Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of ...
354-608
1.94e-119
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of the centromere assembly complex in eukaryotes. CENP-C recruits the DNA methyltransferases DNMT3B, in order to establish the necessary epigenetic DNA-methylation essential for maintenance of chromatin structure and genomic stability. This middle region of CENP-C is the binding-domain for DNMT3B. Binding of CENP-C and DNMT3B to DNA occurs at both centromeric and peri-centromeric satellite repeats. CENP-C and DNMT3B regulate the histone code in these regions.
:
Pssm-ID: 464777 Cd Length: 260 Bit Score: 364.93 E-value: 1.94e-119
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a ...
110-350
1.92e-78
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a core component of the centromeric chromatin. On depletion of CENP-C proper formation of both centromeres and kinetochores is prevented. The N-terminal of CENP-C is necessary for recruitment of some but not all components of the Mis12 complex of the kinetochore.
The actual alignment was detected with superfamily member pfam15622:
Pssm-ID: 464778 Cd Length: 287 Bit Score: 257.47 E-value: 1.92e-78
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
908-942
1.97e-04
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.
The actual alignment was detected with superfamily member pfam11699:
Pssm-ID: 477354 [Multi-domain] Cd Length: 85 Bit Score: 41.15 E-value: 1.97e-04
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of ...
354-608
1.94e-119
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of the centromere assembly complex in eukaryotes. CENP-C recruits the DNA methyltransferases DNMT3B, in order to establish the necessary epigenetic DNA-methylation essential for maintenance of chromatin structure and genomic stability. This middle region of CENP-C is the binding-domain for DNMT3B. Binding of CENP-C and DNMT3B to DNA occurs at both centromeric and peri-centromeric satellite repeats. CENP-C and DNMT3B regulate the histone code in these regions.
Pssm-ID: 464777 Cd Length: 260 Bit Score: 364.93 E-value: 1.94e-119
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a ...
110-350
1.92e-78
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a core component of the centromeric chromatin. On depletion of CENP-C proper formation of both centromeres and kinetochores is prevented. The N-terminal of CENP-C is necessary for recruitment of some but not all components of the Mis12 complex of the kinetochore.
Pssm-ID: 464778 Cd Length: 287 Bit Score: 257.47 E-value: 1.92e-78
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary ...
908-942
1.97e-04
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary for centromere formation. CENP-C is the inner-kinetochore centromere (CEN) binding protein. In the budding-yeast, Mif2, the yeast homolog, binds in the CDEIII region of the centromere, and has been shown to recruit a substantial subset of all inner and outer kinetochore proteins. Mif2 adopts a cupin fold and is extremely similar both in polypeptide chain conformation and in dimer geometry to the dimerization domain of a bacterial transcription factor. The Mif2 dimer appears to be part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. This C-terminal domain is the region via which CENP-C localizes to centromeres throughout the cell cycle 2,3].
Pssm-ID: 403028 [Multi-domain] Cd Length: 85 Bit Score: 41.15 E-value: 1.97e-04
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of ...
354-608
1.94e-119
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of the centromere assembly complex in eukaryotes. CENP-C recruits the DNA methyltransferases DNMT3B, in order to establish the necessary epigenetic DNA-methylation essential for maintenance of chromatin structure and genomic stability. This middle region of CENP-C is the binding-domain for DNMT3B. Binding of CENP-C and DNMT3B to DNA occurs at both centromeric and peri-centromeric satellite repeats. CENP-C and DNMT3B regulate the histone code in these regions.
Pssm-ID: 464777 Cd Length: 260 Bit Score: 364.93 E-value: 1.94e-119
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a ...
110-350
1.92e-78
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a core component of the centromeric chromatin. On depletion of CENP-C proper formation of both centromeres and kinetochores is prevented. The N-terminal of CENP-C is necessary for recruitment of some but not all components of the Mis12 complex of the kinetochore.
Pssm-ID: 464778 Cd Length: 287 Bit Score: 257.47 E-value: 1.92e-78
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary ...
908-942
1.97e-04
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary for centromere formation. CENP-C is the inner-kinetochore centromere (CEN) binding protein. In the budding-yeast, Mif2, the yeast homolog, binds in the CDEIII region of the centromere, and has been shown to recruit a substantial subset of all inner and outer kinetochore proteins. Mif2 adopts a cupin fold and is extremely similar both in polypeptide chain conformation and in dimer geometry to the dimerization domain of a bacterial transcription factor. The Mif2 dimer appears to be part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. This C-terminal domain is the region via which CENP-C localizes to centromeres throughout the cell cycle 2,3].
Pssm-ID: 403028 [Multi-domain] Cd Length: 85 Bit Score: 41.15 E-value: 1.97e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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