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Conserved domains on  [gi|1475413996|ref|WP_118779529|]
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Fic family protein [Corynebacterium sp. HMSC076G08]

Protein Classification

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
8-108 9.91e-28

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 104.38  E-value: 9.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475413996   8 PTGLRTIQNWIGgsnhtlfgAEFIPAPPRLVHDLVDDLCLYL-DGASHGALIQAAIAHAQFKTIHPFADGNGRVGRALIH 86
Cdd:COG3177   115 PGEYRTGQVGIG--------AVYVPPPPEEVPELMEELLDWLnEEDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMN 186

                          90       100
                  ....*....|....*....|..
gi 1475413996  87 GILLRREPTEYTILPVSLVLDT 108
Cdd:COG3177   187 LLLLRAGLLSQPLLPLSRIIEE 208
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
8-108 9.91e-28

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 104.38  E-value: 9.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475413996   8 PTGLRTIQNWIGgsnhtlfgAEFIPAPPRLVHDLVDDLCLYL-DGASHGALIQAAIAHAQFKTIHPFADGNGRVGRALIH 86
Cdd:COG3177   115 PGEYRTGQVGIG--------AVYVPPPPEEVPELMEELLDWLnEEDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMN 186

                          90       100
                  ....*....|....*....|..
gi 1475413996  87 GILLRREPTEYTILPVSLVLDT 108
Cdd:COG3177   187 LLLLRAGLLSQPLLPLSRIIEE 208
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 27-89 9.79e-18

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: 73.27  E-value: 9.79e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475413996  27 GAEFIPAPPRLVHDLVDDLCLYLDGASHGALIQAAIAHAQFKTIHPFADGNGRVGRALIHGIL 89
Cdd:pfam02661  32 LLESALARPEQIPFGLEELLLYPDLDREHPLEKAAALHFGFAKIHPFRDGNGRTARLLANLFL 94
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
8-108 9.91e-28

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 104.38  E-value: 9.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475413996   8 PTGLRTIQNWIGgsnhtlfgAEFIPAPPRLVHDLVDDLCLYL-DGASHGALIQAAIAHAQFKTIHPFADGNGRVGRALIH 86
Cdd:COG3177   115 PGEYRTGQVGIG--------AVYVPPPPEEVPELMEELLDWLnEEDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMN 186

                          90       100
                  ....*....|....*....|..
gi 1475413996  87 GILLRREPTEYTILPVSLVLDT 108
Cdd:COG3177   187 LLLLRAGLLSQPLLPLSRIIEE 208
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 27-89 9.79e-18

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: 73.27  E-value: 9.79e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475413996  27 GAEFIPAPPRLVHDLVDDLCLYLDGASHGALIQAAIAHAQFKTIHPFADGNGRVGRALIHGIL 89
Cdd:pfam02661  32 LLESALARPEQIPFGLEELLLYPDLDREHPLEKAAALHFGFAKIHPFRDGNGRTARLLANLFL 94
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
11-92 3.09e-07

Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 47.61  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475413996  11 LRTIQNWIGGsnhTLFG-AEFIPappRLVHDLVDDL--CLYLDGASHGALIQ-AAIAHAQFKTIHPFADGNGRVGRALIH 86
Cdd:COG2184    74 IRTVNISKGG---TRFApPSFIE---RELEALFDDLreENYLRGLDREEFAErLARFHGELNVIHPFREGNGRTQRLFFD 147


                  ....*.
gi 1475413996  87 gILLRR 92
Cdd:COG2184   148 -QLARQ 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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