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Conserved domains on  [gi|2783282676|ref|WP_369021509|]
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Fic family protein [Verminephrobacter aporrectodeae]

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];
3-254 8.16e-69

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 214.93  E-value: 8.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676   3 SALDQRKAELDdcrPLPAvTAASLREKLALEWTYHSNAIEGNTLTLRETKVVLEGITVGGKTLREHFEAINHQEAIQFVE 82
Cdd:COG3177     9 AEADEALGRLD---GLPE-ELRELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLTGGPPLRDEREVLNYVEALEYLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  83 DLVgKSADINEWNIRNIHQLVLRNIA--SNEAGRYRRENVVItGSSTIPPDHVRLPEVMADLMAWYGADgQSLHPIERAA 160
Cdd:COG3177    85 ELL-RGEPLTEELILELHRILLKGLRgeDKEPGEYRTGQVGI-GAVYVPPPPEEVPELMEELLDWLNEE-DELHPLIKAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676 161 QLHTRFVGIHPFLDGNGRTGRLLLNFELMREG------FPPVIIRKEDRLAYYNALDKACATRDYEDITQMVAEGIARSL 234
Cdd:COG3177   162 IAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVRETGDLTPWIEFFLEAILEAA 241

                         250       260
                  ....*....|....*....|..
gi 2783282676 235 GTYLEVV--IGCKPDPLLDERA 254
Cdd:COG3177   242 EEALALLerLLELARGRLNERQ 263
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
3-254 8.16e-69

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 214.93  E-value: 8.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676   3 SALDQRKAELDdcrPLPAvTAASLREKLALEWTYHSNAIEGNTLTLRETKVVLEGITVGGKTLREHFEAINHQEAIQFVE 82
Cdd:COG3177     9 AEADEALGRLD---GLPE-ELRELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLTGGPPLRDEREVLNYVEALEYLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  83 DLVgKSADINEWNIRNIHQLVLRNIA--SNEAGRYRRENVVItGSSTIPPDHVRLPEVMADLMAWYGADgQSLHPIERAA 160
Cdd:COG3177    85 ELL-RGEPLTEELILELHRILLKGLRgeDKEPGEYRTGQVGI-GAVYVPPPPEEVPELMEELLDWLNEE-DELHPLIKAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676 161 QLHTRFVGIHPFLDGNGRTGRLLLNFELMREG------FPPVIIRKEDRLAYYNALDKACATRDYEDITQMVAEGIARSL 234
Cdd:COG3177   162 IAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVRETGDLTPWIEFFLEAILEAA 241

                         250       260
                  ....*....|....*....|..
gi 2783282676 235 GTYLEVV--IGCKPDPLLDERA 254
Cdd:COG3177   242 EEALALLerLLELARGRLNERQ 263
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 90-188 2.00e-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: 77.89  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  90 DINEWNIRNIHQLVlrnIASNEAGRYRRENVVITGSSTIPPDHVRLPEVMADLMAWYgaDGQSLHPIERAAQLHTRFVGI 169
Cdd:pfam02661   1 YLDLEDLLALHRLL---IERHGGAGGARDVNVSGLLESALARPEQIPFGLEELLLYP--DLDREHPLEKAAALHFGFAKI 75

                          90
                  ....*....|....*....
gi 2783282676 170 HPFLDGNGRTGRLLLNFEL 188
Cdd:pfam02661  76 HPFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 55-219 3.87e-09

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: 54.84  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  55 LEGITVGGKTLR---EHFEAINHQEAIQFVEDLVGKSADI-NEWNIRNIHQLVLRNIAsNEAGRYRR--ENVVITGSStI 128
Cdd:TIGR02613   9 LEGLLPGHITTRgelDEFEQANIAEGILWAEGRRRKKKDIlSETFLRRLHRRMFGDVW-RWAGDFRTtqKNIGVSPLQ-I 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676 129 PpdhVRLPEVMADLMAWygADGQSLHPIERAAQLHTRFVGIHPFLDGNGRTGRLLLNFELMREGFPPV------IIRKED 202
Cdd:TIGR02613  87 P---SELAILLDDVRYW--LQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPFtwgsgsLALVGD 161

                         170
                  ....*....|....*..
gi 2783282676 203 RLAYYNALDKACATRDY 219
Cdd:TIGR02613 162 LRKEYIAALKAADRHDY 178
PRK14052 PRK14052
adenosine monophosphate-protein transferase vopS;
161-204 1.27e-03

adenosine monophosphate-protein transferase vopS;


