ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
7-327
3.12e-103
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
The actual alignment was detected with superfamily member TIGR03739:
Pssm-ID: 483947 [Multi-domain] Cd Length: 320 Bit Score: 305.59 E-value: 3.12e-103
PRTRC system protein D; A novel genetic system characterized by six major proteins, included a ...
7-327
3.12e-103
PRTRC system protein D; A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family is designated PRTRC system protein D. The gray zone, between trusted and noise, includes proteins found in the same genomes as other proteins of the PRTRC systems, but not in the same contiguous gene region.
Pssm-ID: 274757 [Multi-domain] Cd Length: 320 Bit Score: 305.59 E-value: 3.12e-103
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ...
7-322
3.65e-45
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: 156.67 E-value: 3.65e-45
Actin like proteins N terminal domain; This is the N-terminal domain found in archaeal actin ...
7-158
1.83e-22
Actin like proteins N terminal domain; This is the N-terminal domain found in archaeal actin homolog Ta0583 found in thermophilic archaeon Thermoplasma acidophilum. Structural analysis indicate that the fold of Ta0583 contains the core structure of actin indicating that it belongs to the actin/Hsp70 superfamily of ATPases. Furthermore,Ta0583 co-crystallized with ADP shows that the nucleotide binds at the interface between the subdomains of Ta0583 in a manner similar to that of actin. It has been suggested that Ta0583 might function in the cellular organization of T. acidophilum. Other family members include ParM another actin-like protein found in Staphylococcus aureus. Crystal structure co-ordinates revealed that this protein is most structurally related to the chromosomally encoded Actin-like proteins (Alp) Ta0583 from the archaea Thermoplasma acidophilum. Furthermore, biophysical analyses have suggested that ParM filaments undergo a treadmilling-like mechanism of motion in vitro similar to that of F-actin. The recruitment of ParM to the segrosome complex, was shown to be required for the conversion of static ParM filaments to a dynamic form proficient for active segregation and facilitated by the C-terminus of ParR
Pssm-ID: 465606 Cd Length: 149 Bit Score: 91.63 E-value: 1.83e-22
PRTRC system protein D; A novel genetic system characterized by six major proteins, included a ...
7-327
3.12e-103
PRTRC system protein D; A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. It is often found on plasmids. This protein family is designated PRTRC system protein D. The gray zone, between trusted and noise, includes proteins found in the same genomes as other proteins of the PRTRC systems, but not in the same contiguous gene region.
Pssm-ID: 274757 [Multi-domain] Cd Length: 320 Bit Score: 305.59 E-value: 3.12e-103
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ...
7-322
3.65e-45
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: 156.67 E-value: 3.65e-45
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
7-323
3.95e-28
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: 109.92 E-value: 3.95e-28
nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and ...
6-326
4.38e-27
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: 107.76 E-value: 4.38e-27
Actin like proteins N terminal domain; This is the N-terminal domain found in archaeal actin ...
7-158
1.83e-22
Actin like proteins N terminal domain; This is the N-terminal domain found in archaeal actin homolog Ta0583 found in thermophilic archaeon Thermoplasma acidophilum. Structural analysis indicate that the fold of Ta0583 contains the core structure of actin indicating that it belongs to the actin/Hsp70 superfamily of ATPases. Furthermore,Ta0583 co-crystallized with ADP shows that the nucleotide binds at the interface between the subdomains of Ta0583 in a manner similar to that of actin. It has been suggested that Ta0583 might function in the cellular organization of T. acidophilum. Other family members include ParM another actin-like protein found in Staphylococcus aureus. Crystal structure co-ordinates revealed that this protein is most structurally related to the chromosomally encoded Actin-like proteins (Alp) Ta0583 from the archaea Thermoplasma acidophilum. Furthermore, biophysical analyses have suggested that ParM filaments undergo a treadmilling-like mechanism of motion in vitro similar to that of F-actin. The recruitment of ParM to the segrosome complex, was shown to be required for the conversion of static ParM filaments to a dynamic form proficient for active segregation and facilitated by the C-terminus of ParR
Pssm-ID: 465606 Cd Length: 149 Bit Score: 91.63 E-value: 1.83e-22
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
7-322
7.53e-19
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: 85.79 E-value: 7.53e-19
nucleotide-binding domain (NBD) of Thermoplasma acidophilum archaeal actin homolog and similar ...
5-323
5.01e-13
nucleotide-binding domain (NBD) of Thermoplasma acidophilum archaeal actin homolog and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Thermoplasma acidophilum archaeal actin homolog Ta0583, which is the archaeal counterpart of the eukaryotic structural protein actin, such as MreB and ParM. Ta0583 could have a function in cellular organization. It polymerizes into bundles of filaments, forming a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm. Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction. Nucleoside diphosphate or AMP-PNP does not support polymerization.
Pssm-ID: 466877 [Multi-domain] Cd Length: 323 Bit Score: 68.80 E-value: 5.01e-13
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ...
89-323
2.29e-08
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Bacillus subtilis actin-like protein Alp7A, a plasmid partitioning protein that functions in plasmid segregation. The subfamily also includes Bacillus thuringiensis ParM hybrid fusion protein.
Pssm-ID: 466873 [Multi-domain] Cd Length: 368 Bit Score: 55.03 E-value: 2.29e-08
nucleotide-binding domain (NBD) of Bacillus subtilis plasmid segregating actin AlfA and ...
7-258
1.77e-03
nucleotide-binding domain (NBD) of Bacillus subtilis plasmid segregating actin AlfA and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Bacillus subtilis plasmid segregating actin AlfA that forms ATP-dependent filaments both in vivo and in vitro. Unlike ParM, AlfA forms stable filaments that remain assembled indefinitely in the ADP-bound state, and it is structurally polar but grows at equal rates from both ends. In addition, AlfA lacks the canonical actin subdomain IIb, which plays important structural and functional roles in all other actins. Also, AlfA polymerization interfaces have diverged extensively from other actins, and AlfA binds ATP through completely novel interactions with the adenosine base.
Pssm-ID: 466874 [Multi-domain] Cd Length: 264 Bit Score: 39.32 E-value: 1.77e-03
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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