Symplekin tight junction protein C terminal; This domain family is found in eukaryotes, and is ...
887-1067
8.87e-74
Symplekin tight junction protein C terminal; This domain family is found in eukaryotes, and is approximately 180 amino acids in length. There is a single completely conserved residue P that may be functionally important. Symplekn has been localized, by light and electron microscopy, to the plaque associated with the cytoplasmic face of the tight junction-containing zone (zonula occludens) of polar epithelial cells and of Sertoli cells of testis. However, both the mRNA and the protein can also be detected in a wide range of cell types that do not form tight junctions. Careful analyses have revealed that the protein occurs in all these diverse cells in the nucleoplasm, and only in those cells forming tight junctions is it recruited, partly but specifically, to the plaque structure of the zonula occludens.
:
Pssm-ID: 463523 Cd Length: 185 Bit Score: 242.52 E-value: 8.87e-74
Symplekin/PTA1 N-terminal; This is the N-terminal domain found in the symplekin protein from ...
116-326
8.98e-64
Symplekin/PTA1 N-terminal; This is the N-terminal domain found in the symplekin protein from animals and PTA1 protein from budding yeasts and is typically between 239 to 261 amino acids in length. Symplekin is a scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. PTA1 is involved in pre-tRNA processing. PTA1 is a subunit of the cleavage and polyadenylation factor (CPF), which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. This domain has the ARM or HEAT fold, with seven pairs of antiparallel alpha-helices arranged in the shape of an arc. It is important for interaction with Ssu72 and stimulates Ssu72 C-terminal domain phosphatase activity in vitro.
:
Pssm-ID: 463403 Cd Length: 218 Bit Score: 215.54 E-value: 8.98e-64
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
1-198
1.36e-04
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.
The actual alignment was detected with superfamily member cd19953:
Pssm-ID: 410996 [Multi-domain] Cd Length: 630 Bit Score: 45.98 E-value: 1.36e-04
Symplekin tight junction protein C terminal; This domain family is found in eukaryotes, and is ...
887-1067
8.87e-74
Symplekin tight junction protein C terminal; This domain family is found in eukaryotes, and is approximately 180 amino acids in length. There is a single completely conserved residue P that may be functionally important. Symplekn has been localized, by light and electron microscopy, to the plaque associated with the cytoplasmic face of the tight junction-containing zone (zonula occludens) of polar epithelial cells and of Sertoli cells of testis. However, both the mRNA and the protein can also be detected in a wide range of cell types that do not form tight junctions. Careful analyses have revealed that the protein occurs in all these diverse cells in the nucleoplasm, and only in those cells forming tight junctions is it recruited, partly but specifically, to the plaque structure of the zonula occludens.
Pssm-ID: 463523 Cd Length: 185 Bit Score: 242.52 E-value: 8.87e-74
Symplekin/PTA1 N-terminal; This is the N-terminal domain found in the symplekin protein from ...
116-326
8.98e-64
Symplekin/PTA1 N-terminal; This is the N-terminal domain found in the symplekin protein from animals and PTA1 protein from budding yeasts and is typically between 239 to 261 amino acids in length. Symplekin is a scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. PTA1 is involved in pre-tRNA processing. PTA1 is a subunit of the cleavage and polyadenylation factor (CPF), which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. This domain has the ARM or HEAT fold, with seven pairs of antiparallel alpha-helices arranged in the shape of an arc. It is important for interaction with Ssu72 and stimulates Ssu72 C-terminal domain phosphatase activity in vitro.
Pssm-ID: 463403 Cd Length: 218 Bit Score: 215.54 E-value: 8.98e-64
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
1-198
1.36e-04
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.
Pssm-ID: 410996 [Multi-domain] Cd Length: 630 Bit Score: 45.98 E-value: 1.36e-04
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
323-649
7.37e-04
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 7.37e-04
Symplekin tight junction protein C terminal; This domain family is found in eukaryotes, and is ...
887-1067
8.87e-74
Symplekin tight junction protein C terminal; This domain family is found in eukaryotes, and is approximately 180 amino acids in length. There is a single completely conserved residue P that may be functionally important. Symplekn has been localized, by light and electron microscopy, to the plaque associated with the cytoplasmic face of the tight junction-containing zone (zonula occludens) of polar epithelial cells and of Sertoli cells of testis. However, both the mRNA and the protein can also be detected in a wide range of cell types that do not form tight junctions. Careful analyses have revealed that the protein occurs in all these diverse cells in the nucleoplasm, and only in those cells forming tight junctions is it recruited, partly but specifically, to the plaque structure of the zonula occludens.
Pssm-ID: 463523 Cd Length: 185 Bit Score: 242.52 E-value: 8.87e-74
Symplekin/PTA1 N-terminal; This is the N-terminal domain found in the symplekin protein from ...
116-326
8.98e-64
Symplekin/PTA1 N-terminal; This is the N-terminal domain found in the symplekin protein from animals and PTA1 protein from budding yeasts and is typically between 239 to 261 amino acids in length. Symplekin is a scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. PTA1 is involved in pre-tRNA processing. PTA1 is a subunit of the cleavage and polyadenylation factor (CPF), which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. This domain has the ARM or HEAT fold, with seven pairs of antiparallel alpha-helices arranged in the shape of an arc. It is important for interaction with Ssu72 and stimulates Ssu72 C-terminal domain phosphatase activity in vitro.
Pssm-ID: 463403 Cd Length: 218 Bit Score: 215.54 E-value: 8.98e-64
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
1-198
1.36e-04
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.
Pssm-ID: 410996 [Multi-domain] Cd Length: 630 Bit Score: 45.98 E-value: 1.36e-04
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
323-649
7.37e-04
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 7.37e-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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(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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