ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
1-351
0e+00
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 cd24136:
Pssm-ID: 483947 [Multi-domain] Cd Length: 354 Bit Score: 620.86 E-value: 0e+00
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
1-351
0e+00
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK2.
Pssm-ID: 466986 [Multi-domain] Cd Length: 354 Bit Score: 620.86 E-value: 0e+00
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
1-347
8.74e-158
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit abnormalities in bipolar spindle organization, chromosome segregation, and contractile ring formation. Analyses have demonstrated that encodes three protein isoforms, all of which contain a domain with high similarity to the pantothenate kinases of A. nidulans and mouse. A role of fumble in membrane synthesis has been proposed.
Pssm-ID: 460995 [Multi-domain] Cd Length: 311 Bit Score: 444.63 E-value: 8.74e-158
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
1-350
4.54e-117
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of pantothenate kinase, characterized from the fungus Aspergillus nidulans and with similar forms known in several other eukaryotes. It also includes forms from several Gram-positive bacteria suggested to have originated from the eukaryotic form by lateral transfer. It differs in a number of biochemical properties (such as inhibition by acetyl-CoA) from most bacterial CoaA and lacks sequence similarity. This enzyme is the key regulatory step in the biosynthesis of coenzyme A (CoA). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 273135 [Multi-domain] Cd Length: 296 Bit Score: 340.92 E-value: 4.54e-117
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
1-351
0e+00
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK2.
Pssm-ID: 466986 [Multi-domain] Cd Length: 354 Bit Score: 620.86 E-value: 0e+00
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
1-349
0e+00
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK1.
Pssm-ID: 466985 [Multi-domain] Cd Length: 352 Bit Score: 600.83 E-value: 0e+00
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
1-349
0e+00
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK3.
Pssm-ID: 466987 [Multi-domain] Cd Length: 353 Bit Score: 553.84 E-value: 0e+00
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
1-349
0e+00
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The Pank1-like subfamily includes PanK1-3.
Pssm-ID: 466972 [Multi-domain] Cd Length: 303 Bit Score: 542.50 E-value: 0e+00
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
1-349
2.06e-165
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK-II that belongs 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: 466866 [Multi-domain] Cd Length: 299 Bit Score: 463.66 E-value: 2.06e-165
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
1-347
8.74e-158
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit abnormalities in bipolar spindle organization, chromosome segregation, and contractile ring formation. Analyses have demonstrated that encodes three protein isoforms, all of which contain a domain with high similarity to the pantothenate kinases of A. nidulans and mouse. A role of fumble in membrane synthesis has been proposed.
Pssm-ID: 460995 [Multi-domain] Cd Length: 311 Bit Score: 444.63 E-value: 8.74e-158
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
1-349
1.21e-129
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from eukaryotes; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from eukaryotes. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4.
Pssm-ID: 466936 [Multi-domain] Cd Length: 327 Bit Score: 373.92 E-value: 1.21e-129
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
1-350
4.54e-117
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of pantothenate kinase, characterized from the fungus Aspergillus nidulans and with similar forms known in several other eukaryotes. It also includes forms from several Gram-positive bacteria suggested to have originated from the eukaryotic form by lateral transfer. It differs in a number of biochemical properties (such as inhibition by acetyl-CoA) from most bacterial CoaA and lacks sequence similarity. This enzyme is the key regulatory step in the biosynthesis of coenzyme A (CoA). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 273135 [Multi-domain] Cd Length: 296 Bit Score: 340.92 E-value: 4.54e-117
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
1-349
1.19e-108
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK4, which is a putative bifunctional protein with a predicted amino-terminal pantothenate kinase (type II PanK) domain fused to a carboxy-terminal phosphatase domain. PanK4 homologs are found in animals, fungi, and plants. The human PanK4 kinase domain has catalytically-inactivating amino acid substitutions, thus it is characterized as a catalytically inactive pseudoPanK.
Pssm-ID: 466973 [Multi-domain] Cd Length: 339 Bit Score: 321.05 E-value: 1.19e-108
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
45-349
4.64e-50
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from bacteria; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from bacteria.
Pssm-ID: 466935 [Multi-domain] Cd Length: 262 Bit Score: 168.13 E-value: 4.64e-50
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
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
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(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
(CDART).
Modify your query to search against a different database and/or use advanced search options
