ArgK/MeaB family GTPase such as human mitochondrial methylmalonic aciduria type A protein, mycobacterial methylmalonyl Co-A mutase-associated GTPase MeaB, and Escherichia coli GTPase ArgK
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
17-323
2.43e-176
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of two transporter system periplasmic binding proteins and consequently inhibits those transporters. This kinase is also found in Gram-positive bacteria, archaea, and the roundworm C. elegans. It may have a more general, but still unknown function. Mutations have also been found that do not phosphorylate the periplasmic binding proteins, yet still allow transport. The ATPase activity of this protein seems to be necessary, however. [Transport and binding proteins, Amino acids, peptides and amines, Regulatory functions, Protein interactions]
Pssm-ID: 129833 [Multi-domain] Cd Length: 300 Bit Score: 490.05 E-value: 2.43e-176
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
22-294
4.24e-159
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.
Pssm-ID: 281323 [Multi-domain] Cd Length: 272 Bit Score: 445.34 E-value: 4.24e-159
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.
Pssm-ID: 349768 Cd Length: 252 Bit Score: 409.65 E-value: 3.22e-145
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
57-214
2.18e-03
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 2.18e-03
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
17-323
2.43e-176
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of two transporter system periplasmic binding proteins and consequently inhibits those transporters. This kinase is also found in Gram-positive bacteria, archaea, and the roundworm C. elegans. It may have a more general, but still unknown function. Mutations have also been found that do not phosphorylate the periplasmic binding proteins, yet still allow transport. The ATPase activity of this protein seems to be necessary, however. [Transport and binding proteins, Amino acids, peptides and amines, Regulatory functions, Protein interactions]
Pssm-ID: 129833 [Multi-domain] Cd Length: 300 Bit Score: 490.05 E-value: 2.43e-176
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
22-294
4.24e-159
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.
Pssm-ID: 281323 [Multi-domain] Cd Length: 272 Bit Score: 445.34 E-value: 4.24e-159
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.
Pssm-ID: 349768 Cd Length: 252 Bit Score: 409.65 E-value: 3.22e-145
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
56-201
2.39e-06
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 45.50 E-value: 2.39e-06
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
64-209
2.11e-04
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 41.95 E-value: 2.11e-04
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
57-214
2.18e-03
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 2.18e-03
hydrogenase accessory protein HypB; A GTP hydrolase for assembly of nickel metallocenter of ...
61-203
4.31e-03
hydrogenase accessory protein HypB; A GTP hydrolase for assembly of nickel metallocenter of hydrogenase. A similar protein, ureG, is an accessory protein for urease, which also uses nickel. hits scoring 75 and above are safe as orthologs. [SS 1/05/04 I changed the role_ID and process GO from protein folding to to protein modification, since a protein folding role has not been established, but HypB is implicated in insertion of nickel into the large subunit of NiFe hydrogenases.] [Protein fate, Protein modification and repair]
Pssm-ID: 272891 Cd Length: 208 Bit Score: 37.76 E-value: 4.31e-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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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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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
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Domains are color coded according to superfamilies
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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
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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
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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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