phage antirepressor KilAC domain-containing protein, partial [Anaerococcus lactolyticus]
KilAC family protein( domain architecture ID 10007652)
KilAC family protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
KilAC | COG3645 | Phage antirepressor protein YoqD, KilAC domain [Mobilome: prophages, transposons]; |
2-207 | 2.06e-34 | ||||
Phage antirepressor protein YoqD, KilAC domain [Mobilome: prophages, transposons]; : Pssm-ID: 442862 [Multi-domain] Cd Length: 249 Bit Score: 122.48 E-value: 2.06e-34
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Name | Accession | Description | Interval | E-value | ||||
KilAC | COG3645 | Phage antirepressor protein YoqD, KilAC domain [Mobilome: prophages, transposons]; |
2-207 | 2.06e-34 | ||||
Phage antirepressor protein YoqD, KilAC domain [Mobilome: prophages, transposons]; Pssm-ID: 442862 [Multi-domain] Cd Length: 249 Bit Score: 122.48 E-value: 2.06e-34
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ANT | pfam03374 | Phage antirepressor protein KilAC domain; This domain was called the KilAC domain by Iyer and ... |
103-202 | 6.35e-27 | ||||
Phage antirepressor protein KilAC domain; This domain was called the KilAC domain by Iyer and colleagues. Pssm-ID: 460903 Cd Length: 105 Bit Score: 98.80 E-value: 6.35e-27
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Bro-N | smart01040 | BRO family, N-terminal domain; This family includes the N-terminus of baculovirus BRO and ALI ... |
1-64 | 1.21e-22 | ||||
BRO family, N-terminal domain; This family includes the N-terminus of baculovirus BRO and ALI motif proteins. The function of BRO proteins is unknown. It has been suggested that BRO-A and BRO-C are DNA binding proteins that influence host DNA replication and/or transcription. This Pfam domain does not include the characteristic invariant alanine, leucine, isoleucine motif of the ALI proteins. Pssm-ID: 214989 Cd Length: 89 Bit Score: 87.24 E-value: 1.21e-22
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8prop_hemeD1_NirF | cd20778 | eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
66-204 | 1.38e-03 | ||||
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC. Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 38.80 E-value: 1.38e-03
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Name | Accession | Description | Interval | E-value | ||||
KilAC | COG3645 | Phage antirepressor protein YoqD, KilAC domain [Mobilome: prophages, transposons]; |
2-207 | 2.06e-34 | ||||
Phage antirepressor protein YoqD, KilAC domain [Mobilome: prophages, transposons]; Pssm-ID: 442862 [Multi-domain] Cd Length: 249 Bit Score: 122.48 E-value: 2.06e-34
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COG3617 | COG3617 | Prophage antirepressor [Mobilome: prophages, transposons]; |
1-71 | 3.20e-33 | ||||
Prophage antirepressor [Mobilome: prophages, transposons]; Pssm-ID: 442835 Cd Length: 106 Bit Score: 114.99 E-value: 3.20e-33
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ANT | pfam03374 | Phage antirepressor protein KilAC domain; This domain was called the KilAC domain by Iyer and ... |
103-202 | 6.35e-27 | ||||
Phage antirepressor protein KilAC domain; This domain was called the KilAC domain by Iyer and colleagues. Pssm-ID: 460903 Cd Length: 105 Bit Score: 98.80 E-value: 6.35e-27
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Bro-N | smart01040 | BRO family, N-terminal domain; This family includes the N-terminus of baculovirus BRO and ALI ... |
1-64 | 1.21e-22 | ||||
BRO family, N-terminal domain; This family includes the N-terminus of baculovirus BRO and ALI motif proteins. The function of BRO proteins is unknown. It has been suggested that BRO-A and BRO-C are DNA binding proteins that influence host DNA replication and/or transcription. This Pfam domain does not include the characteristic invariant alanine, leucine, isoleucine motif of the ALI proteins. Pssm-ID: 214989 Cd Length: 89 Bit Score: 87.24 E-value: 1.21e-22
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Bro-N | pfam02498 | BRO family, N-terminal domain; This family includes the N-terminus of baculovirus BRO and ALI ... |
1-64 | 9.83e-19 | ||||
BRO family, N-terminal domain; This family includes the N-terminus of baculovirus BRO and ALI motif proteins. The function of BRO proteins is unknown. It has been suggested that BRO-A and BRO-C are DNA binding proteins that influence host DNA replication and/or transcription. This Pfam domain does not include the characteriztic invariant alanine, leucine, isoleucine motif of the ALI proteins. Pssm-ID: 376797 Cd Length: 96 Bit Score: 77.40 E-value: 9.83e-19
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8prop_hemeD1_NirF | cd20778 | eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
66-204 | 1.38e-03 | ||||
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC. Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 38.80 E-value: 1.38e-03
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Blast search parameters | ||||
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