BppU family phage baseplate upper protein [Staphylococcus aureus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
BppU_N | pfam10651 | BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also ... |
9-152 | 6.66e-32 | |||
BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also known as ORF48) which is found in phage from a number of different bacteria. The N-terminal domain exhibits a beta-sandwich immunoglobulin fold. : Pssm-ID: 431419 Cd Length: 141 Bit Score: 118.97 E-value: 6.66e-32
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pyocin_knob | cd19958 | knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly ... |
286-338 | 3.54e-04 | |||
knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly repeated structural domain in R-type pyocins, which are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. R-type pyocins are structurally similar to simple contractile tails, such as those of phage P2 and Mu, and they punch a hole in the bacterial envelope to efficiently kill target cells. The second knob domain may contain regions responsible for determining the killing spectrum. Knob-like domains occur in host-recognition and binding proteins of, not only pyocins, but also phages, such as in phage K1F endosialidase (not represented by this model), where it may interact with sialic acid, the cell surface molecule that is recognized during infection. : Pssm-ID: 410997 [Multi-domain] Cd Length: 80 Bit Score: 39.24 E-value: 3.54e-04
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CPSase_L_D3 super family | cl47772 | Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
136-186 | 2.75e-03 | |||
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The actual alignment was detected with superfamily member pfam02787: Pssm-ID: 460695 Cd Length: 79 Bit Score: 36.59 E-value: 2.75e-03
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Name | Accession | Description | Interval | E-value | |||
BppU_N | pfam10651 | BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also ... |
9-152 | 6.66e-32 | |||
BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also known as ORF48) which is found in phage from a number of different bacteria. The N-terminal domain exhibits a beta-sandwich immunoglobulin fold. Pssm-ID: 431419 Cd Length: 141 Bit Score: 118.97 E-value: 6.66e-32
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pyocin_knob | cd19958 | knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly ... |
286-338 | 3.54e-04 | |||
knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly repeated structural domain in R-type pyocins, which are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. R-type pyocins are structurally similar to simple contractile tails, such as those of phage P2 and Mu, and they punch a hole in the bacterial envelope to efficiently kill target cells. The second knob domain may contain regions responsible for determining the killing spectrum. Knob-like domains occur in host-recognition and binding proteins of, not only pyocins, but also phages, such as in phage K1F endosialidase (not represented by this model), where it may interact with sialic acid, the cell surface molecule that is recognized during infection. Pssm-ID: 410997 [Multi-domain] Cd Length: 80 Bit Score: 39.24 E-value: 3.54e-04
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CPSase_L_D3 | pfam02787 | Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
136-186 | 2.75e-03 | |||
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. Pssm-ID: 460695 Cd Length: 79 Bit Score: 36.59 E-value: 2.75e-03
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Name | Accession | Description | Interval | E-value | |||
BppU_N | pfam10651 | BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also ... |
9-152 | 6.66e-32 | |||
BppU N-terminal domain; This is the N-terminal domain of baseplate upper proteins (BppU, also known as ORF48) which is found in phage from a number of different bacteria. The N-terminal domain exhibits a beta-sandwich immunoglobulin fold. Pssm-ID: 431419 Cd Length: 141 Bit Score: 118.97 E-value: 6.66e-32
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pyocin_knob | cd19958 | knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly ... |
286-338 | 3.54e-04 | |||
knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly repeated structural domain in R-type pyocins, which are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. R-type pyocins are structurally similar to simple contractile tails, such as those of phage P2 and Mu, and they punch a hole in the bacterial envelope to efficiently kill target cells. The second knob domain may contain regions responsible for determining the killing spectrum. Knob-like domains occur in host-recognition and binding proteins of, not only pyocins, but also phages, such as in phage K1F endosialidase (not represented by this model), where it may interact with sialic acid, the cell surface molecule that is recognized during infection. Pssm-ID: 410997 [Multi-domain] Cd Length: 80 Bit Score: 39.24 E-value: 3.54e-04
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CPSase_L_D3 | pfam02787 | Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
136-186 | 2.75e-03 | |||
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. Pssm-ID: 460695 Cd Length: 79 Bit Score: 36.59 E-value: 2.75e-03
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Blast search parameters | ||||
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