NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
40-278
1.07e-107
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.
Pssm-ID: 427137 Cd Length: 239 Bit Score: 314.84 E-value: 1.07e-107
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
292-350
1.57e-12
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).
Pssm-ID: 212160 [Multi-domain] Cd Length: 58 Bit Score: 61.59 E-value: 1.57e-12
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
40-278
1.07e-107
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.
Pssm-ID: 427137 Cd Length: 239 Bit Score: 314.84 E-value: 1.07e-107
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
292-350
1.57e-12
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).
Pssm-ID: 212160 [Multi-domain] Cd Length: 58 Bit Score: 61.59 E-value: 1.57e-12
Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III ...
293-353
9.39e-10
Type III antifreeze protein, may be specific to the Zoarcoidei; Antifreeze protein III inhibits the growth of ice crystals and protects fish from cold damage in sub-freezing temperatures.
Pssm-ID: 212162 Cd Length: 62 Bit Score: 54.01 E-value: 9.39e-10
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
294-350
1.15e-05
SAF domain; This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins.
Pssm-ID: 430140 [Multi-domain] Cd Length: 63 Bit Score: 42.54 E-value: 1.15e-05
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus ...
295-350
3.68e-04
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus assembly CpaB; FlgA is a putative periplasmic chaperone that assists in the formation of the flagellar P ring; CpaB is a protein invoved in the assembly of the flp pili, which are bacterial virulence factors mediating non-specific adherence to surfaces; these proteins appear to contain a single SAF domain. This intermediate family also contains the SAF domains of sialic acid synthetases and type III antifreeze proteins, which also share the same extensive core structure.
Pssm-ID: 212159 [Multi-domain] Cd Length: 61 Bit Score: 38.22 E-value: 3.68e-04
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,
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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.
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(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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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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