Pssm-ID: 184477 [Multi-domain]  Cd Length: 387  Bit Score: 39.55  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2783282676 161 QLHTRFVGIHPFLDGNGRTGRLLLNF-ELMREGFPPVIIRKEDRL 204
Cdd:PRK14052  339 QLFAGVIGYHGFTDGNGRMGRMLYAIaELRNDSFNPLAMNAENSL 383
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
3-254 8.16e-69

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 214.93  E-value: 8.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676   3 SALDQRKAELDdcrPLPAvTAASLREKLALEWTYHSNAIEGNTLTLRETKVVLEGITVGGKTLREHFEAINHQEAIQFVE 82
Cdd:COG3177     9 AEADEALGRLD---GLPE-ELRELLRKLLIEEAYASSAIEGNTLTLDEVRSLLEGGLTGGPPLRDEREVLNYVEALEYLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  83 DLVgKSADINEWNIRNIHQLVLRNIA--SNEAGRYRRENVVItGSSTIPPDHVRLPEVMADLMAWYGADgQSLHPIERAA 160
Cdd:COG3177    85 ELL-RGEPLTEELILELHRILLKGLRgeDKEPGEYRTGQVGI-GAVYVPPPPEEVPELMEELLDWLNEE-DELHPLIKAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676 161 QLHTRFVGIHPFLDGNGRTGRLLLNFELMREG------FPPVIIRKEDRLAYYNALDKACATRDYEDITQMVAEGIARSL 234
Cdd:COG3177   162 IAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVRETGDLTPWIEFFLEAILEAA 241

                         250       260
                  ....*....|....*....|..
gi 2783282676 235 GTYLEVV--IGCKPDPLLDERA 254
Cdd:COG3177   242 EEALALLerLLELARGRLNERQ 263
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
 90-188 2.00e-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: 77.89  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  90 DINEWNIRNIHQLVlrnIASNEAGRYRRENVVITGSSTIPPDHVRLPEVMADLMAWYgaDGQSLHPIERAAQLHTRFVGI 169
Cdd:pfam02661   1 YLDLEDLLALHRLL---IERHGGAGGARDVNVSGLLESALARPEQIPFGLEELLLYP--DLDREHPLEKAAALHFGFAKI 75

                          90
                  ....*....|....*....
gi 2783282676 170 HPFLDGNGRTGRLLLNFEL 188
Cdd:pfam02661  76 HPFRDGNGRTARLLANLFL 94
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
96-231 2.78e-13

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


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 66.49  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  96 IRNIHQLVLRNIASnEAGRYRRENVVITGSSTIPPDHVR--LPEVMADLMAWYGADGQSLHP-IERAAQLHTRFVGIHPF 172
Cdd:COG2184    56 LKAIHRRLFGDVYD-WAGQIRTVNISKGGTRFAPPSFIEreLEALFDDLREENYLRGLDREEfAERLARFHGELNVIHPF 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2783282676 173 LDGNGRTGRLLLNFELMREGFpPVIIRKEDRLAYYNALdKACATRDYEDITQMVAEGIA 231
Cdd:COG2184   135 REGNGRTQRLFFDQLARQAGY-PLDWSRVDKEEYLEAL-IAADNGDYSPLKALFRDALT 191
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
 55-219 3.87e-09

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: 54.84  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676  55 LEGITVGGKTLR---EHFEAINHQEAIQFVEDLVGKSADI-NEWNIRNIHQLVLRNIAsNEAGRYRR--ENVVITGSStI 128
Cdd:TIGR02613   9 LEGLLPGHITTRgelDEFEQANIAEGILWAEGRRRKKKDIlSETFLRRLHRRMFGDVW-RWAGDFRTtqKNIGVSPLQ-I 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2783282676 129 PpdhVRLPEVMADLMAWygADGQSLHPIERAAQLHTRFVGIHPFLDGNGRTGRLLLNFELMREGFPPV------IIRKED 202
Cdd:TIGR02613  87 P---SELAILLDDVRYW--LQNGTFSPDEIAIRFHHRLVAIHPFPNGNGRHARLATDLLLEQQGYSPFtwgsgsLALVGD 161

                         170
                  ....*....|....*..
gi 2783282676 203 RLAYYNALDKACATRDY 219
Cdd:TIGR02613 162 LRKEYIAALKAADRHDY 178
PRK14052 PRK14052
adenosine monophosphate-protein transferase vopS;
161-204 1.27e-03

adenosine monophosphate-protein transferase vopS;


Pssm-ID: 184477 [Multi-domain]  Cd Length: 387  Bit Score: 39.55  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2783282676 161 QLHTRFVGIHPFLDGNGRTGRLLLNF-ELMREGFPPVIIRKEDRL 204
Cdd:PRK14052  339 QLFAGVIGYHGFTDGNGRMGRMLYAIaELRNDSFNPLAMNAENSL 383
 
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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