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Conserved domains on  [gi|919220865|ref|WP_052773317|]
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MULTISPECIES: Fic family protein [Bifidobacterium]

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

Gene Ontology:  GO:0005524|GO:0000287|GO:0042803

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
57-398 8.05e-44

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 155.61  E-value: 8.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865  57 TSMLTEKILLAERRVSRLwNQIPGVMRwDYIRHSISEELFATNEMEGVRSTRKETQEAVEAADKARKDGDDPKaRFSEFA 136
Cdd:COG3177    1 TPELLKLLAEADEALGRL-DGLPEELR-ELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLTGGPPLRDER-EVLNYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 137 KLYLNLTDKDSALPAGIADIRDIYdKIVLDEINESDKPDGElFRKGDVEIQgphglAIHNGVKGEgNIGALLTDMIH-LA 215
Cdd:COG3177   78 EALEYLLELLRGEPLTEELILELH-RILLKGLRGEDKEPGE-YRTGQVGIG-----AVYVPPPPE-EVPELMEELLDwLN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 216 TSDEIPRLQSAIMSHFLFEYVHPFYDGNGRTGRYLLALYL-NHDLTMPTVLSLSRTIAENKNAYYKAFMEAEDKlncGEL 294
Cdd:COG3177  150 EEDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLlRAGLLSQPLLPLSRIIEEDRDEYYDALEAVRET---GDL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 295 TLFVNTILGFIRKAQDELIDELEvRVDQLDKGRavcdqlerkhgLSAKAVSILYGVIQEEMFdstksmTLNDAAYHIRLS 374
Cdd:COG3177  227 TPWIEFFLEAILEAAEEALALLE-RLLELARGR-----------LNERQRKLLELLFENPVL------TASELAELLGVS 288
                        330       340
                 ....*....|....*....|....*
gi 919220865 375 KQSARKYVGELMDAG-LAIQSGKRP 398
Cdd:COG3177  289 RRTARRDLKDLVELGiLEKVGGGRN 313
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
57-398 8.05e-44

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 155.61  E-value: 8.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865  57 TSMLTEKILLAERRVSRLwNQIPGVMRwDYIRHSISEELFATNEMEGVRSTRKETQEAVEAADKARKDGDDPKaRFSEFA 136
Cdd:COG3177    1 TPELLKLLAEADEALGRL-DGLPEELR-ELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLTGGPPLRDER-EVLNYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 137 KLYLNLTDKDSALPAGIADIRDIYdKIVLDEINESDKPDGElFRKGDVEIQgphglAIHNGVKGEgNIGALLTDMIH-LA 215
Cdd:COG3177   78 EALEYLLELLRGEPLTEELILELH-RILLKGLRGEDKEPGE-YRTGQVGIG-----AVYVPPPPE-EVPELMEELLDwLN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 216 TSDEIPRLQSAIMSHFLFEYVHPFYDGNGRTGRYLLALYL-NHDLTMPTVLSLSRTIAENKNAYYKAFMEAEDKlncGEL 294
Cdd:COG3177  150 EEDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLlRAGLLSQPLLPLSRIIEEDRDEYYDALEAVRET---GDL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 295 TLFVNTILGFIRKAQDELIDELEvRVDQLDKGRavcdqlerkhgLSAKAVSILYGVIQEEMFdstksmTLNDAAYHIRLS 374
Cdd:COG3177  227 TPWIEFFLEAILEAAEEALALLE-RLLELARGR-----------LNERQRKLLELLFENPVL------TASELAELLGVS 288
                        330       340
                 ....*....|....*....|....*
gi 919220865 375 KQSARKYVGELMDAG-LAIQSGKRP 398
Cdd:COG3177  289 RRTARRDLKDLVELGiLEKVGGGRN 313
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
153-255 6.08e-12

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: 61.71  E-value: 6.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865  153 IADIRDIYDKIVLDEINESDKPDGELFRKGDVEIQGPHglaihngvkgegNIGALLTDMIHLATSDEIPRLQSAIMSHFL 232
Cdd:pfam02661   4 LEDLLALHRLLIERHGGAGGARDVNVSGLLESALARPE------------QIPFGLEELLLYPDLDREHPLEKAAALHFG 71
                          90       100
                  ....*....|....*....|...
gi 919220865  233 FEYVHPFYDGNGRTGRYLLALYL 255
Cdd:pfam02661  72 FAKIHPFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
206-298 7.68e-03

mobile mystery protein B; Members of this protein family, which we designate mobile mystery protein B, are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein A (TIGR02612), a member of the family of helix-turn-helix DNA binding proteins (pfam01381). This protein is encoded by the downstream member of the gene pair and belongs to the Fic protein family (pfam02661), where Fic (filamentation induced by cAMP) is a regulator of cell division. The characteristics of having a two-gene operon in a varied context and often on plasmids, with one member affecting cell division and the other able to bind DNA, suggests similarity to addiction modules.


