM) protein or LMN2R, is a nuclear envelope protein that anchors the lamina and the heterochromatin to the inner nuclear membrane, in cellular senescence induced by excess thymidine. It is also important for cholesterol biosynthesis. LBR can interact with chromodomain proteins and DNA. It contains one Tudor 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. Pssm-ID: 410452 Cd Length: 51 Bit Score: 33.43 E-value: 4.99e-03
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| Tudor_SF | cd04508 | Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ... |
65-109 | 9.17e-03 | ||
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain. Pssm-ID: 410449 [Multi-domain] Cd Length: 47 Bit Score: 32.56 E-value: 9.17e-03
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