aminoglycoside phosphotransferase family protein inactivates its antibiotic substrate by phosphorylation, similar to streptomycin 6-kinase that catalyzes the phosphorylation of streptomycin to form streptomycin 6-phosphate
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside ...
3-240
3.52e-72
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation utilizing ATP. Likewise hydroxyurea is inactivated by phosphorylation of the hydroxy group in the hydroxylamine moiety.
Pssm-ID: 398368 [Multi-domain] Cd Length: 250 Bit Score: 221.33 E-value: 3.52e-72
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
65-166
9.01e-03
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270702 [Multi-domain] Cd Length: 300 Bit Score: 36.85 E-value: 9.01e-03
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside ...
3-240
3.52e-72
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation utilizing ATP. Likewise hydroxyurea is inactivated by phosphorylation of the hydroxy group in the hydroxylamine moiety.
Pssm-ID: 398368 [Multi-domain] Cd Length: 250 Bit Score: 221.33 E-value: 3.52e-72
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
65-172
1.81e-03
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 441905 [Multi-domain] Cd Length: 297 Bit Score: 39.14 E-value: 1.81e-03
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
65-166
9.01e-03
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270702 [Multi-domain] Cd Length: 300 Bit Score: 36.85 E-value: 9.01e-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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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.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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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.
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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)
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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,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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the domain superfamily to which the specific and non-specific hits belong
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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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