MULTISPECIES: cyclic di-AMP binding protein CbpA [Lactobacillus]
CBS domain-containing protein( domain architecture ID 17609527)
CBS (cystathione beta synthase) domain-containing protein; CBS domains may act as regulatory units
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
CBS_CbpA | NF038387 | cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ... |
1-213 | 3.91e-140 | ||||
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain. : Pssm-ID: 439679 Cd Length: 209 Bit Score: 390.83 E-value: 3.91e-140
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Name | Accession | Description | Interval | E-value | ||||
CBS_CbpA | NF038387 | cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ... |
1-213 | 3.91e-140 | ||||
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain. Pssm-ID: 439679 Cd Length: 209 Bit Score: 390.83 E-value: 3.91e-140
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CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
13-120 | 9.64e-12 | ||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 59.95 E-value: 9.64e-12
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CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
1-119 | 1.24e-10 | ||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 57.18 E-value: 1.24e-10
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PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
5-56 | 8.32e-04 | ||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 40.20 E-value: 8.32e-04
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CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
13-46 | 1.75e-03 | ||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 35.65 E-value: 1.75e-03
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Name | Accession | Description | Interval | E-value | ||||
CBS_CbpA | NF038387 | cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria ... |
1-213 | 3.91e-140 | ||||
cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain. Pssm-ID: 439679 Cd Length: 209 Bit Score: 390.83 E-value: 3.91e-140
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CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
13-120 | 9.64e-12 | ||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 59.95 E-value: 9.64e-12
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CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
1-119 | 1.24e-10 | ||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 57.18 E-value: 1.24e-10
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COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
1-127 | 2.35e-10 | ||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 56.80 E-value: 2.35e-10
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COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
1-122 | 6.31e-08 | ||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 51.42 E-value: 6.31e-08
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YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
1-116 | 2.24e-04 | ||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 39.90 E-value: 2.24e-04
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PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
5-56 | 8.32e-04 | ||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 40.20 E-value: 8.32e-04
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CBS_pair_bac | cd04643 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
5-119 | 9.12e-04 | ||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341400 [Multi-domain] Cd Length: 130 Bit Score: 38.25 E-value: 9.12e-04
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CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
13-46 | 1.75e-03 | ||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 35.65 E-value: 1.75e-03
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Blast search parameters | ||||
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