MULTISPECIES: plasmid segregation protein ParM domain-containing protein [Enterobacteriaceae]
Protein Classification
acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)
acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| ASKHA_ATPase-like super family | cl49607 | ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
22-341 | 8.87e-145 | ||||||
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 pfam06406: Pssm-ID: 483947 [Multi-domain] Cd Length: 317 Bit Score: 411.45 E-value: 8.87e-145
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| Name | Accession | Description | Interval | E-value | ||||||
| StbA | pfam06406 | StbA protein; This family consists of several bacterial StbA plasmid stability proteins. |
22-341 | 8.87e-145 | ||||||
StbA protein; This family consists of several bacterial StbA plasmid stability proteins. Pssm-ID: 310773 [Multi-domain] Cd Length: 317 Bit Score: 411.45 E-value: 8.87e-145
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| ASKHA_NBD_ParM_R1-like | cd24022 | nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
24-339 | 1.52e-80 | ||||||
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: 248.34 E-value: 1.52e-80
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| PRK13917 | PRK13917 | plasmid segregation protein ParM; Provisional |
148-333 | 4.35e-03 | ||||||
plasmid segregation protein ParM; Provisional Pssm-ID: 184393 [Multi-domain] Cd Length: 344 Bit Score: 38.72 E-value: 4.35e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| StbA | pfam06406 | StbA protein; This family consists of several bacterial StbA plasmid stability proteins. |
22-341 | 8.87e-145 | ||||||
StbA protein; This family consists of several bacterial StbA plasmid stability proteins. Pssm-ID: 310773 [Multi-domain] Cd Length: 317 Bit Score: 411.45 E-value: 8.87e-145
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| ASKHA_NBD_ParM_R1-like | cd24022 | nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
24-339 | 1.52e-80 | ||||||
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: 248.34 E-value: 1.52e-80
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| ASKHA_NBD_ParM-like | cd10227 | nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
24-333 | 7.20e-18 | ||||||
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: 82.18 E-value: 7.20e-18
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| ASKHA_NBD_ParM_Psk41-like | cd24021 | nucleotide-binding domain (NBD) of Staphylococcus aureus pSK41 actin-like ParM protein and ... |
135-333 | 2.72e-14 | ||||||
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: 72.32 E-value: 2.72e-14
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| ASKHA_NBD_ParM_pCBH-like | cd24025 | nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ... |
114-333 | 3.31e-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: 63.45 E-value: 3.31e-11
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| ASKHA_NBD_ParM_Alp12-like | cd24026 | nucleotide-binding domain (NBD) of Clostridium tetani actin-like protein Alp12 and similar ... |
24-333 | 7.49e-10 | ||||||
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: 59.22 E-value: 7.49e-10
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| ASKHA_NBD_HSP70_HSPA12 | cd10229 | nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
175-333 | 4.75e-06 | ||||||
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B. Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 48.04 E-value: 4.75e-06
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| ASKHA_NBD_HSP70 | cd10170 | nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
194-339 | 1.64e-05 | ||||||
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 45.94 E-value: 1.64e-05
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| ASKHA_NBD_ParM_Alp7A-like | cd24023 | nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ... |
158-330 | 8.66e-05 | ||||||
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: 43.86 E-value: 8.66e-05
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| PRK13917 | PRK13917 | plasmid segregation protein ParM; Provisional |
148-333 | 4.35e-03 | ||||||
plasmid segregation protein ParM; Provisional Pssm-ID: 184393 [Multi-domain] Cd Length: 344 Bit Score: 38.72 E-value: 4.35e-03
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