fic/DOC family protein [Staphylococcus aureus]
Fic family protein( domain architecture ID 11459786)
Fic (Filamentation induced by cAMP) family protein similar to Shewanella oneidensis adenosine monophosphate-protein transferase SoFic, which mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
COG3177 | COG3177 | Fic family protein [Transcription]; |
17-261 | 5.31e-32 | |||||
Fic family protein [Transcription]; : Pssm-ID: 442410 [Multi-domain] Cd Length: 316 Bit Score: 119.79 E-value: 5.31e-32
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Name | Accession | Description | Interval | E-value | |||||
COG3177 | COG3177 | Fic family protein [Transcription]; |
17-261 | 5.31e-32 | |||||
Fic family protein [Transcription]; Pssm-ID: 442410 [Multi-domain] Cd Length: 316 Bit Score: 119.79 E-value: 5.31e-32
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Fic | pfam02661 | Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ... |
17-121 | 3.12e-14 | |||||
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc.This domain forms complexes with Phd antitoxins containing pfam02604. Pssm-ID: 426907 Cd Length: 94 Bit Score: 66.72 E-value: 3.12e-14
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Name | Accession | Description | Interval | E-value | |||||
COG3177 | COG3177 | Fic family protein [Transcription]; |
17-261 | 5.31e-32 | |||||
Fic family protein [Transcription]; Pssm-ID: 442410 [Multi-domain] Cd Length: 316 Bit Score: 119.79 E-value: 5.31e-32
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Fic | pfam02661 | Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ... |
17-121 | 3.12e-14 | |||||
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc.This domain forms complexes with Phd antitoxins containing pfam02604. Pssm-ID: 426907 Cd Length: 94 Bit Score: 66.72 E-value: 3.12e-14
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FIDO | COG2184 | Fido, protein-threonine AMPylation domain [Signal transduction mechanisms]; |
79-165 | 2.01e-03 | |||||
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms]; Pssm-ID: 441787 [Multi-domain] Cd Length: 196 Bit Score: 38.37 E-value: 2.01e-03
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Blast search parameters | ||||
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