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.

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                  ....*....|....*....|....*....|....*....|
gi 1187953341  20 KWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:cd10221    69 KYPIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTE 108

nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.

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                  ....*....|....*....|....*....|....*....|
gi 1187953341  20 KWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:cd10221    69 KYPIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTE 108

Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily

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                   ....*....|....*....|....*....|....*....|
gi 1187953341   20 KWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:smart00268  63 KYPIENGIVENWDDMEKIWDYTFFNELRVEPEEHPVLLTE 102

nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.

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                  ....*....|....*....|....*....|....*....|
gi 1187953341  20 KWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:cd10221    69 KYPIRHGIVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTE 108

Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily

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                   ....*....|....*....|....*....|....*....|
gi 1187953341   20 KWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:smart00268  63 KYPIENGIVENWDDMEKIWDYTFFNELRVEPEEHPVLLTE 102

nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar proteins; The family includes actin and human actin-related proteins T1, T2, and T3. Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Arp-T1, encoded by ACTRT1/ARPT1 gene expressed in testis, negatively regulates the Hedgehog (SHH) signaling, binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. Arp-T2 (also called actin-related protein M2; encoded by ACTRT2/ARPM2 gene expressed in testis and various other cell types) and Arp-T3 (also called actin-related protein M1; encoded by ACTRT3/ARPM1 gene expressed in all tested human tissues) play general roles in the organization of the cytoskeleton like other cytoplasmic actin-related proteins.

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                  ....*....|....*....|....*....|....*....|
gi 1187953341  20 KWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:cd13397    63 SYPIEHGIVTNWDDMEKIWHHTFENELRVKPEEHPVLLTE 102

nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Actin is a monomeric globular protein (G-actin) that reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. At low salt concentrations, actin exists as a monomer, and as the salt concentration rises F-actin forms, with the consequent hydrolysis of ATP. F-actin assembly is in constant flux with G-actin association occurring at the barbed end (+) and its disassociation at the pointed end (-). Actin monomers that have been released from the pointed end can be reused, if the ADP is exchanged for ATP. F-actin filaments can assemble into higher order structures, for example branched F-actin, and stress fibers. Actin binding proteins regulate actin filament dynamics by a range of functions including actin severing, depolymerizing, capping, stabilizing and de novo actin polymerization. Actins interaction with myosin is the basis of muscular contraction and many aspects of cell motility. In vertebrates there are three main groups of actin isoforms, alpha, beta and gamma. The alpha actins found in muscle tissues are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. In plants there are many isoforms which are probably involved in a variety of functions such as cytoplasmic streaming, cell shape determination, tip growth, graviperception, cell wall deposition, etc.

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                  ....*....|....*....|....*....|....*....|
gi 1187953341  20 KWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:cd10224    63 KYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTE 102

nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, also called centractin, actin-like protein, alpha-centractin, actin-RPV, or centrosome-associated actin homolog, may be a component of a multi-subunit centrosomal complex involved in microtubule-based vesicle motility. In yeast, actin-related protein is essential for viability and is associated with the centrosome. In vertebrates, Arp1 is a core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. It is required for proper orientation of the mitotic spindle. Arp1 is the only actin-related protein known to form actin-like filaments. Human Arp1/centractin is encoded by the ACTR1A gene.

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                  ....*....|....*....|....*....|....*....|....*.
gi 1187953341  20 KWPIRHGIIEDWDLMERfmeqvVFKY------LRAEPEDHYFLMVE 59
Cdd:cd10216    64 RYPMEHGIVTDWNDMER-----IWQYvysklqLNTFSEEHPVLLTE 104

nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ubiquitous in eukaryotes, and the major component of the actin cytoskeleton; monomeric globular protein (G-actin) reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. F-actin filaments form with the consequent hydrolysis of ATP. Some actin-related proteins (Arps) have roles in cytoskeletal functions, such as actin polymerization (Arp2/3) and dynein motor activity (Arp1). Both conventional actin and specific Arps have been implicated in chromatin remodeling and/or transcription regulation. The actin/ARP 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.

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gi 1187953341  27 IIEDWDLMERFMEQVVFKYLRAEPEDHYFLMVE 59
Cdd:cd10169    22 LIFPWDDMEKIWEHVFYNLLRVDPEEHPVLLTE 54

actin-like protein; Provisional

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                  ....*....|....*....|....*....|....*....
gi 1187953341  21 WPIRHGIIEDWDLMERFMEQvVFKYLRAEPEDHYFLMVE 59
Cdd:PTZ00466   76 YPINHGIIENWNDMENIWIH-VYNSMKINSEEHPVLLTE 113