Pssm-ID: 131662  Cd Length: 186  Bit Score: 37.51  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865  206 ALLTDMIHLATSDEIPRLQSAIMSHFLFEYVHPFYDGNGRTGRYLLALYLNHDLTMP-TVLSLSRTIAENKNAYYKAFME 284
Cdd:TIGR02613  92 ILLDDVRYWLQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPfTWGSGSLALVGDLRKEYIAALK 171
                          90
                  ....*....|....
gi 919220865  285 AEDKLNCGELTLFV 298
Cdd:TIGR02613 172 AADRHDYGPLLEFA 185
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
57-398 8.05e-44

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 155.61  E-value: 8.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865  57 TSMLTEKILLAERRVSRLwNQIPGVMRwDYIRHSISEELFATNEMEGVRSTRKETQEAVEAADKARKDGDDPKaRFSEFA 136
Cdd:COG3177    1 TPELLKLLAEADEALGRL-DGLPEELR-ELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLTGGPPLRDER-EVLNYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 137 KLYLNLTDKDSALPAGIADIRDIYdKIVLDEINESDKPDGElFRKGDVEIQgphglAIHNGVKGEgNIGALLTDMIH-LA 215
Cdd:COG3177   78 EALEYLLELLRGEPLTEELILELH-RILLKGLRGEDKEPGE-YRTGQVGIG-----AVYVPPPPE-EVPELMEELLDwLN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 216 TSDEIPRLQSAIMSHFLFEYVHPFYDGNGRTGRYLLALYL-NHDLTMPTVLSLSRTIAENKNAYYKAFMEAEDKlncGEL 294
Cdd:COG3177  150 EEDELHPLIKAAIAHYQFETIHPFADGNGRTGRLLMNLLLlRAGLLSQPLLPLSRIIEEDRDEYYDALEAVRET---GDL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865 295 TLFVNTILGFIRKAQDELIDELEvRVDQLDKGRavcdqlerkhgLSAKAVSILYGVIQEEMFdstksmTLNDAAYHIRLS 374
Cdd:COG3177  227 TPWIEFFLEAILEAAEEALALLE-RLLELARGR-----------LNERQRKLLELLFENPVL------TASELAELLGVS 288
                        330       340
                 ....*....|....*....|....*
gi 919220865 375 KQSARKYVGELMDAG-LAIQSGKRP 398
Cdd:COG3177  289 RRTARRDLKDLVELGiLEKVGGGRN 313
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
153-255 6.08e-12

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: 61.71  E-value: 6.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865  153 IADIRDIYDKIVLDEINESDKPDGELFRKGDVEIQGPHglaihngvkgegNIGALLTDMIHLATSDEIPRLQSAIMSHFL 232
Cdd:pfam02661   4 LEDLLALHRLLIERHGGAGGARDVNVSGLLESALARPE------------QIPFGLEELLLYPDLDREHPLEKAAALHFG 71
                          90       100
                  ....*....|....*....|...
gi 919220865  233 FEYVHPFYDGNGRTGRYLLALYL 255
Cdd:pfam02661  72 FAKIHPFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
206-298 7.68e-03

mobile mystery protein B; Members of this protein family, which we designate mobile mystery protein B, are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein A (TIGR02612), a member of the family of helix-turn-helix DNA binding proteins (pfam01381). This protein is encoded by the downstream member of the gene pair and belongs to the Fic protein family (pfam02661), where Fic (filamentation induced by cAMP) is a regulator of cell division. The characteristics of having a two-gene operon in a varied context and often on plasmids, with one member affecting cell division and the other able to bind DNA, suggests similarity to addiction modules.


Pssm-ID: 131662  Cd Length: 186  Bit Score: 37.51  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919220865  206 ALLTDMIHLATSDEIPRLQSAIMSHFLFEYVHPFYDGNGRTGRYLLALYLNHDLTMP-TVLSLSRTIAENKNAYYKAFME 284
Cdd:TIGR02613  92 ILLDDVRYWLQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPfTWGSGSLALVGDLRKEYIAALK 171
                          90
                  ....*....|....
gi 919220865  285 AEDKLNCGELTLFV 298
Cdd:TIGR02613 172 AADRHDYGPLLEFA 185
 
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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