nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
5-316
1.30e-76
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 237.17 E-value: 1.30e-76
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
5-316
1.30e-76
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 237.17 E-value: 1.30e-76
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
3-314
3.34e-17
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 79.87 E-value: 3.34e-17
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ...
2-316
7.80e-11
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium botulinum pCBH plasmid segregation protein ParM, an actin-like polymerizing motor. pCBH ParM filament structure is far more complex in comparison to the known filament structures of actin, MreB, and other ParMs. It is bipolar and stiff and like microtubules. The 15 polymerizing strands are likely to exert greater combined force relative to typical two-stranded actin-like filaments.
Pssm-ID: 466875 [Multi-domain] Cd Length: 326 Bit Score: 61.91 E-value: 7.80e-11
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and ...
69-314
4.04e-06
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and similar proteins from the ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Staphylococcus aureus pSK41 actin-like ParM protein, which is functionally homologous to R1 ParM, a known actin homologue, suggesting that it may also form filaments to drive partition. However, pSK41 ParM shows the strongest structural homology to the archaeal actin-like protein Thermoplasma acidophilum Ta0583, but not R1 ParM.
Pssm-ID: 466871 [Multi-domain] Cd Length: 298 Bit Score: 47.67 E-value: 4.04e-06
nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar ...
80-314
5.79e-05
nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium tetani actin-like protein Alp12. It is a dynamically unstable force-generating motor involved in segregating the pE88 plasmid, which encodes the lethal tetanus toxin. Alp12 filaments have a unique polymer structure that is entirely different from F-actin and display dynamic behavior like microtubules. Alp12 can be repeatedly cycled between states of polymerization and dissociation, making it a novel candidate for incorporation into fuel-propelled nanobiopolymer machines.
Pssm-ID: 466876 [Multi-domain] Cd Length: 308 Bit Score: 44.20 E-value: 5.79e-05
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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of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
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(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
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,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
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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